ID A0A0F7HET2_SERFO Unreviewed; 352 AA.
AC A0A0F7HET2;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 45.
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:VEI68030.1};
GN ORFNames=CRN79_00390 {ECO:0000313|EMBL:ATM74393.1}, NCTC13193_02162
GN {ECO:0000313|EMBL:VEI68030.1}, WN53_18040
GN {ECO:0000313|EMBL:AKG70876.1};
OS Serratia fonticola.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=47917 {ECO:0000313|EMBL:AKG70876.1, ECO:0000313|Proteomes:UP000034699};
RN [1] {ECO:0000313|EMBL:AKG70876.1, ECO:0000313|Proteomes:UP000034699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 4576 {ECO:0000313|EMBL:AKG70876.1,
RC ECO:0000313|Proteomes:UP000034699};
RA Chan K.-G., Ee R.;
RT "Complete Genome Sequencing of Serratia Fonticola DSM-4576.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ATM74393.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FDAARGOS_411 {ECO:0000313|EMBL:ATM74393.1};
RA Minogue T., Wolcott M., Wasieloski L., Aguilar W., Moore D., Tallon L.J.,
RA Sadzewicz L., Ott S., Zhao X., Nagaraj S., Vavikolanu K., Aluvathingal J.,
RA Nadendla S., Sichtig H.;
RT "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS):
RT Supporting development and validation of Infectious Disease Dx tests.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ATM74393.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FDAARGOS_411 {ECO:0000313|EMBL:ATM74393.1};
RA Goldberg B., Campos J., Tallon L., Sadzewicz L., Ott S., Zhao X.,
RA Nagaraj S., Vavikolanu K., Aluvathingal J., Nadendla S., Geyer C.,
RA Sichtig H.;
RT "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS):
RT Supporting development and validation of Infectious Disease Dx tests.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:VEI68030.1, ECO:0000313|Proteomes:UP000270487}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC13193 {ECO:0000313|EMBL:VEI68030.1,
RC ECO:0000313|Proteomes:UP000270487};
RG Pathogen Informatics;
RL Submitted (DEC-2018) 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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00842}.
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DR EMBL; CP011254; AKG70876.1; -; Genomic_DNA.
DR EMBL; CP023956; ATM74393.1; -; Genomic_DNA.
DR EMBL; LR134492; VEI68030.1; -; Genomic_DNA.
DR RefSeq; WP_024485662.1; NZ_SUPV01000022.1.
DR AlphaFoldDB; A0A0F7HET2; -.
DR STRING; 47917.AV650_13500; -.
DR GeneID; 30322083; -.
DR KEGG; sfw:WN53_18040; -.
DR PATRIC; fig|47917.8.peg.3733; -.
DR Proteomes; UP000034699; Chromosome.
DR Proteomes; UP000221800; Chromosome.
DR Proteomes; UP000270487; Chromosome 1.
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}; Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
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:UP000034699};
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..21
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00842"
FT CHAIN 22..352
FT /note="Outer membrane protein A"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00842"
FT /id="PRO_5002516162"
FT DOMAIN 214..344
FT /note="OmpA-like"
FT /evidence="ECO:0000259|PROSITE:PS51123"
FT SITE 77
FT /note="Part of salt bridge gating mechanism"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00842"
FT SITE 163
FT /note="Part of salt bridge gating mechanism"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00842"
SQ SEQUENCE 352 AA; 37365 MW; 4A748052884652C4 CRC64;
MKKTAIALAV ALAGFATVAQ AAPKDDTWYT GAKLGWSQFH DTGFYGNGYT VDNDARKDQI
GAGAFVGYQA NQYLGFEMGY DWLGRMKYTG ANTGSFKAQG VQLAAKLSYP IMNDLDIYTR
LGGMVWRADS DGAGSNGGNH DTGVSPLAAV GVEYALNRDW ATRLDYQWVN NIGDAGTVGA
RPDNGMLSVG VSYRFGQEVA APVVAPAPAP APVVETKKFT LTSDVLFAFN KATLKPEGQQ
ALDQLYTQLS SLDPKDGSVV VLGFTDAVGS AEYNLRLSEQ RAQSVVDYLV SKGIPSDKIS
ARGMGKANPV TGDSCGYRSG RATAAQIACL APDRRVEIEV KGIKEVVSQP QG
//
