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LIVJ_SALTY
ID   LIVJ_SALTY              Reviewed;         365 AA.
AC   P17215;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Leu/Ile/Val/Thr-binding protein;
DE            Short=LIVT-BP;
DE   Flags: Precursor;
GN   Name=livJ; Synonyms=livB; OrderedLocusNames=STM3567;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 23-36.
RC   STRAIN=LT2;
RX   PubMed=2193932; DOI=10.1093/oxfordjournals.jbchem.a123026;
RA   Ohnishi K., Nakazima A., Matsubara K., Kiritani K.;
RT   "Cloning and nucleotide sequences of livB and livC, the structural genes
RT   encoding binding proteins of the high-affinity branched-chain amino acid
RT   transport in Salmonella typhimurium.";
RL   J. Biochem. 107:202-208(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
CC   -!- FUNCTION: This protein is a component of the leucine, isoleucine,
CC       valine, threonine transport system, which is one of the two periplasmic
CC       binding protein-dependent transport systems of the high-affinity
CC       transport of the branched-chain amino acids. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the leucine-binding protein family.
CC       {ECO:0000305}.
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DR   EMBL; D00478; BAA00369.1; -; Genomic_DNA.
DR   EMBL; AE006468; AAL22427.1; -; Genomic_DNA.
DR   PIR; JU0128; JU0128.
DR   RefSeq; NP_462468.1; NC_003197.2.
DR   RefSeq; WP_000676957.1; NC_003197.2.
DR   AlphaFoldDB; P17215; -.
DR   SMR; P17215; -.
DR   STRING; 99287.STM3567; -.
DR   PaxDb; P17215; -.
DR   EnsemblBacteria; AAL22427; AAL22427; STM3567.
DR   GeneID; 1255090; -.
DR   KEGG; stm:STM3567; -.
DR   PATRIC; fig|99287.12.peg.3770; -.
DR   HOGENOM; CLU_027128_6_0_6; -.
DR   OMA; MEFTGAR; -.
DR   PhylomeDB; P17215; -.
DR   BioCyc; SENT99287:STM3567-MON; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0006865; P:amino acid transport; IEA:UniProtKB-KW.
DR   InterPro; IPR028081; Leu-bd.
DR   InterPro; IPR000709; Leu_Ile_Val-bd.
DR   InterPro; IPR028082; Peripla_BP_I.
DR   Pfam; PF13458; Peripla_BP_6; 1.
DR   PRINTS; PR00337; LEUILEVALBP.
DR   SUPFAM; SSF53822; SSF53822; 1.
PE   1: Evidence at protein level;
KW   Amino-acid transport; Direct protein sequencing; Disulfide bond; Periplasm;
KW   Reference proteome; Signal; Transport.
FT   SIGNAL          1..21
FT   CHAIN           22..365
FT                   /note="Leu/Ile/Val/Thr-binding protein"
FT                   /id="PRO_0000017701"
FT   DISULFID        74..99
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   365 AA;  38787 MW;  5465154B6B4D9566 CRC64;
     MKGKTLLAGC IALSLSHMAF ADDIKVAVVG AMSGPVAQYG DQEFTGAEQA IADINAKGGI
     KGDKLVAVKY DDACDPKQAV AVANKVVNDG IKYVIGHLCS SSTQPASDIY EDEGILMITP
     AATAPELTAR GYKLVLRTTG LDSDQGPTAA KYILEKVKPQ RIAIIHDKQQ YGEGLARAVQ
     DGLKKGGVNV VFFDGITAGE KDFSTLVARL KKENIDFVYY GGYHPEMGQI LRQSRAAGLK
     TQFMGPEGVA NVSLSNIAGE SAEGLLVTKP KNYDQVPANK PIVDAIKAKK QDPSGAFVWT
     TYAALQSLQA GLNHSDDPAE IAKYLKGATV DTVMGPLSWD EKGDLKGFEF GVFDWHANGT
     ATDAK
 
 
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