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OMPA_BUCAI
ID   OMPA_BUCAI              Reviewed;         349 AA.
AC   P57414;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 1.
DT   25-MAY-2022, entry version 114.
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=BU332;
OS   Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS   pisum symbiotic bacterium).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=107806;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=APS;
RX   PubMed=10993077; DOI=10.1038/35024074;
RA   Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT   "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT   sp. APS.";
RL   Nature 407:81-86(2000).
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   -!- SUBUNIT: Monomer and homodimer. {ECO:0000255|HAMAP-Rule:MF_00842}.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00842}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_00842}.
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   -!- 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; BA000003; BAB13037.1; -; Genomic_DNA.
DR   RefSeq; NP_240151.1; NC_002528.1.
DR   RefSeq; WP_010896071.1; NC_002528.1.
DR   AlphaFoldDB; P57414; -.
DR   SMR; P57414; -.
DR   STRING; 107806.10039003; -.
DR   EnsemblBacteria; BAB13037; BAB13037; BAB13037.
DR   KEGG; buc:BU332; -.
DR   PATRIC; fig|107806.10.peg.342; -.
DR   eggNOG; COG2885; Bacteria.
DR   eggNOG; COG3637; Bacteria.
DR   HOGENOM; CLU_031536_0_0_6; -.
DR   OMA; HDTGFYG; -.
DR   Proteomes; UP000001806; 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   3: Inferred from homology;
KW   Cell outer membrane; Disulfide bond; Ion transport; Membrane; Porin;
KW   Reference proteome; Signal; Transmembrane; Transmembrane beta strand;
KW   Transport.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT   CHAIN           23..349
FT                   /note="Outer membrane protein A"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT                   /id="PRO_0000020105"
FT   TRANSMEM        27..37
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT   TRANSMEM        63..74
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT   TRANSMEM        78..86
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT   TRANSMEM        105..116
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT   TRANSMEM        121..129
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT   TRANSMEM        154..163
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT   TRANSMEM        168..175
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT   TRANSMEM        194..202
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT   DOMAIN          220..348
FT                   /note="OmpA-like"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT   REGION          207..218
FT                   /note="Hinge-like"
FT   SITE            81
FT                   /note="Part of salt bridge gating mechanism"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT   SITE            171
FT                   /note="Part of salt bridge gating mechanism"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT   DISULFID        321..333
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
SQ   SEQUENCE   349 AA;  39303 MW;  CC14AB1BD590CF58 CRC64;
     MKKRALAIAF LLASLIPSAA QAEEENGWYL GAKFGWSHFN PLKYDMNNSQ VNNNDSSIEN
     LSAPIVGLFL GYEFNPYFSL EIENDTNGFF PHLIFQKNNE HIQSNSVQLA TKLSYPITDE
     FHLYTKLGGI VSWNDLSSKN TLKNLFSKES ALLPSLSLGA EYIFNETFIT RLDYTWKNSV
     KNIANASIKP ALGDAVLSIG WKFGKSDISD MFSSDDSEPL NEQYSVLNEN INFPFNSTEL
     KPSSYDKLNK LDDDIKDMQL KNVSIVLLGH ADKIGSDEYN QKLSEDRAYS IKNYLASRGF
     SRDKITVKGM GKLYPLTNQV CRDVVNKPLL ISCLAPDRRV EIEVLSDVQ
 
 
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