OMPA_SHIFL
ID OMPA_SHIFL Reviewed; 348 AA.
AC A0A2S4N3N0; Q7UD17; Q83RX2;
DT 05-JUN-2019, integrated into UniProtKB/Swiss-Prot.
DT 18-JUL-2018, sequence version 1.
DT 03-AUG-2022, entry version 23.
DE RecName: Full=Outer membrane protein A {ECO:0000255|HAMAP-Rule:MF_00842};
DE AltName: Full=Outer membrane porin A {ECO:0000255|HAMAP-Rule:MF_00842};
DE Flags: Precursor;
GN Name=ompA {ECO:0000255|HAMAP-Rule:MF_00842}; OrderedLocusNames=SF0957;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP SUBUNIT (MICROBIAL INFECTION), SUBCELLULAR LOCATION (MICROBIAL INFECTION),
RP AND DISRUPTION PHENOTYPE.
RC STRAIN=PE577 / Serotype 2a;
RX PubMed=22386055; DOI=10.1016/j.virol.2012.01.040;
RA Parent K.N., Gilcrease E.B., Casjens S.R., Baker T.S.;
RT "Structural evolution of the P22-like phages: comparison of Sf6 and P22
RT procapsid and virion architectures.";
RL Virology 427:177-188(2012).
RN [3]
RP FUNCTION (MICROBIAL INFECTION), AND DISRUPTION PHENOTYPE.
RC STRAIN=PE577 / Serotype 2a;
RX PubMed=24673644; DOI=10.1111/mmi.12536;
RA Parent K.N., Erb M.L., Cardone G., Nguyen K., Gilcrease E.B., Porcek N.B.,
RA Pogliano J., Baker T.S., Casjens S.R.;
RT "OmpA and OmpC are critical host factors for bacteriophage Sf6 entry in
RT Shigella.";
RL Mol. Microbiol. 92:47-60(2014).
RN [4] {ECO:0007744|PDB:3NB3}
RP STRUCTURE BY ELECTRON MICROSCOPY (19.00 ANGSTROMS), PROTEIN SEQUENCE OF
RP 22-26, IDENTIFICATION BY MASS SPECTROMETRY, AND SUBUNIT (MICROBIAL
RP INFECTION).
RC STRAIN=M94;
RX PubMed=21071053; DOI=10.1016/j.virol.2010.10.030;
RA Zhao H., Sequeira R.D., Galeva N.A., Tang L.;
RT "The host outer membrane proteins OmpA and OmpC are associated with the
RT Shigella phage Sf6 virion.";
RL Virology 409:319-327(2011).
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:0000255|HAMAP-
CC Rule:MF_00842}.
CC -!- FUNCTION: Required for conjugation with F-type plasmids; probably
CC serves as the mating receptor on recipient cells. {ECO:0000255|HAMAP-
CC Rule:MF_00842}.
CC -!- FUNCTION: (Microbial infection) Serves as a secondary receptor during
CC phage Sf6 infection; infection requires both lipopolysaccharide (LPS)
CC and the OmpA beta-barrel. {ECO:0000269|PubMed:24673644}.
CC -!- SUBUNIT: Monomer and homodimer. {ECO:0000255|HAMAP-Rule:MF_00842}.
CC -!- SUBUNIT: (Microbial infection) Upon infection with phage Sf6 associates
CC with the mature bacteriophage capsid (PubMed:21071053,
CC PubMed:22386055). Was originally suggested to be within the
CC bacteriophage capsid (PubMed:21071053). This has been disproven
CC (PubMed:22386055). {ECO:0000269|PubMed:21071053,
CC ECO:0000269|PubMed:22386055}.
CC -!- SUBCELLULAR LOCATION: Extracellular vesicle. Note=(Microbial infection)
CC Upon infection with phage Sf6 is found in extracellular vesicles that
CC associate with the tails of mature phage particles.
CC {ECO:0000269|PubMed:22386055}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane
CC {ECO:0000250|UniProtKB:P0A910, ECO:0000255|HAMAP-Rule:MF_00842}; Multi-
CC pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00842,
CC ECO:0000305|PubMed:21071053}.
CC -!- DOMAIN: The extracellular loops are most variable in sequence, and in
CC some bacteria confer sensitivity to phage and/or colicins.
CC {ECO:0000255|HAMAP-Rule:MF_00842}.
