ID C0Q8D5_SALPC Unreviewed; 358 AA.
AC C0Q8D5;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=Outer membrane protein A {ECO:0000256|ARBA:ARBA00029539, ECO:0000256|HAMAP-Rule:MF_00842};
DE AltName: Full=Outer membrane porin A {ECO:0000256|HAMAP-Rule:MF_00842};
DE Flags: Precursor;
GN Name=ompA {ECO:0000256|HAMAP-Rule:MF_00842,
GN ECO:0000313|EMBL:ACN46780.1};
GN OrderedLocusNames=SPC_2679 {ECO:0000313|EMBL:ACN46780.1};
OS Salmonella paratyphi C (strain RKS4594).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=476213 {ECO:0000313|EMBL:ACN46780.1, ECO:0000313|Proteomes:UP000001599};
RN [1] {ECO:0000313|EMBL:ACN46780.1, ECO:0000313|Proteomes:UP000001599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RKS4594 {ECO:0000313|EMBL:ACN46780.1,
RC ECO:0000313|Proteomes:UP000001599};
RX PubMed=19229335; DOI=10.1371/journal.pone.0004510;
RA Liu W.-Q., Feng Y., Wang Y., Zou Q.-H., Chen F., Guo J.-T., Peng Y.-H.,
RA Jin Y., Li Y.-G., Hu S.-N., Johnston R.N., Liu G.-R., Liu S.-L.;
RT "Salmonella paratyphi C: genetic divergence from Salmonella choleraesuis
RT and pathogenic convergence with Salmonella typhi.";
RL PLoS ONE 4:E4510-E4510(2009).
CC -!- FUNCTION: Required for conjugation with F-type plasmids; probably
CC serves as the mating receptor on recipient cells. {ECO:0000256|HAMAP-
CC Rule:MF_00842}.
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:0000256|HAMAP-
CC Rule:MF_00842}.
CC -!- SUBUNIT: Monomer and homodimer. {ECO:0000256|HAMAP-Rule:MF_00842}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane
CC {ECO:0000256|ARBA:ARBA00004571, ECO:0000256|HAMAP-Rule:MF_00842};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004571,
CC ECO:0000256|HAMAP-Rule:MF_00842}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- DOMAIN: The extracellular loops are most variable in sequence, and in
CC some bacteria confer sensitivity to phage and/or colicins.
CC {ECO:0000256|HAMAP-Rule:MF_00842}.
CC -!- SIMILARITY: Belongs to the outer membrane OOP (TC 1.B.6) superfamily.
CC OmpA family. {ECO:0000256|ARBA:ARBA00005710, ECO:0000256|HAMAP-
CC Rule:MF_00842}.
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DR EMBL; CP000857; ACN46780.1; -; Genomic_DNA.
DR AlphaFoldDB; C0Q8D5; -.
DR KEGG; sei:SPC_2679; -.
DR HOGENOM; CLU_031536_0_0_6; -.
DR Proteomes; UP000001599; 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:monoatomic ion transmembrane transport; IEA:UniProtKB-UniRule.
DR CDD; cd07185; OmpA_C-like; 1.
DR Gene3D; 2.40.160.20; -; 1.
DR Gene3D; 3.30.1330.60; OmpA-like domain; 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 PANTHER; PTHR30329:SF23; LIPOPROTEIN YIAD-RELATED; 1.
DR PANTHER; PTHR30329; STATOR ELEMENT OF FLAGELLAR MOTOR COMPLEX; 1.
DR Pfam; PF00691; OmpA; 1.
DR Pfam; PF01389; OmpA_membrane; 1.
DR PRINTS; PR01021; OMPADOMAIN.
DR PRINTS; PR01022; OUTRMMBRANEA.
DR SUPFAM; SSF103088; OmpA-like; 1.
DR SUPFAM; SSF56925; OMPA-like; 1.
DR PROSITE; PS01068; OMPA_1; 1.
DR PROSITE; PS51123; OMPA_2; 1.
PE 3: Inferred from homology;
KW Cell outer membrane {ECO:0000256|ARBA:ARBA00023237, ECO:0000256|HAMAP-
KW Rule:MF_00842}; Conjugation {ECO:0000256|HAMAP-Rule:MF_00842};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|HAMAP-
KW Rule:MF_00842};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065, ECO:0000256|HAMAP-
KW Rule:MF_00842};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00842};
KW Porin {ECO:0000256|ARBA:ARBA00023114, ECO:0000256|HAMAP-Rule:MF_00842};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|HAMAP-Rule:MF_00842};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_00842};
KW Transmembrane beta strand {ECO:0000256|ARBA:ARBA00022452,
KW ECO:0000256|HAMAP-Rule:MF_00842};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_00842}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00842"
FT CHAIN 30..358
FT /note="Outer membrane protein A"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00842"
FT /id="PRO_5026408995"
FT DOMAIN 222..350
FT /note="OmpA-like"
FT /evidence="ECO:0000259|PROSITE:PS51123"
FT SITE 81
FT /note="Part of salt bridge gating mechanism"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00842"
FT SITE 171
FT /note="Part of salt bridge gating mechanism"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00842"
FT DISULFID 323..335
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00842"
SQ SEQUENCE 358 AA; 38423 MW; 16649FF9FA38C631 CRC64;
MDDNEAQKMK KTAIAIAVAL AGFATVAQAA PKDNTWYAGA KLGWSQYHDT GFINNDGPTH
ENQLGAGAFG GYQVNPYVGF EMGYDWLGRM PYKGDNINGA YKAQGVQLTA KLGYPITDDL
DVYTRLGGMV WRADTKSNVP GGPSTKDHDT GVSPVFAGGI EYAITPEIAT RLEYQWTNNI
GDANTIGTRP DNGLLSVGVS YRFGQQEAAP VVAPAPAPAP EVQTKHFTLK SDVLFNFNKS
TLKPEGQQAL DQLYSQLSNL DPKDGSVVVL GFTDRIGSDA YNQGLSEKRA QSVVDYLISK
GIPSNKISAR GMGESNPVTG NTCDNVKPRA ALIDCLAPDR RVEIEVKGVK DVVTQPQA
//
