ID W0Q5Z2_9PAST Unreviewed; 359 AA.
AC W0Q5Z2;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
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 ORFNames=X781_21690 {ECO:0000313|EMBL:AHG74314.1};
OS Mannheimia sp. USDA-ARS-USMARC-1261.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Mannheimia.
OX NCBI_TaxID=1432056 {ECO:0000313|EMBL:AHG74314.1, ECO:0000313|Proteomes:UP000019094};
RN [1] {ECO:0000313|EMBL:AHG74314.1, ECO:0000313|Proteomes:UP000019094}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=USDA-ARS-USMARC-1261 {ECO:0000313|EMBL:AHG74314.1,
RC ECO:0000313|Proteomes:UP000019094};
RX PubMed=24526648;
RA Harhay G.P., Murray R.W., Lubbers B., Griffin D., Koren S., Phillippy A.M.,
RA Harhay D.M., Bono J., Clawson M.L., Heaton M.P., Chitko-McKown C.G.,
RA Smith T.P.;
RT "Complete Closed Genome Sequences of Four Mannheimia varigena Isolates from
RT Cattle with Shipping Fever.";
RL Genome Announc. 2:e00088-14(2014).
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; CP006942; AHG74314.1; -; Genomic_DNA.
DR RefSeq; WP_025236848.1; NZ_CP006942.1.
DR AlphaFoldDB; W0Q5Z2; -.
DR STRING; 1432056.X781_21690; -.
DR KEGG; mvr:X781_21690; -.
DR PATRIC; fig|1432056.3.peg.2165; -.
DR eggNOG; COG2885; Bacteria.
DR eggNOG; COG3637; Bacteria.
DR HOGENOM; CLU_031536_0_0_6; -.
DR OrthoDB; 1149075at2; -.
DR Proteomes; UP000019094; 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; 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; PS51123; OMPA_2; 1.
PE 3: Inferred from homology;
KW Cell outer membrane {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..19
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00842"
FT CHAIN 20..359
FT /note="Outer membrane protein A"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00842"
FT /id="PRO_5026399921"
FT DOMAIN 227..355
FT /note="OmpA-like"
FT /evidence="ECO:0000259|PROSITE:PS51123"
FT SITE 82
FT /note="Part of salt bridge gating mechanism"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00842"
FT SITE 172
FT /note="Part of salt bridge gating mechanism"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00842"
FT DISULFID 328..340
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00842"
SQ SEQUENCE 359 AA; 38249 MW; BB560E71597B229F CRC64;
MKKTLVALAV LSTAAVAQAA PQANTFYAGA KAGWASFHDG LTQFDAKDNK GEGFGINRNS
VTYGVFGGYQ ILNQNNVGLA VELGYDYFGR VRGNEGEDKA IKHVAHGTHL SLKPSYEVAP
NLDVYGKVGA ALVRNDYKGY NGYKDQRAHN LKTSLLLGAG LEYAITPELA ARVEYQYLQA
AGNLDKARQK ANLDWIDAQY SPKIHSVSAG LTYRFGQGAA PVEAPEVVTK NFAFSSDVLF
DFAKSSLKPA AATALDAAHT EISNLGLANP AIQVNGYTDR IGKDAANLKL SQRRAETVAN
YIVSKGANPA NVTAVGYGEA NPVTGNTCDA VKGRKALIAC LAPDRRVEIQ VQGSKEVTM
//
