E.coli K-12 (MG1655) Exportome

UniProt Name:
D-alanyl-D-alanine carboxypeptidase DacC (DD-carboxypeptidase) (DD-peptidase) (EC 3.4.16.4) (Penicillin-binding protein 6) (PBP-6)
Localization:
Peripheral inner membrane protein facing the periplasm
Notes:
Putative amphiphilic alpha-helical anchor at the C-terminusPMID: 8162192. PMID: 9858669 DacC(PBP-6) anchors to the periplasmic face of the inner membrane via C-terminal amphiphilic alpha-helix. The Alpha-helical conformation in the C-terminal anchoring domain is observed in aqueous solution or in the presence of phospholipid vesicles. PMID: 9371419
References:
PMID: 8162192 PMID: 9371419 PMID: 9858669
Pseudogene/Mobile Element:
-

mRNA molec/cell:
-

Proteomics:
PMID: 16606699 PMID: 12624733 PMID: 12488465 PMID: 19348461 PMID: 20222674 PMID: 16967446 PMID: 19767571 PMID: 15115803 PMID: 20932056 PMID: 18796603
Proteomics / Inner Membrane fraction:
PMID: 17446557 PMID: 17309111

Protein molec/cell:
-
PaxDb:
249 ppm

Class:
Multi-domain proteins (alpha and beta)
SCOP: 56572
Fold:
Penicillin-binding protein associated domain SCOP: 69188
Super Family:
beta-lactamase/transpeptidase-like
SCOP: 56601
Penicillin-binding protein associated domain
SCOP: 69189

Go to Complexes

UniProt Name:
Flagellar hook-basal body complex protein FliE
Localization:
Peripheral inner membrane protein facing the periplasm
Notes:
MS-ring rod junction protein
References:
PMID: 10809679
Pseudogene/Mobile Element:
-

mRNA molec/cell:
-

Proteomics:
PMID: 19767571
Proteomics / Inner Membrane fraction:
-

Protein molec/cell:
-
PaxDb:
0.052 ppm

Class:
-
Fold:
-
Super Family:
-

Go to Complexes

UniProt Name:
Probable anaerobic dimethyl sulfoxide reductase chain YnfG (DMSO reductase iron-sulfur subunit YnfG)
Localization:
Peripheral inner membrane protein facing the periplasm
Notes:
The physiological substrate and relevance of the YnfFGH S- and N-oxide reductase is unknown. DmsB paralog. So far, hydroxy pyridine N-oxide is the best substrate for YnfFGH. ynfFGH are expressed anaerobically. YnfG can function with DmsAC, replacing DmsB a as the electron transfer subunit. The ynfEFGHI operon is a paralogue of the Escherichia coli dmsABC operon. ynfE and ynfF are paralogues of dmsA. ynfG and ynfH are paralogues of dmsB and dmsC, respectively. PMID: 14522592
References:
PMID: 14522592
Pseudogene/Mobile Element:
-

mRNA molec/cell:
-

Proteomics:
PMID: 16606699 PMID: 20222674
Proteomics / Inner Membrane fraction:
-

Protein molec/cell:
-
PaxDb:
7.71 ppm

Class:
Alpha and beta proteins (a+b)
SCOP: 53931
Fold:
Ferredoxin-like SCOP: 54861
Super Family:
4Fe-4S ferredoxins
SCOP: 54862

Go to Complexes

UniProt Name:
Hydrogenase-2 operon protein HybA
Localization:
Peripheral inner membrane protein facing the periplasm
Notes:
TAT secretion system. Part of membrane-associated hydrogenase 4 complex. PMID: 9738917
References:
PMID: 15911532 PMID: 21890895 PMID: 22313414 PMID: 9738917
Pseudogene/Mobile Element:
-

mRNA molec/cell:
-

Proteomics:
PMID: 16606699 PMID: 12624733 PMID: 19348461 PMID: 20222674 PMID: 19767571
Proteomics / Inner Membrane fraction:
-

Protein molec/cell:
-
PaxDb:
12.4 ppm

Class:
Alpha and beta proteins (a+b)
SCOP: 53931
Fold:
Ferredoxin-like SCOP: 54861
Super Family:
4Fe-4S ferredoxins
SCOP: 54862

