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OPPB_ECOLI
ID   OPPB_ECOLI              Reviewed;         306 AA.
AC   P0AFH2; P31132; P76026; P77550;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Oligopeptide transport system permease protein OppB;
GN   Name=oppB; OrderedLocusNames=b1244, JW1236;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA   Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA   Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA   Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA   Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA   Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA   Wada C., Yamamoto Y., Horiuchi T.;
RT   "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT   the 28.0-40.1 min region on the linkage map.";
RL   DNA Res. 3:363-377(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16.
RX   PubMed=2187863; DOI=10.1016/s0021-9258(19)38898-2;
RA   Kashiwagi K., Yamaguchi Y., Sakai Y., Kobayashi H., Igarashi K.;
RT   "Identification of the polyamine-induced protein as a periplasmic
RT   oligopeptide binding protein.";
RL   J. Biol. Chem. 265:8387-8391(1990).
RN   [5]
RP   TOPOLOGY [LARGE SCALE ANALYSIS].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=15919996; DOI=10.1126/science.1109730;
RA   Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT   "Global topology analysis of the Escherichia coli inner membrane
RT   proteome.";
RL   Science 308:1321-1323(2005).
CC   -!- FUNCTION: Part of the binding-protein-dependent transport system for
CC       oligopeptides; probably responsible for the translocation of the
CC       substrate across the membrane.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC       permease family. OppBC subfamily. {ECO:0000305}.
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DR   EMBL; U00096; AAC74326.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA14776.1; -; Genomic_DNA.
DR   EMBL; J05433; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; G64871; B36263.
DR   RefSeq; NP_415760.1; NC_000913.3.
DR   RefSeq; WP_000911112.1; NZ_STEB01000005.1.
DR   AlphaFoldDB; P0AFH2; -.
DR   SMR; P0AFH2; -.
DR   BioGRID; 4261152; 281.
DR   ComplexPortal; CPX-4343; Murein tripeptide ABC transporter complex.
DR   ComplexPortal; CPX-4344; Oligopeptide ABC transporter complex.
DR   DIP; DIP-48074N; -.
DR   STRING; 511145.b1244; -.
DR   TCDB; 3.A.1.5.41; the atp-binding cassette (abc) superfamily.
DR   jPOST; P0AFH2; -.
DR   PaxDb; P0AFH2; -.
DR   PRIDE; P0AFH2; -.
DR   EnsemblBacteria; AAC74326; AAC74326; b1244.
DR   EnsemblBacteria; BAA14776; BAA14776; BAA14776.
DR   GeneID; 66674935; -.
DR   GeneID; 945823; -.
DR   KEGG; ecj:JW1236; -.
DR   KEGG; eco:b1244; -.
DR   PATRIC; fig|1411691.4.peg.1039; -.
DR   EchoBASE; EB0669; -.
DR   eggNOG; COG0601; Bacteria.
DR   InParanoid; P0AFH2; -.
DR   OMA; FLMVNVM; -.
DR   PhylomeDB; P0AFH2; -.
DR   BioCyc; EcoCyc:OPPB-MON; -.
DR   BioCyc; MetaCyc:OPPB-MON; -.
DR   PRO; PR:P0AFH2; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0055052; C:ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; IC:ComplexPortal.
DR   GO; GO:0016020; C:membrane; IC:ComplexPortal.
DR   GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR   GO; GO:0140205; P:oligopeptide import across plasma membrane; IC:ComplexPortal.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0140207; P:tripeptide import across plasma membrane; IC:ComplexPortal.
DR   CDD; cd06261; TM_PBP2; 1.
DR   Gene3D; 1.10.3720.10; -; 1.
DR   InterPro; IPR045621; BPD_transp_1_N.
DR   InterPro; IPR000515; MetI-like.
DR   InterPro; IPR035906; MetI-like_sf.
DR   Pfam; PF00528; BPD_transp_1; 1.
DR   Pfam; PF19300; BPD_transp_1_N; 1.
DR   SUPFAM; SSF161098; SSF161098; 1.
DR   PROSITE; PS50928; ABC_TM1; 1.
PE   1: Evidence at protein level;
KW   Cell inner membrane; Cell membrane; Membrane; Peptide transport;
KW   Protein transport; Reference proteome; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..306
FT                   /note="Oligopeptide transport system permease protein OppB"
FT                   /id="PRO_0000060143"
FT   TOPO_DOM        1..9
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:15919996"
FT   TRANSMEM        10..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   TOPO_DOM        31..99
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305|PubMed:15919996"
FT   TRANSMEM        100..121
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   TOPO_DOM        122..137
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:15919996"
FT   TRANSMEM        138..158
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   TOPO_DOM        159..172
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305|PubMed:15919996"
FT   TRANSMEM        173..190
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   TOPO_DOM        191..226
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:15919996"
FT   TRANSMEM        227..250
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   TOPO_DOM        251..271
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305|PubMed:15919996"
FT   TRANSMEM        272..293
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   TOPO_DOM        294..306
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:15919996"
FT   DOMAIN          94..293
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
SQ   SEQUENCE   306 AA;  33443 MW;  F74579B3F9EA4615 CRC64;
     MLKFILRRCL EAIPTLFILI TISFFMMRLA PGSPFTGERT LPPEVMANIE AKYHLNDPIM
     TQYFSYLKQL AHGDFGPSFK YKDYSVNDLV ASSFPVSAKL GAAAFFLAVI LGVSAGVIAA
     LKQNTKWDYT VMGLAMTGVV IPSFVVAPLL VMIFAIILHW LPGGGWNGGA LKFMILPMVA
     LSLAYIASIA RITRGSMIEV LHSNFIRTAR AKGLPMRRII LRHALKPALL PVLSYMGPAF
     VGIITGSMVI ETIYGLPGIG QLFVNGALNR DYSLVLSLTI LVGALTILFN AIVDVLYAVI
     DPKIRY
 
 
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