ID A8AIC2_CITK8 Unreviewed; 356 AA.
AC A8AIC2;
DT 23-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 23-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 91.
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 OrderedLocusNames=CKO_02111 {ECO:0000313|EMBL:ABV13235.1};
OS Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Citrobacter.
OX NCBI_TaxID=290338 {ECO:0000313|EMBL:ABV13235.1, ECO:0000313|Proteomes:UP000008148};
RN [1] {ECO:0000313|EMBL:ABV13235.1, ECO:0000313|Proteomes:UP000008148}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-895 / CDC 4225-83 / SGSC4696
RC {ECO:0000313|Proteomes:UP000008148};
RG The Citrobacter koseri Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA Latreille P., Courtney L., Wang C., Pepin K., Bhonagiri V., Nash W.,
RA Johnson M., Thiruvilangam P., Wilson R.;
RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000822; ABV13235.1; -; Genomic_DNA.
DR AlphaFoldDB; A8AIC2; -.
DR STRING; 290338.CKO_02111; -.
DR KEGG; cko:CKO_02111; -.
DR HOGENOM; CLU_031536_0_0_6; -.
DR Proteomes; UP000008148; 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};
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 Reference proteome {ECO:0000313|Proteomes:UP000008148};
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..356
FT /note="Outer membrane protein A"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00842"
FT /id="PRO_5026411068"
FT DOMAIN 220..348
FT /note="OmpA-like"
FT /evidence="ECO:0000259|PROSITE:PS51123"
FT SITE 83
FT /note="Part of salt bridge gating mechanism"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00842"
FT SITE 169
FT /note="Part of salt bridge gating mechanism"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00842"
FT DISULFID 321..333
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00842"
SQ SEQUENCE 356 AA; 38273 MW; B9FECA6F6D96EE6D CRC64;
MDDNEAQKMK KTAIAIAVAL AGFATVAQAA PKDNTWYTGA KLGWSQFHDV GNNQIDNNGP
THESQLGAGA FGGYQVNPYV GFEMGYDWLG RMPYKGNTQN GAFKAQGVQL TAKLGYPITD
DLDVYTRLGG MVWRADAQNN TGFKDHDTGV SPVFAGGVEY AVTRDIATRL EYQWTNNIGD
ANTVGGRPDN GLLSVGVSYR FGQQEEAAPI APAPAPAPEV QTKHFTLKSD VLFNFNKATL
KPEGQQALDQ MYSQLSNLDP KDGSVVVLGF TDRIGSDAYN QGLSEKRAQS VVDYLISKGI
PADKISARGM GESNPVTGNT CDNVKARAAL IDCLAPDRRV EIEVKGVKDV VTQPQA
//