Go to Complexes

UniProt Name:
Hydrogenase-2 large chain (HYD2) (EC 1.12.99.6) (Membrane-bound hydrogenase 2 large subunit) (NiFe hydrogenase)
Localization:
Peripheral inner membrane protein facing the periplasm
Notes:
The protein is attached to this location through a 5kDa segment of its small subunit hybO that is has a TAT signal peptide. Secreted using the TAT system (piggyback). PMID: 10224080 An active tryptic fragment of membrane-bound hydrogenase isoenzyme 2 from anaerobically grown Escherichia coli has been purified. This indicates that HYD2 is attached to the periplasmic side of the cytoplasmic membrane.PMID: 3516690 The intracellular availability of nickel is essential for the processing of the large subunit and for the transmembrane translocation of HYD2. PMID: 8772179 PMID: 9738917 Disulfide bond-containing protein PMID: 25664544
References:
PMID: 10224080 PMID: 25664544 PMID: 3516690 PMID: 8772179 PMID: 9738917
Pseudogene/Mobile Element:
-

mRNA molec/cell:
-

Proteomics:
PMID: 16606699 PMID: 12624733 PMID: 12488465 PMID: 19348461 PMID: 20222674 PMID: 16967446 PMID: 16858726 PMID: 19767571 PMID: 15919657 PMID: 15115803 PMID: 20932056
Proteomics / Inner Membrane fraction:
PMID: 15919657 PMID: 17309111

Protein molec/cell:
-
PaxDb:
60.5 ppm

Class:
Multi-domain proteins (alpha and beta)
SCOP: 56572
Fold:
HydB/Nqo4-like
SCOP: 56761
Super Family:
HydB/Nqo4-like
SCOP: 56762

Go to Complexes

UniProt Name:
Periplasmic protein CpxP (ORF_o167) (Periplasmic accessory protein CpxP)
Localization:
Peripheral inner membrane protein facing the periplasm
Notes:
-
References:
PMID: 10972835 PMID: 17904518 PMID: 21317318
Pseudogene/Mobile Element:
pseudogene (Ochman & Davalos, 2006)

mRNA molec/cell:
-

Proteomics:
PMID: 16606699 PMID: 12488465 PMID: 20222674 PMID: 20803007
Proteomics / Inner Membrane fraction:
-

Protein molec/cell:
-
PaxDb:
0 ppm

Class:
-
Fold:
-
Super Family:
-

Go to Complexes

UniProt Name:
D-alanyl-D-alanine carboxypeptidase DacA (DD-carboxypeptidase) (DD-peptidase) (EC 3.4.16.4) (Beta-lactamase) (EC 3.5.2.6) (Penicillin-binding protein 5) (PBP-5)
Localization:
Peripheral inner membrane protein facing the periplasm
Notes:
Anchored to inner membrane by C-terminal tailPMID: 2194801. Using natural isotope abundance NMR, the structure of the PBP 5 anchor peptide within a micelle was determinedPMID: 20192190. The structure conforms to a helix-bend-helix-turn-helix motif and reveals that the anchor enters the membrane so as to form an amphiphilic structure within the interface of the hydrophilic/hydrophobic boundary regions near the lipid head groups. PBP-5 deletion mutants exhibit irregular distribution of MreB at the deformed zones PMID: 20545860. PMID: 3279397 PMID: 8424800 DacA(PBP-5) anchors to the periplasmic face of the inner membrane via C-terminal amphiphilic alpha-helix. The Alpha-helical conformation in the C-terminal anchoring domain is observed in aqueous solution or in the presence of phospholipid vesicles. A pH dependent loss of alpha-helical conformation in the peptide corresponding to the PBP5 C-terminus was found to correlate with the susceptibility of PBP5 to membrane extraction. PMID: 9371419
References:
PMID: 20192190 PMID: 20545860 PMID: 2194801 PMID: 24057063 PMID: 3279397 PMID: 8424800 PMID: 9371419
Pseudogene/Mobile Element:
-

mRNA molec/cell:
3

Proteomics:
PMID: 16606699 PMID: 12624733 PMID: 12488465 PMID: 19348461 PMID: 20222674 PMID: 16967446 PMID: 19767571 PMID: 20521846 PMID: 15115803 PMID: 20932056 PMID: 18796603
Proteomics / Inner Membrane fraction:
PMID: 17309111