CC -!- DISRUPTION PHENOTYPE: No effect on propagation of phage Sf6
CC (PubMed:22386055). Upon infection with phage Sf6, single deletion
CC mutant has a wild-type level of small plaques but a better than wild-
CC type survival level; double ompA-ompC deletions have about 10-fold
CC fewer plaques and survive infection considerably better than wild-type,
CC are infected more slowly and have fewer extracellular vesicles
CC associated with mature bacteriophage (PubMed:24673644).
CC {ECO:0000269|PubMed:22386055, ECO:0000269|PubMed:24673644}.
CC -!- SIMILARITY: Belongs to the outer membrane OOP (TC 1.B.6) superfamily.
CC OmpA family. {ECO:0000255|HAMAP-Rule:MF_00842}.
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DR EMBL; AE005674; AAN42586.2; -; Genomic_DNA.
DR RefSeq; NP_706879.2; NC_004337.2.
DR RefSeq; WP_005047463.1; NZ_WPGW01000054.1.
DR PDB; 3NB3; EM; -; A/B/C=1-346.
DR PDBsum; 3NB3; -.
DR AlphaFoldDB; A0A2S4N3N0; -.
DR SMR; A0A2S4N3N0; -.
DR STRING; 198214.SF0957; -.
DR EnsemblBacteria; AAN42586; AAN42586; SF0957.
DR GeneID; 1023906; -.
DR GeneID; 58390353; -.
DR KEGG; sfl:SF0957; -.
DR PATRIC; fig|198214.7.peg.1115; -.
DR HOGENOM; CLU_031536_0_0_6; -.
DR OMA; HDTGFYG; -.
DR OrthoDB; 583204at2; -.
DR Proteomes; UP000001006; 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:ion transmembrane transport; IEA:UniProtKB-UniRule.
DR CDD; cd07185; OmpA_C-like; 1.
DR Gene3D; 3.30.1330.60; -; 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 Pfam; PF00691; OmpA; 1.
DR Pfam; PF01389; OmpA_membrane; 1.
DR PRINTS; PR01021; OMPADOMAIN.
DR PRINTS; PR01022; OUTRMMBRANEA.
DR SUPFAM; SSF103088; SSF103088; 1.
DR SUPFAM; SSF56925; SSF56925; 1.
DR PROSITE; PS01068; OMPA_1; 1.
DR PROSITE; PS51123; OMPA_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell outer membrane; Conjugation; Direct protein sequencing;
KW Disulfide bond; Host-virus interaction; Ion transport; Membrane; Porin;
KW Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane beta strand; Transport.
FT SIGNAL 1..21
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00842,
FT ECO:0000269|PubMed:21071053"
FT CHAIN 22..348
FT /note="Outer membrane protein A"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT /id="PRO_0000447414"
FT TRANSMEM 27..37
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT TRANSMEM 55..66
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT TRANSMEM 70..78
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT TRANSMEM 96..107
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT TRANSMEM 112..120
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P0A910, ECO:0000255|HAMAP-
FT Rule:MF_00842"
FT TRANSMEM 146..155
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT TRANSMEM 160..167
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT TRANSMEM 186..194
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT REPEAT 205..206
FT /note="1"
FT REPEAT 207..208
FT /note="2"
FT REPEAT 209..210
FT /note="3"
FT DOMAIN 212..340
FT /note="OmpA-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT REGION 201..210
FT /note="Hinge-like"
FT /evidence="ECO:0000305"
FT REGION 205..210
FT /note="3 X 2 AA tandem repeats of A-P"
FT SITE 73
FT /note="Part of salt bridge gating mechanism"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT SITE 163
FT /note="Part of salt bridge gating mechanism"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT DISULFID 313..325
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
SQ SEQUENCE 348 AA; 37283 MW; 42623C67041D62F4 CRC64;
MKKTAIAIAV ALAGFATVAQ AAPKDNTWYT GAKLGWSQYH DTGFIPNNGP THENQLGAGA
FGGYQVNPYV GFEMGYDWLG RMPYKGDNIN GAYKAQGVQL TAKLGYPITD DLDIYTRLGG
MVWRADTKAN VPGGASFKDH DTGVSPVFAG GVEYAITPEI ATRLEYQWTN NIGDANTIGT
RPDNGLLSLG VSYRFGQGEA APVVAPAPAP EVQTKHFTLK SDVLFNFNKA TLKPEGQAAL
DQLYSQLSNL DPKDGSVVVL GYTDRIGSDA YNQGLSERRA QSVVDYLISK GIPADKISAR
GMGESNPVTG NTCDNVKQRA ALIDCLAPDR RVEIEVKGIK DVVTQPQA
