ID F5BBE0_PASMD Unreviewed; 348 AA.
AC F5BBE0;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Outer membrane protein A {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:AEC04326.1};
OS Pasteurella multocida.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Pasteurella.
OX NCBI_TaxID=747 {ECO:0000313|EMBL:AEC04326.1};
RN [1] {ECO:0000313|EMBL:AEC04326.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=49A {ECO:0000313|EMBL:AEC04326.1};
RA Verma S., Verma L., Sharma M.;
RT "Sequence Diversity of outer membrane protein gene (ompA) of Pasteurella
RT multocida recovered from diseased & apparently healthy animals.";
RL Submitted (DEC-2010) 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; HQ829463; AEC04326.1; -; Genomic_DNA.
DR AlphaFoldDB; F5BBE0; -.
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:SF21; MOTILITY PROTEIN B; 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 Signal {ECO:0000256|ARBA:ARBA00022729, 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..21
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00842"
FT CHAIN 22..348
FT /note="Outer membrane protein A"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00842"
FT /id="PRO_5026396112"
FT DOMAIN 222..348
FT /note="OmpA-like"
FT /evidence="ECO:0000259|PROSITE:PS51123"
FT SITE 78
FT /note="Part of salt bridge gating mechanism"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00842"
FT SITE 176
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 348 AA; 37594 MW; 23F69BA834EDE962 CRC64;
MKKTAIALTI VALAVASVAQ AVPQPNTFYV GAKAGWASFH DGLNQIEYKS KTSFGSKRNS
VTYGVFGGYQ ITDNFAVELG YDDFGRAKVR ANSKTTAFDA AKHTNHGTHL SLKASYPLLD
GLDVYARVGA ALIRSDYKLY APLINKRLSP HFKITQVSPV FAGGLEYAFI PELTLRVEYQ
WVNNVGKFEY ADGQYADFRP DIGSVTAGLS YRFGQSVYVP EVVSKTFTLN TDVTFGFDKA
DLKPAAQNVL DGIYGEIAQL KSASVAVAGY TDRLGSDAYN LKLSQRRADT VANYLVAKGV
AQNAISATGH GEANPVTGNK CDSVKGRKAL IACLADDRRV EIPVKGNK
//
