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LIVH_SALTI
ID   LIVH_SALTI              Reviewed;         308 AA.
AC   P0A2J2; P30295;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=High-affinity branched-chain amino acid transport system permease protein LivH;
DE   AltName: Full=LIV-I protein H;
GN   Name=livH; Synonyms=livA; OrderedLocusNames=STY4249, t3959;
OS   Salmonella typhi.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=90370;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CT18;
RX   PubMed=11677608; DOI=10.1038/35101607;
RA   Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA   Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA   Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA   Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA   Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA   Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA   Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA   Barrell B.G.;
RT   "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT   serovar Typhi CT18.";
RL   Nature 413:848-852(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700931 / Ty2;
RX   PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA   Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA   Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT   "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT   CT18.";
RL   J. Bacteriol. 185:2330-2337(2003).
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; AL513382; CAD08067.1; -; Genomic_DNA.
DR   EMBL; AE014613; AAO71429.1; -; Genomic_DNA.
DR   RefSeq; NP_458357.1; NC_003198.1.
DR   RefSeq; WP_000003007.1; NZ_WSUR01000001.1.
DR   AlphaFoldDB; P0A2J2; -.
DR   STRING; 220341.16505046; -.
DR   EnsemblBacteria; AAO71429; AAO71429; t3959.
DR   KEGG; stt:t3959; -.
DR   KEGG; sty:STY4249; -.
DR   PATRIC; fig|220341.7.peg.4339; -.
DR   eggNOG; COG0559; Bacteria.
DR   HOGENOM; CLU_039929_3_1_6; -.
DR   OMA; NMGWFLI; -.
DR   Proteomes; UP000000541; Chromosome.
DR   Proteomes; UP000002670; 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   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_0000060060"
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..70
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        71..91
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        92..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..246
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        247..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;  32990 MW;  1E177EF797D47330 CRC64;
     MSEQFLYFLQ QMFNGVTLGS TYALIAIGYT MVYGIIGMIN FAHGEVYMIG SYVSFMIIAA
     LMMMGIDTSW LLVAAGFIGA IIIASAYGWS IERVAYRPVR NSKRLIALIS AIGMSIFLQN
     YVSLTEGSRD VALPSLFNGQ WIVGSSENFS ASITTMQAVI WIVTFLAMLA LTIFIRYSRM
     GRACRACAED LKMASLLGIN TDRVIALTFV IGAAMAAVAG VLLGQFYGVI NPYIGFMAGM
     KAFTAAVLGG IGSIPGAMIG GLILGVAEAL SSAYLSTEYK DVVSFALLIL VLLVMPTGIL
     GRPEVEKV
 
 
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