OMPA_ECO57
ID OMPA_ECO57 Reviewed; 346 AA.
AC P0A911; P02934;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Outer membrane protein A {ECO:0000255|HAMAP-Rule:MF_00842};
DE AltName: Full=Outer membrane porin A {ECO:0000255|HAMAP-Rule:MF_00842};
DE Flags: Precursor;
GN Name=ompA {ECO:0000255|HAMAP-Rule:MF_00842};
GN OrderedLocusNames=Z1307, ECs1041;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
CC -!- FUNCTION: With TolR probably plays a role in maintaining the position
CC of the peptidoglycan cell wall in the periplasm. Acts as a porin with
CC low permeability that allows slow penetration of small solutes; an
CC internal gate slows down solute passage. {ECO:0000255|HAMAP-
CC Rule:MF_00842}.
CC -!- FUNCTION: Required for conjugation with F-type plasmids; probably
CC serves as the mating receptor on recipient cells. {ECO:0000255|HAMAP-
CC Rule:MF_00842}.
CC -!- SUBUNIT: Monomer and homodimer. {ECO:0000255|HAMAP-Rule:MF_00842}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000255|HAMAP-
CC Rule:MF_00842}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_00842}.
CC -!- DOMAIN: The extracellular loops are most variable in sequence, and in
CC some bacteria confer sensitivity to phage and/or colicins.
CC {ECO:0000255|HAMAP-Rule:MF_00842}.
CC -!- SIMILARITY: Belongs to the outer membrane OOP (TC 1.B.6) superfamily.
CC OmpA family. {ECO:0000255|HAMAP-Rule:MF_00842}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE005174; AAG55443.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB34464.1; -; Genomic_DNA.
DR PIR; A90759; A90759.
DR PIR; G85622; G85622.
DR RefSeq; NP_309068.1; NC_002695.1.
DR RefSeq; WP_000750416.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P0A911; -.
DR BMRB; P0A911; -.
DR SMR; P0A911; -.
DR STRING; 155864.EDL933_1224; -.
DR EnsemblBacteria; AAG55443; AAG55443; Z1307.
DR EnsemblBacteria; BAB34464; BAB34464; ECs_1041.
DR GeneID; 917123; -.
DR KEGG; ece:Z1307; -.
DR KEGG; ecs:ECs_1041; -.
DR PATRIC; fig|386585.9.peg.1165; -.
DR eggNOG; COG2885; Bacteria.
DR eggNOG; COG3637; Bacteria.
DR HOGENOM; CLU_031536_0_0_6; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046930; C:pore complex; IEA:UniProtKB-KW.
DR GO; GO:0015288; F:porin activity; IEA:UniProtKB-UniRule.
DR GO; GO:0034220; P:ion transmembrane transport; IEA:UniProtKB-UniRule.
DR CDD; cd07185; OmpA_C-like; 1.
DR Gene3D; 3.30.1330.60; -; 1.
DR HAMAP; MF_00842; OmpA; 1.
DR InterPro; IPR011250; OMP/PagP_b-brl.
DR InterPro; IPR006664; OMP_bac.
DR InterPro; IPR002368; OmpA.
DR InterPro; IPR006665; OmpA-like.
DR InterPro; IPR006690; OMPA-like_CS.
DR InterPro; IPR036737; OmpA-like_sf.
DR InterPro; IPR000498; OmpA-like_TM_dom.
DR Pfam; PF00691; OmpA; 1.
DR Pfam; PF01389; OmpA_membrane; 1.
DR PRINTS; PR01021; OMPADOMAIN.
DR PRINTS; PR01022; OUTRMMBRANEA.
DR SUPFAM; SSF103088; SSF103088; 1.
DR SUPFAM; SSF56925; SSF56925; 1.
DR PROSITE; PS01068; OMPA_1; 1.
DR PROSITE; PS51123; OMPA_2; 1.
PE 3: Inferred from homology;
KW Cell outer membrane; Conjugation; Disulfide bond; Ion transport; Membrane;
KW Porin; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane beta strand; Transport.
FT SIGNAL 1..21
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT CHAIN 22..346
FT /note="Outer membrane protein A"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT /id="PRO_0000020095"
FT TRANSMEM 27..37
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT TRANSMEM 55..66
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT TRANSMEM 70..78
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT TRANSMEM 96..107
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT TRANSMEM 112..120
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT TRANSMEM 142..151
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT TRANSMEM 156..163
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT TRANSMEM 182..190
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT REPEAT 201..202
FT /note="1"
FT REPEAT 203..204
FT /note="2"
FT REPEAT 205..206
FT /note="3"
FT REPEAT 207..208
FT /note="4"
FT DOMAIN 210..338
FT /note="OmpA-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT REGION 197..208
FT /note="Hinge-like"
FT REGION 201..208
FT /note="4 X 2 AA tandem repeats of A-P"
FT SITE 73
FT /note="Part of salt bridge gating mechanism"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT SITE 159
FT /note="Part of salt bridge gating mechanism"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT DISULFID 311..323
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
SQ SEQUENCE 346 AA; 37201 MW; 195147734CDF8B04 CRC64;
MKKTAIAIAV ALAGFATVAQ AAPKDNTWYT GAKLGWSQYH DTGFINNNGP THENQLGAGA
FGGYQVNPYV GFEMGYDWLG RMPYKGSVEN GAYKAQGVQL TAKLGYPITD DLDIYTRLGG
MVWRADTKSN VYGKNHDTGV SPVFAGGVEY AITPEIATRL EYQWTNNIGD AHTIGTRPDN
GMLSLGVSYR FGQGEAAPVV APAPAPAPEV QTKHFTLKSD VLFNFNKATL KPEGQAALDQ
LYSQLSNLDP KDGSVVVLGY TDRIGSDAYN QGLSERRAQS VVDYLISKGI PADKISARGM
GESNPVTGNT CDNVKQRAAL IDCLAPDRRV EIEVKGIKDV VTQPQA