Protein molec/cell:
5
PaxDb:
195 ppm

Class:
Multi-domain proteins (alpha and beta)
SCOP: 56572
Fold:
beta-lactamase/transpeptidase-like
SCOP: 56600
Penicillin-binding protein associated domain
SCOP: 69188
Super Family:
beta-lactamase/transpeptidase-like
SCOP: 56601
Penicillin-binding protein associated domain
SCOP: 69189

Go to Complexes

UniProt Name:
Maltose/maltodextrin-binding periplasmic protein (MMBP) (Maltodextrin-binding protein) (Maltose-binding protein) (MBP)
Localization:
Peripheral inner membrane protein facing the periplasm, periplasmic
Notes:
Potential substrate of periplasmic peptidyl prolyl cis???trans isomerase SurA. Sequence contains known binding motif of SurA [RYEF]X[RYEF][P]. MalE is maintained in an unfolded conformation by the cytoplasmic chaperone SecB. Potential Skp substrate PMID: 19953543 PMID: 9298646 An amber mutation in the secA gene of Escherichia coli causes a pleiotropic decrease in the synthesis of secreted proteins. PMID: 3009404 Potential substrate of periplasmic chaperone YfgM. PMID: 25403562 Putative substrate for the periplasmic chaperone YfgM. PMID: 25403562
References:
PMID: 18498364 PMID: 1989077 PMID: 19953543 PMID: 25403562 PMID: 3009404 PMID: 9298646
Pseudogene/Mobile Element:
-

mRNA molec/cell:
-

Proteomics:
PMID: 16606699 PMID: 12624733 PMID: 12488465 PMID: 19348461 PMID: 20222674 PMID: 19003857 PMID: 19767571 PMID: 15115803 PMID: 17446557 PMID: 18425732
Proteomics / Inner Membrane fraction:
PMID: 17446557

Protein molec/cell:
-
PaxDb:
1392 ppm

Class:
Alpha and beta proteins (a/b)
SCOP: 51349
Fold:
Periplasmic binding protein-like II
SCOP: 53849
Super Family:
Periplasmic binding protein-like II
SCOP: 53850

Go to Complexes

UniProt Name:
Alkaline phosphatase isozyme conversion protein (EC 3.4.11.-)
Localization:
Peripheral inner membrane protein facing the periplasm
Notes:
-
References:
PMID: 3316184
Pseudogene/Mobile Element:
-

mRNA molec/cell:
-

Proteomics:
PMID: 20222674
Proteomics / Inner Membrane fraction:
-

Protein molec/cell:
-
PaxDb:
1.08 ppm

Class:
Alpha and beta proteins (a/b)
SCOP: 51349
Fold:
Phosphorylase/hydrolase-like
SCOP: 53162
Super Family:
Zn-dependent exopeptidases
SCOP: 53187

Go to Complexes

UniProt Name:
Fe(3+) dicitrate-binding periplasmic protein (Iron(III) dicitrate-binding periplasmic protein)
Localization:
Peripheral inner membrane protein facing the periplasm, periplasmic
Notes:
-
References:
PMID: 2651410
Pseudogene/Mobile Element:
-

mRNA molec/cell:
-

Proteomics:
PMID: 19348461 PMID: 20222674 PMID: 19767571 PMID: 15115803
Proteomics / Inner Membrane fraction:
-

Protein molec/cell:
-
PaxDb:
0 ppm

Class:
Alpha and beta proteins (a/b)
SCOP: 51349
Fold:
Chelatase-like
SCOP: 53799
Super Family:
Helical backbone metal receptor
SCOP: 53807

