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SSTT_PROMH
ID   SSTT_PROMH              Reviewed;         417 AA.
AC   B4EXQ1;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=Serine/threonine transporter SstT {ECO:0000255|HAMAP-Rule:MF_01582};
DE   AltName: Full=Na(+)/serine-threonine symporter {ECO:0000255|HAMAP-Rule:MF_01582};
GN   Name=sstT {ECO:0000255|HAMAP-Rule:MF_01582}; OrderedLocusNames=PMI3701;
OS   Proteus mirabilis (strain HI4320).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Proteus.
OX   NCBI_TaxID=529507;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HI4320;
RX   PubMed=18375554; DOI=10.1128/jb.01981-07;
RA   Pearson M.M., Sebaihia M., Churcher C., Quail M.A., Seshasayee A.S.,
RA   Luscombe N.M., Abdellah Z., Arrosmith C., Atkin B., Chillingworth T.,
RA   Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA   Rabbinowitsch E., Walker D., Whithead S., Thomson N.R., Rather P.N.,
RA   Parkhill J., Mobley H.L.T.;
RT   "Complete genome sequence of uropathogenic Proteus mirabilis, a master of
RT   both adherence and motility.";
RL   J. Bacteriol. 190:4027-4037(2008).
CC   -!- FUNCTION: Involved in the import of serine and threonine into the cell,
CC       with the concomitant import of sodium (symport system).
CC       {ECO:0000255|HAMAP-Rule:MF_01582}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-serine(in) + Na(+)(in) = L-serine(out) + Na(+)(out);
CC         Xref=Rhea:RHEA:29575, ChEBI:CHEBI:29101, ChEBI:CHEBI:33384;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01582};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:29577;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01582};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-threonine(in) + Na(+)(in) = L-threonine(out) + Na(+)(out);
CC         Xref=Rhea:RHEA:69999, ChEBI:CHEBI:29101, ChEBI:CHEBI:57926;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01582};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:70001;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01582};
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01582}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01582}.
CC   -!- SIMILARITY: Belongs to the dicarboxylate/amino acid:cation symporter
CC       (DAACS) (TC 2.A.23) family. {ECO:0000255|HAMAP-Rule:MF_01582}.
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DR   EMBL; AM942759; CAR47213.1; -; Genomic_DNA.
DR   RefSeq; WP_012368852.1; NC_010554.1.
DR   AlphaFoldDB; B4EXQ1; -.
DR   SMR; B4EXQ1; -.
DR   STRING; 529507.PMI3701; -.
DR   EnsemblBacteria; CAR47213; CAR47213; PMI3701.
DR   GeneID; 6801223; -.
DR   KEGG; pmr:PMI3701; -.
DR   PATRIC; fig|529507.6.peg.3622; -.
DR   eggNOG; COG3633; Bacteria.
DR   HOGENOM; CLU_044581_0_0_6; -.
DR   OMA; PVNLQLC; -.
DR   Proteomes; UP000008319; 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:0015171; F:amino acid transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0015293; F:symporter activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0032329; P:serine transport; IEA:InterPro.
DR   GO; GO:0015826; P:threonine transport; IEA:InterPro.
DR   Gene3D; 1.10.3860.10; -; 1.
DR   HAMAP; MF_01582; Ser_Thr_transp_SstT; 1.
DR   InterPro; IPR001991; Na-dicarboxylate_symporter.
DR   InterPro; IPR036458; Na:dicarbo_symporter_sf.
DR   InterPro; IPR023025; Ser_Thr_transp_SstT.
DR   PANTHER; PTHR42865; PTHR42865; 1.
DR   Pfam; PF00375; SDF; 1.
DR   SUPFAM; SSF118215; SSF118215; 1.
PE   3: Inferred from homology;
KW   Amino-acid transport; Cell inner membrane; Cell membrane; Membrane;
KW   Reference proteome; Symport; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..417
FT                   /note="Serine/threonine transporter SstT"
FT                   /id="PRO_1000197555"
FT   TRANSMEM        21..41
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01582"
FT   TRANSMEM        49..69
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01582"
FT   TRANSMEM        83..103
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01582"
FT   TRANSMEM        142..162
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01582"
FT   TRANSMEM        193..213
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01582"
FT   TRANSMEM        218..238
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01582"
FT   TRANSMEM        291..311
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01582"
FT   TRANSMEM        331..351
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01582"
SQ   SEQUENCE   417 AA;  43878 MW;  EFDA4FB328F1235C CRC64;
     MDKQQSRVLN LLFQGSLVKQ ILAGLIAGIL LAWLAPEVAK MMSLLGNLFI SALKAVAPVL
     VWVLVMASIA NHRQGQKTSI RPILVLYLLA TFFAALTAVV ASFVFPSVLT LVVNDSQLSP
     PENIAEVLKG VLINVVANPV DALINGNYMG ILAWAIGLGL ALRHASDTTK ALTQDFADAV
     TNLVRVVIRL APIGIFGLVS STIATTGFKA LAGYLHVLLV LIGCMLFVAL VVNPLIVFWK
     IRRNPYPLVW ACLRESGVTA FFTRSSAANI PVNMAMCRRM NLNEDTYSVS IPLGATINMG
     GAAITITILT LAAVNTLGMP VDIPTALLLS LVAAICACGA SGVAGGSLLL IPLACSMFGI
     SNDLAMQVVA VGVMIGVLQD SAETALNSST DVLFTATVCI AEDERLVANP LTEKNNG
 
 
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