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LIVH_ECO57
ID   LIVH_ECO57              Reviewed;         308 AA.
AC   P0AEX8; P08340;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=High-affinity branched-chain amino acid transport system permease protein LivH;
DE   AltName: Full=LIV-I protein H;
GN   Name=livH; OrderedLocusNames=Z4827, ECs4304;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Part of the binding-protein-dependent transport system for
CC       branched-chain amino acids. Probably responsible for the translocation
CC       of the substrates across the membrane (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC       permease family. LivHM subfamily. {ECO:0000305}.
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DR   EMBL; AE005174; AAG58564.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB37727.1; -; Genomic_DNA.
DR   PIR; H86012; H86012.
DR   PIR; H91166; H91166.
DR   RefSeq; NP_312331.1; NC_002695.1.
DR   RefSeq; WP_001295111.1; NZ_SWKA01000005.1.
DR   AlphaFoldDB; P0AEX8; -.
DR   STRING; 155864.EDL933_4667; -.
DR   EnsemblBacteria; AAG58564; AAG58564; Z4827.
DR   EnsemblBacteria; BAB37727; BAB37727; ECs_4304.
DR   GeneID; 67417084; -.
DR   GeneID; 915841; -.
DR   KEGG; ece:Z4827; -.
DR   KEGG; ecs:ECs_4304; -.
DR   PATRIC; fig|386585.9.peg.4496; -.
DR   eggNOG; COG0559; Bacteria.
DR   HOGENOM; CLU_039929_3_1_6; -.
DR   OMA; NMGWFLI; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0006865; P:amino acid transport; IEA:UniProtKB-KW.
DR   InterPro; IPR001851; ABC_transp_permease.
DR   Pfam; PF02653; BPD_transp_2; 1.
PE   3: Inferred from homology;
KW   Amino-acid transport; Cell inner membrane; Cell membrane; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..308
FT                   /note="High-affinity branched-chain amino acid transport
FT                   system permease protein LivH"
FT                   /id="PRO_0000060059"
FT   TOPO_DOM        1..21
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        22..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        43..45
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        46..66
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        67..68
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        69..89
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        90..104
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        105..125
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        126..154
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        155..175
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        176..203
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        204..224
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        225..245
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        246..266
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        267..280
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        281..301
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        302..308
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   308 AA;  32982 MW;  8C8A4BD56718A4BE CRC64;
     MSEQFLYFLQ QMFNGVTLGS TYALIAIGYT MVYGIIGMIN FAHGEVYMIG SYVSFMIIAA
     LMMMGIDTGW LLVAAGFVGA IVIASAYGWS IERVAYRPVR NSKRLIALIS AIGMSIFLQN
     YVSLTEGSRD VALPSLFNGQ WVVGHSENFS ASITTMQAVI WIVTFLAMLA LTIFIRYSRM
     GRACRACAED LKMASLLGIN TDRVIALTFV IGAAMAAVAG VLLGQFYGVI NPYIGFMAGM
     KAFTAAVLGG IGSIPGAMIG GLILGIAEAL SSAYLSTEYK DVVSFALLIL VLLVMPTGIL
     GRPEVEKV
 
 
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