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OMPA_BUCAP
ID   OMPA_BUCAP              Reviewed;         347 AA.
AC   Q8K9L4;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 116.
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=BUsg_320;
OS   Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=198804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sg;
RX   PubMed=12089438; DOI=10.1126/science.1071278;
RA   Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA   Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT   "50 million years of genomic stasis in endosymbiotic bacteria.";
RL   Science 296:2376-2379(2002).
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; AE013218; AAM67874.1; -; Genomic_DNA.
DR   RefSeq; WP_011053841.1; NC_004061.1.
DR   AlphaFoldDB; Q8K9L4; -.
DR   SMR; Q8K9L4; -.
DR   STRING; 198804.BUsg_320; -.
DR   EnsemblBacteria; AAM67874; AAM67874; BUsg_320.
DR   KEGG; bas:BUsg_320; -.
DR   eggNOG; COG2885; Bacteria.
DR   eggNOG; COG3637; Bacteria.
DR   HOGENOM; CLU_031536_0_0_6; -.
DR   OMA; LMNTYPQ; -.
DR   OrthoDB; 583204at2; -.
DR   Proteomes; UP000000416; 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   Signal; Transmembrane; Transmembrane beta strand; Transport.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT   CHAIN           22..347
FT                   /note="Outer membrane protein A"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT                   /id="PRO_0000020106"
FT   TRANSMEM        26..36
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..347
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   347 AA;  39950 MW;  55D23E2AF7D5A887 CRC64;
     MKKQALTIIF LLVSLVTGIQ AKENDHWYLG TKMGWSDFNI LEYRSKDITP FDTKIDTKNP
     LGAPVFGLFL GYEFNPYFSF EIENDTTGFS PHLIFQKNEQ NIQINSLQLA TKLSYPITDD
     FHIYTQLGGM MFWDNLSFKK DLQNIFTEKS RLIPNVSLGA EYIFNKKFIT RLDYTWKSNI
     AKIMNLSMKP VLGDVALSFG WKFGKSNINE IFSSYIPQSS DKQYVALNEN INFPFNSTEL
     KPISHDKLQK LQKEIKNIKS KNIFIMLSGH ADRIGNKEYN QKLSENRAYS IKNYFTSHGI
     SQDKISIQGM GNEFSLTNQI CKDVSDRPLL ISCLAPDRRV EIEVLSD
 
 
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