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OMPA_KLEAE
ID   OMPA_KLEAE              Reviewed;         350 AA.
AC   P09146;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   03-AUG-2022, entry version 109.
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};
OS   Klebsiella aerogenes (Enterobacter aerogenes).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=548;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6363059; DOI=10.1111/j.1432-1033.1983.tb07853.x;
RA   Braun G., Cole S.T.;
RT   "Molecular characterization of the gene coding for major outer membrane
RT   protein OmpA from Enterobacter aerogenes.";
RL   Eur. J. Biochem. 137:495-500(1983).
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   -!- 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; X00254; CAA25062.1; -; Genomic_DNA.
DR   PIR; S07222; S07222.
DR   AlphaFoldDB; P09146; -.
DR   SMR; P09146; -.
DR   STRING; 548.EAG7_02416; -.
DR   PRIDE; P09146; -.
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; Conjugation; Disulfide bond; Ion transport; Membrane;
KW   Porin; Repeat; Signal; Transmembrane; Transmembrane beta strand; Transport.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT   CHAIN           22..350
FT                   /note="Outer membrane protein A"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT                   /id="PRO_0000020096"
FT   TRANSMEM        27..37
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT   TRANSMEM        59..70
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT   TRANSMEM        74..82
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT   TRANSMEM        100..111
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT   TRANSMEM        116..124
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000255|HAMAP-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   REPEAT          211..212
FT                   /note="4"
FT   DOMAIN          214..342
FT                   /note="OmpA-like"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT   REGION          205..212
FT                   /note="4 X 2 AA tandem repeats of A-P"
FT   SITE            77
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        315..327
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
SQ   SEQUENCE   350 AA;  37575 MW;  6276C6F2F21065DA CRC64;
     MKKTAIAIAV ALAGFATVAQ AAPKDNTWYA GGKLGWSQFH DTGWYNSNLN NNGPTHESQL
     GAGAFGGYQV NPYLGFEMGY DWLGRMPYKG VKVNGAFSSQ AVQLTAKLGY PITDDLDIYT
     RLGGMVWRAD SSNSIAGDNH DTGVSPVFAG GVEWAMTRDI ATRLEYQWVN NIGDAGTVGV
     RPDNGMLSVG VSYRFGQEDN APVVAPAPAP APEVTTKTFT LKSDVLFNFN KATLKPEGQQ
     ALDQLYTQLS NMDPKDGSAV VLGYTDRIGS EQYNQKLSEK RAQSVVDYLV AKGIPANKIS
     ARGMGESDPV TGNTCDNVKA RAALIDCLAP DRRVAIEVKG YKDVVTQPQA
 
 
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