Reviewed, UniProtKB/Swiss-Prot P0A910 (OMPA_ECOLI)

Names and origin

Protein names

Recommended name:
    Outer membrane protein A
Alternative name(s):
    Outer membrane protein II*

Gene names

Name:	ompA
Synonyms:	con, tolG, tut
Ordered Locus Names:	b0957, JW0940

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	346 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Required for the action of colicins K and L and for the stabilization of mating aggregates in conjugation. Serves as a receptor for a number of T-even like phages. Also acts as a porin with low permeability that allows slow penetration of small solutes.
Subunit structure	Homodimer. Ref.16
Subcellular location	Cell outer membrane; Multi-pass membrane protein Ref.16 Ref.13.
Sequence similarities	Belongs to the ompA family. Contains 1 OmpA-like domain.
Mass spectrometry	Molecular mass is 35177 Da from positions 22 - 346. Determined by ESI. Ref.20

Ontologies

Keywords
Biological process	Conjugation Ion transport Phage recognition Transport
Cellular component	Cell membrane Cell outer membrane Membrane
Domain	Repeat Signal Transmembrane
Molecular function	Porin
PTM	Disulfide bond
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	conjugation Inferred from electronic annotation. Source: UniProtKB-KW detection of virus Inferred from electronic annotation. Source: UniProtKB-KW entry of virus into host cell Inferred from electronic annotation. Source: UniProtKB-KW ion transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cell outer membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW pore complex Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	protein binding Inferred from physical interaction. Source: IntAct structural molecule activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
arrD	P78285	1	EBI-371347,EBI-1118665
ttdA	P05847	1	EBI-371347,EBI-1113137

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 21

21

Ref.6 Ref.7 Ref.8 Ref.9

Chain

22 – 346

325

Outer membrane protein A

PRO_0000020094

Regions

Topological domain

22 – 26

5

Periplasmic Ref.14 Ref.15

Transmembrane

27 – 37

11

Topological domain

38 – 54

17

Extracellular Ref.14 Ref.15

Transmembrane

55 – 66

12

Topological domain

67 – 69

3

Periplasmic Ref.14 Ref.15

Transmembrane

70 – 78

9

Topological domain

79 – 95

17

Extracellular Ref.14 Ref.15

Transmembrane

96 – 107

12

Topological domain

108 – 111

4

Periplasmic Ref.14 Ref.15

Transmembrane

112 – 124

13

Topological domain

125 – 137

13

Extracellular Ref.14 Ref.15

Transmembrane

138 – 151

14

Topological domain

152 – 155

4

Periplasmic Ref.14 Ref.15

Transmembrane

156 – 163

8

Topological domain

164 – 181

18

Extracellular Ref.14 Ref.15

Transmembrane

182 – 190

9

Topological domain

191 – 346

156

Periplasmic Ref.14 Ref.15

Repeat

201 – 202

2

1

Repeat

203 – 204

2

2

Repeat

205 – 206

2

3

Repeat

207 – 208

2

4

Domain

210 – 338

129

OmpA-like

Region

197 – 208

12

Hinge-like

Region

201 – 208

8

4 X 2 AA tandem repeats of A-P

Amino acid modifications

Disulfide bond

311 ↔ 323

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

346

Helix Strand Turn

Details...

