OMPA_YERPS
ID OMPA_YERPS Reviewed; 353 AA.
AC P38399; Q66CF0;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 2.
DT 25-MAY-2022, entry version 126.
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}; OrderedLocusNames=YPTB1453;
OS Yersinia pseudotuberculosis serotype I (strain IP32953).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=273123;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IP32953;
RX PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA Derbise A., Hauser L.J., Garcia E.;
RT "Insights into the evolution of Yersinia pestis through whole-genome
RT comparison with Yersinia pseudotuberculosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004).
RN [2]
RP PROTEIN SEQUENCE OF 22-50.
RX PubMed=2478630;
RA Zhang J.J., Hamachi M., Hamachi T., Zhao Y.P., Yu D.T.Y.;
RT "The bacterial outer membrane protein that reacts with anti-HLA-B27
RT antibodies is the OmpA protein.";
RL J. Immunol. 143:2955-2960(1989).
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 -!- 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}.
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DR EMBL; BX936398; CAH20693.1; -; Genomic_DNA.
DR PIR; A60752; A60752.
DR RefSeq; WP_002213066.1; NZ_CP009712.1.
DR AlphaFoldDB; P38399; -.
DR SMR; P38399; -.
DR EnsemblBacteria; CAH20693; CAH20693; YPTB1453.
DR GeneID; 66842112; -.
DR KEGG; ypo:BZ17_1065; -.
DR KEGG; yps:YPTB1453; -.
DR PATRIC; fig|273123.14.peg.1130; -.
DR OMA; HDTGFYG; -.
DR Proteomes; UP000001011; 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 1: Evidence at protein level;
KW Cell outer membrane; Direct protein sequencing; Disulfide bond;
KW Ion transport; Membrane; Porin; Repeat; Signal; Transmembrane;
KW Transmembrane beta strand; Transport.
FT SIGNAL 1..21
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00842,
FT ECO:0000269|PubMed:2478630"
FT CHAIN 22..353
FT /note="Outer membrane protein A"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT /id="PRO_0000020103"
FT TRANSMEM 27..37
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT TRANSMEM 56..67
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT TRANSMEM 71..79
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT TRANSMEM 97..108
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT TRANSMEM 113..121
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT TRANSMEM 148..157
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT TRANSMEM 162..169
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT TRANSMEM 188..196
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT REPEAT 208..209
FT /note="1"
FT REPEAT 210..211
FT /note="2"
FT REPEAT 212..213
FT /note="3"
FT REPEAT 214..215
FT /note="4"
FT DOMAIN 217..345
FT /note="OmpA-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT REGION 208..215
FT /note="4 X 2 AA approximate tandem repeats of A-P"
FT SITE 74
FT /note="Part of salt bridge gating mechanism"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT SITE 165
FT /note="Part of salt bridge gating mechanism"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT DISULFID 318..330
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT CONFLICT 35
FT /note="G -> P (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 42..45
FT /note="TGSI -> DPW (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 49
FT /note="D -> K (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 353 AA; 37930 MW; 38D23EFDD5466CBF CRC64;
MKKTAIALAV ALVGFATVAQ AAPKDNTWYT GGKLGWSQYQ DTGSIINNDG PTHKDQLGAG
AFFGYQANQY LGFEMGYDWL GRMPYKGDIN NGAFKAQGVQ LAAKLSYPVA QDLDVYTRLG
GLVWRADAKG SFDGGLDRAS GHDTGVSPLV ALGAEYAWTK NWATRMEYQW VNNIGDRETV
GARPDNGLLS VGVSYRFGQE DAAAPIVAPT PAPAPIVDTK RFTLKSDVLF GFNKANLKPE
GQQALDQLYA QLSSIDPKDG SVVVLGFADR IGQPAPNLAL SQRRADSVRD YLVSKGIPAD
KITARGEGQA NPVTGNTCDN VKPRAALIEC LAPDRRVEIE VKGYKEVVTQ PQA