Go to Complexes

UniProt Name:
Dimethyl sulfoxide reductase DmsA (DMSO reductase) (DMSOR) (Me2SO reductase) (EC 1.8.5.3)
Localization:
Peripheral inner membrane protein facing the periplasm
Notes:
TAT signal peptide, dmsABC complex. Part of the anaerobic dimethylsulphoxide (DMSO) reductase DmsABC. The DmsC polypeptide is composed of eight segments of hydrophobic amino acids of appropriate length to cross the cytoplasmic membrane, suggesting that this subunit functions to anchor the DMSO enzyme to the membrane. PMID: 3062312 There are contradictory experiments although it seems that the senario of the DmsABC complex facing the cytoplasm is more favoured. PMID: 11389150 The hydrophobic region of the DmsA twin-arginine leader peptide determines specificity with chaperone DmsD. PMID: 24093457 Fluorescence analysis of these YFP chimeras revealed a wide range of interactions such as the one between the Tat substrate dimethyl sulfoxide reductase (DmsA) and its dedicated proofreading chaperone DmsD. PMID: 20169075 The localization of DmsAB was compared in a strain expressing a partial DmsC subunit (pDMSC59X) with full-length DmsC originating from the chromosomal copy of the dms operon. In those experiments some DmsAB was reported in the periplasm in the absence of full-length DmsC, leading us to suggest that DmsC might serve a stop-transfer role. PMID: 9546395 TTnphoA fusions, and electron paramagnetic resonance monitoring the effects of the probe dysprosium(III) on an engineered 3Fe4S cluster in DmsB indicated that DmsAB faces the cytoplasm PMID: 2170332 PMID: 3280546 PMID: 3062312 Interacts with DmsD, a redox enzyme maturation protein (REMP). PMID: 20153451
References:
PMID: 11389150 PMID: 17218314 PMID: 20153451 PMID: 20169075 PMID: 2170332 PMID: 24093457 PMID: 3062312 PMID: 3280546 PMID: 9546395
Pseudogene/Mobile Element:
-

mRNA molec/cell:
-

Proteomics:
PMID: 16606699 PMID: 12624733 PMID: 12488465 PMID: 19348461 PMID: 20222674 PMID: 16967446 PMID: 19767571 PMID: 15115803
Proteomics / Inner Membrane fraction:
PMID: 17309111

Protein molec/cell:
-
PaxDb:
10.3 ppm

Class:
Alpha and beta proteins (a/b)
SCOP: 51349
Fold:
Double psi beta-barrel
SCOP: 50684
Formate dehydrogenase/DMSO reductase, domains 1-3
SCOP: 53705
Super Family:
ADC-like
SCOP: 50692
Formate dehydrogenase/DMSO reductase, domains 1-3
SCOP: 53706

Go to Complexes

UniProt Name:
Anaerobic dimethyl sulfoxide reductase chain B (DMSO reductase iron-sulfur subunit)
Localization:
Peripheral inner membrane protein facing the periplasm
Notes:
TAT (piggyback); DmsB is co-exported bound to Tat substrate DmsA. Part of the anaerobic dimethylsulphoxide (DMSO) reductase DmsABC. The DmsC polypeptide is composed of eight segments of hydrophobic amino acids of appropriate length to cross the cytoplasmic membrane, suggesting that this subunit functions to anchor the DMSO enzyme to the membrane. PMID: 3062312 There are contradictory experiments although it seems that the senario of the DmsABC complex facing the cytoplasm is more favoured. PMID: 11389150 The localization of DmsAB was compared in a strain expressing a partial DmsC subunit (pDMSC59X) with full-length DmsC originating from the chromosomal copy of the dms operon. In those experiments some DmsAB was reported in the periplasm in the absence of full-length DmsC, leading us to suggest that DmsC might serve a stop-transfer role. PMID: 9546395 TTnphoA fusions, and electron paramagnetic resonance monitoring the effects of the probe dysprosium(III) on an engineered 3Fe4S cluster in DmsB indicated that DmsAB faces the cytoplasm PMID: 2170332
References:
PMID: 11389150 PMID: 2170332 PMID: 3062312 PMID: 9546395
Pseudogene/Mobile Element:
-

mRNA molec/cell:
-

Proteomics:
PMID: 12624733 PMID: 20222674 PMID: 19767571 PMID: 20803007 PMID: 15115803
Proteomics / Inner Membrane fraction:
-

Protein molec/cell:
-
PaxDb:
5.84 ppm

Class:
Alpha and beta proteins (a+b)
SCOP: 53931
Fold:
Ferredoxin-like
SCOP: 54861
Super Family:
4Fe-4S ferredoxins
SCOP: 54862

Go to Complexes

UniProt Name:
Tail-specific protease (EC 3.4.21.102) (C-terminal-processing peptidase) (PRC protein) (Protease Re)
Localization:
Peripheral inner membrane protein facing the periplasm
Notes:
Fractionation of the maxicells producing the product or prc gene suggested that the product was associated with the periplasmic side of the cytoplasmic membrane. The prc gene, which is involved in cleavage of the C-terminal peptide from the precursor form of penicillin-binding protein 3 (PBP 3) of Escherichia coli. PMID: 1856173 PMID: 1729701
References:
PMID: 1729701 PMID: 1856173
Pseudogene/Mobile Element:
-

mRNA molec/cell:
-

Proteomics:
PMID: 17595003 PMID: 12624733 PMID: 12488465 PMID: 19348461 PMID: 20222674 PMID: 16967446 PMID: 19767571 PMID: 15115803
Proteomics / Inner Membrane fraction:
-