Beta strand

26 – 37

12

Beta strand

41 – 43

3

Beta strand

46 – 48

3

Beta strand

53 – 66

14

Turn

67 – 69

3

Beta strand

70 – 78

9

Beta strand

96 – 124

29

Beta strand

138 – 153

16

Beta strand

156 – 163

8

Turn

172 – 175

4

Beta strand

182 – 190

9

Sequences

	Sequence		Length	Mass (Da)
	P0A910-1 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: 195147734CDF8B04	FASTA	346	37,201
	10 20 30 40 50 60 MKKTAIAIAV ALAGFATVAQ AAPKDNTWYT GAKLGWSQYH DTGFINNNGP THENQLGAGA 70 80 90 100 110 120 FGGYQVNPYV GFEMGYDWLG RMPYKGSVEN GAYKAQGVQL TAKLGYPITD DLDIYTRLGG 130 140 150 160 170 180 MVWRADTKSN VYGKNHDTGV SPVFAGGVEY AITPEIATRL EYQWTNNIGD AHTIGTRPDN 190 200 210 220 230 240 GMLSLGVSYR FGQGEAAPVV APAPAPAPEV QTKHFTLKSD VLFNFNKATL KPEGQAALDQ 250 260 270 280 290 300 LYSQLSNLDP KDGSVVVLGY TDRIGSDAYN QGLSERRAQS VVDYLISKGI PADKISARGM 310 320 330 340 GESNPVTGNT CDNVKQRAAL IDCLAPDRRV EIEVKGIKDV VTQPQA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of the gene ompA coding the outer membrane protein II of Escherichia coli K-12." Beck E., Bremer E. Nucleic Acids Res. 8:3011-3024(1980) [PubMed: 6253901] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	"Gene structure of the OmpA protein, a major surface protein of Escherichia coli required for cell-cell interaction." Movva N.R., Nakamura K., Inouye M. J. Mol. Biol. 143:317-328(1980) [PubMed: 6260961] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[3]	"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. , Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T. DNA Res. 3:137-155(1996) [PubMed: 8905232] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[5]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]	"Primary structure of major outer membrane protein II (ompA protein) of Escherichia coli K-12." Chen R., Schmidmayr W., Kramer C., Chen-Schmeisser U., Henning U. Proc. Natl. Acad. Sci. U.S.A. 77:4592-4596(1980) [PubMed: 7001461] [Abstract] Cited for: PROTEIN SEQUENCE OF 22-346. Strain: K12.
[7]	"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Link A.J., Robison K., Church G.M. Electrophoresis 18:1259-1313(1997) [PubMed: 9298646] [Abstract] Cited for: PROTEIN SEQUENCE OF 22-34. Strain: K12 / EMG2.
[8]	Pasquali C., Sanchez J.-C., Ravier F., Golaz O., Hughes G.J., Frutiger S., Paquet N., Wilkins M., Appel R.D., Bairoch A., Hochstrasser D.F. Submitted (SEP-1994) to UniProtKB Cited for: PROTEIN SEQUENCE OF 22-32. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[9]	"Extraction of membrane proteins by differential solubilization for separation using two-dimensional gel electrophoresis." Molloy M.P., Herbert B.R., Walsh B.J., Tyler M.I., Traini M., Sanchez J.-C., Hochstrasser D.F., Williams K.L., Gooley A.A. Electrophoresis 19:837-844(1998) [PubMed: 9629924] [Abstract] Cited for: PROTEIN SEQUENCE OF 22-26. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[10]	"Escherichia coli K-12 outer membrane protein (OmpA) as a bacteriophage receptor: analysis of mutant genes expressing altered proteins." Morona R., Klose M., Henning U. J. Bacteriol. 159:570-578(1984) [PubMed: 6086577] [Abstract] Cited for: MUTANTS RESISTANT TO PHAGE ENTRY.
[11]	"Bacteriophage receptor area of outer membrane protein OmpA of Escherichia coli K-12." Morona R., Kramer C., Henning U. J. Bacteriol. 164:539-543(1985) [PubMed: 3902787] [Abstract] Cited for: MUTANTS RESISTANT TO PHAGE ENTRY.
[12]	"Pore-forming activity of OmpA protein of Escherichia coli." Sugawara E., Nikaido H. J. Biol. Chem. 267:2507-2511(1992) [PubMed: 1370823] [Abstract] Cited for: PORIN ACTIVITY. Strain: K12.
[13]	"Evidence for a loop-like insertion mechanism of pro-Omp A into the inner membrane of Escherichia coli." Kuhn A., Kiefer D., Koehne C., Zhu H.-Y., Tschantz W.R., Dalbey R.E. Eur. J. Biochem. 226:891-897(1994) [PubMed: 7813480] [Abstract] Cited for: SUBCELLULAR LOCATION.
[14]	"Prediction of transmembrane beta-strands from hydrophobic characteristics of proteins." Gromiha M.M., Ponnuswamy P.K. Int. J. Pept. Protein Res. 42:420-431(1993) [PubMed: 8106193] [Abstract] Cited for: TOPOLOGY.
[15]	"Structural and functional roles of the surface-exposed loops of the beta-barrel membrane protein OmpA from Escherichia coli." Koebnik R. J. Bacteriol. 181:3688-3694(1999) [PubMed: 10368142] [Abstract] Cited for: TOPOLOGY.
[16]	"Protein complexes of the Escherichia coli cell envelope." Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L., von Heijne G., Daley D.O. J. Biol. Chem. 280:34409-34419(2005) [PubMed: 16079137] [Abstract] Cited for: DIMERIZATION, SUBCELLULAR LOCATION. Strain: BL21-DE3.
[17]	"Structure of the outer membrane protein A transmembrane domain." Pautsch A., Schulz G.E. Nat. Struct. Biol. 5:1013-1017(1998) [PubMed: 9808047] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 22-192.
[18]	"High-resolution structure of the OmpA membrane domain." Pautsch A., Schulz G.E. J. Mol. Biol. 298:273-282(2000) [PubMed: 10764596] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).
[19]	"Structure of outer membrane protein A transmembrane domain by NMR spectroscopy." Arora A., Abildgaard F., Bushweller J.H., Tamm L.K. Nat. Struct. Biol. 8:334-338(2001) [PubMed: 11276254] [Abstract] Cited for: STRUCTURE BY NMR OF 22-197.
[20]	"Proteomics on full-length membrane proteins using mass spectrometry." le Coutre J., Whitelegge J.P., Gross A., Turk E., Wright E.M., Kaback H.R., Faull K.F. Biochemistry 39:4237-4242(2000) [PubMed: 10757971] [Abstract] Cited for: MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