Protein molec/cell:
-
PaxDb:
153 ppm

Class:
Alpha and beta proteins (a/b)
SCOP: 51349
Fold:
PDZ domain-like
SCOP: 50155
ClpP/crotonase
SCOP: 52095
Super Family:
PDZ domain-like
SCOP: 50156
ClpP/crotonase
SCOP: 52096

Go to Complexes

UniProt Name:
Formate dehydrogenase, nitrate-inducible, major subunit (EC 1.17.5.3) (Anaerobic formate dehydrogenase major subunit) (Formate dehydrogenase-N subunit alpha) (FDH-N subunit alpha)
Localization:
Peripheral inner membrane protein facing the periplasm
Notes:
TAT secretion system; Formate dehydrogenase allows E.coli to use formate as major electron donor during anaerobic respiration, when nitrate is used as electron acceptor. The alpha subunit forms the active site. FdnG is the catalytic subunit of formate dehydrogenase-N (FdnGHI). FdnG was found in the periplasmic fraction of a mutant lacking the membrane anchor subunit FdnI, confirming that FdnG is located at the periplasmic face of the cytoplasmic membrane. PMID: 11929547 PMID: 11884747 PMID: 12923080 PMID: 11884747 PMID: 16858726
References:
PMID: 11884747 PMID: 11929547 PMID: 12923080 PMID: 15342602 PMID: 16858726 PMID: 17218314
Pseudogene/Mobile Element:
-

mRNA molec/cell:
0

Proteomics:
PMID: 16606699 PMID: 12624733 PMID: 19348461 PMID: 20222674 PMID: 16858726 PMID: 19767571 PMID: 20521846 PMID: 15115803
Proteomics / Inner Membrane fraction:
-

Protein molec/cell:
0
PaxDb:
2.59 ppm

Class:
Alpha and beta proteins (a/b)
SCOP: 51349
Fold:
Double psi beta-barrel
SCOP: 50684
Formate dehydrogenase/DMSO reductase, domains 1-3
SCOP: 53705
Super Family:
ADC-like
SCOP: 50692
Formate dehydrogenase/DMSO reductase, domains 1-3
SCOP: 53706

Go to Complexes

UniProt Name:
D-alanyl-D-alanine carboxypeptidase DacB (DD-carboxypeptidase) (DD-peptidase) (EC 3.4.16.4) (D-alanyl-D-alanine endopeptidase) (DD-endopeptidase) (EC 3.4.21.-) (Penicillin-binding protein 4) (PBP-4)
Localization:
Peripheral inner membrane protein facing the periplasm
Notes:
Exported from cytosol and signal peptide is cleaved. Anchored via C terminal the rest of the protein protudes into periplasm. Involved in peptidoglycan biosynthesis and is Penicillin-binding. PMID: 16411754 PMID: 15576782 DacB(PBP-4) anchors to the periplasmic face of the inner membrane via C-terminal amphiphilic alpha-helix. PMID: 9371419
References:
PMID: 12444970 PMID: 15576782 PMID: 15911532 PMID: 16411754 PMID: 9371419
Pseudogene/Mobile Element:
-

mRNA molec/cell:
-

Proteomics:
PMID: 16606699 PMID: 12624733 PMID: 19348461 PMID: 20222674 PMID: 19767571 PMID: 20932056
Proteomics / Inner Membrane fraction:
-

Protein molec/cell:
1
PaxDb:
4.11 ppm

Class:
Multi-domain proteins (alpha and beta)
SCOP: 56572
Fold:
beta-lactamase/transpeptidase-like SCOP: 56600
Super Family:
beta-lactamase/transpeptidase-like
SCOP: 56601

Go to Complexes

UniProt Name:
Uncharacterized protein YadE
Localization:
-
Notes:
Homolog to C-terminus of DnaA which is a peripherally accossiated proteins with a C-terminal anchor.
References:
-
Pseudogene/Mobile Element:
-

mRNA molec/cell:
0

Proteomics:
PMID: 16606699 PMID: 19348461 PMID: 20222674 PMID: 20932056
Proteomics / Inner Membrane fraction:
-