V00307 Genomic DNA. Translation: CAA23588.1.
U00096 Genomic DNA. Translation: AAC74043.1.
AP009048 Genomic DNA. Translation: BAA35715.1.

PIR

MMECA. A93707.

RefSeq

AP_001587.1.
NP_415477.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BXW	X-ray	2.50	A	22-192	[»]
1G90	NMR	-	A	22-197	[»]
1QJP	X-ray	1.65	A	22-192	[»]
2GE4	NMR	-	A	22-197	[»]
2JMM	NMR	-	A	23-197	[»]

SMR

P0A910. Positions 208-337.

ModBase

Search...

Protein-protein interaction databases

IntAct

P0A910. 9 interactions.

STRING

P0A910.

Protein family/group databases

TCDB

1.B.6.1.1. OmpA-OmpF porin (OOP) family.

2-D gel databases

SWISS-2DPAGE

P0A910.

2DBase-Ecoli

P0A910.

ECO2DBASE

F024.5. 6TH EDITION.
F028.0. 6TH EDITION.
F033.0. 6TH EDITION.
F033.1. 6TH EDITION.

Proteomic databases

PRIDE

P0A910.

Genome annotation databases

GeneID

945571.

GenomeReviews

Gene locus JW0940 in contig AP009048_GR.
Gene locus b0957 in contig U00096_GR.

KEGG

ecj:JW0940.
eco:b0957.

Organism-specific databases

EchoBASE

EB0663.

EcoGene

EG10669. ompA.

CMR

Search...

Phylogenomic databases

eggNOG

COG2885.

HOGENOM

HBG741096.

OMA

DDNEAQK.

Enzyme and pathway databases

BioCyc

EcoCyc:EG10669-MONOMER.
ECOL168927:B0957-MONOMER.

Gene expression databases

Genevestigator

P0A910.

Family and domain databases

InterPro

IPR011250. OMP_b-brl.
IPR006664. OMP_bac.
IPR002368. OmpA.
IPR006690. OMPA-like_CS.
IPR000498. OmpA-like_TM_dom.
IPR006665. OmpA/MotB_C.
[Graphical view]

Gene3D

G3DSA:2.40.160.20. OMP_b-brl. 1 hit.
G3DSA:3.30.1330.60. OmpA/MotB_C. 1 hit.

Pfam

PF00691. OmpA. 1 hit.
PF01389. OmpA_membrane. 1 hit.
[Graphical view]

PRINTS

PR01021. OMPADOMAIN.
PR01022. OUTRMMBRANEA.

PROSITE

PS01068. OMPA_1. 1 hit.
PS51123. OMPA_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

OMPA_ECOLI

Accession

Primary (citable) accession number: P0A910
Secondary accession number(s): P02934

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	January 19, 2010
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)