Protein molec/cell:
1
PaxDb:
1.31 ppm

Class:
Alpha and beta proteins (a/b)
SCOP: 51349
Fold:
7-stranded beta/alpha barrel SCOP: 51988
Super Family:
Glycoside hydrolase/deacetylase
SCOP: 88713

Go to Complexes

UniProt Name:
D-alanyl-D-alanine carboxypeptidase DacD (DD-carboxypeptidase) (DD-peptidase) (EC 3.4.16.4) (Penicillin-binding protein 6b) (PBP-6b)
Localization:
Peripheral inner membrane protein facing the periplasm
Notes:
Penicillin-binding protein 5 (PBP 5); membrane-bound cell wall dd-carboxypeptidase, localized in the outer leaflet of the cytosolic membrane. PMID: 8955390
References:
PMID: 20192190 PMID: 8955390
Pseudogene/Mobile Element:
-

mRNA molec/cell:
-

Proteomics:
PMID: 16606699
Proteomics / Inner Membrane fraction:
-

Protein molec/cell:
-
PaxDb:
0 ppm

Class:
Multi-domain proteins (alpha and beta)
SCOP: 56572
Fold:
Penicillin-binding protein associated domain SCOP: 69188
Super Family:
beta-lactamase/transpeptidase-like
SCOP: 56601
Penicillin-binding protein associated domain
SCOP: 69189

Go to Complexes

UniProt Name:
Hydrogenase-2 small chain (HYD2) (EC 1.12.99.6) (Membrane-bound hydrogenase 2 small subunit) (NiFe hydrogenase)
Localization:
Peripheral inner membrane protein facing the periplasm
Notes:
Copurifies with trigger factor in pull down assays. Exported by the Tat system. Experimentally proven signal peptide cleavage site. Under anaerobic conditions Escherichia coli synthesizes three membrane-associated [NiFe]-hydrogenases (Hyd). Hyd-1 and Hyd-2 are respiratory hydrogenases with their active sites facing the periplasm. PMID: 22769583 PMID: 9738917
References:
PMID: 17218314 PMID: 19737520 PMID: 22769583 PMID: 9738917
Pseudogene/Mobile Element:
-

mRNA molec/cell:
-

Proteomics:
PMID: 16606699 PMID: 19348461 PMID: 20222674 PMID: 16858726 PMID: 19767571
Proteomics / Inner Membrane fraction:
PMID: 17309111

Protein molec/cell:
-
PaxDb:
0 ppm

Class:
Multi-domain proteins (alpha and beta)
SCOP: 56572
Fold:
HydA/Nqo6-like SCOP: 56769
Super Family:
HydA/Nqo6-like
SCOP: 56770

Go to Complexes

UniProt Name:
Protein-methionine-sulfoxide reductase catalytic subunit MsrP (EC 1.8.5.-)
Localization:
Peripheral inner membrane protein facing the periplasm
Notes:
TAT secretion system. PMID: 15355966
References:
PMID: 15355966 PMID: 16042411 PMID: 17218314
Pseudogene/Mobile Element:
-

mRNA molec/cell:
-

Proteomics:
PMID: 20222674
Proteomics / Inner Membrane fraction:
-

Protein molec/cell:
-
PaxDb:
13.2 ppm

Class:
Alpha and beta proteins (a+b)
SCOP: 53931
Fold:
Oxidoreductase molybdopterin-binding domain SCOP: 56523
Super Family:
Oxidoreductase molybdopterin-binding domain
SCOP: 56524

Go to Complexes

UniProt Name:
Multidrug resistance protein MdtA (Multidrug transporter MdtA)
Localization:
Peripheral inner membrane protein facing the periplasm
Notes:
Part of MdtABC-TolC multidrug efflux transport system = [(TolC)3][MdtC][MdtB][MdtA].
References:
PMID: 12107133 PMID: 12107134 PMID: 21890895
Pseudogene/Mobile Element:
-

mRNA molec/cell:
-

Proteomics:
PMID: 19348461 PMID: 20222674 PMID: 19767571 PMID: 20932056
Proteomics / Inner Membrane fraction:
-

Protein molec/cell:
1
PaxDb:
3.05 ppm

Class:
Membrane and cell surface proteins and peptides
SCOP: 56835
Fold:
HlyD-like secretion proteins SCOP: 111368
Super Family:
HlyD-like secretion proteins
SCOP: 111369

Go to Complexes