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PTLA_STRMU
ID   PTLA_STRMU              Reviewed;         104 AA.
AC   P26426;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   03-AUG-2022, entry version 136.
DE   RecName: Full=PTS system lactose-specific EIIA component {ECO:0000303|PubMed:6480107};
DE   AltName: Full=EIIA-Lac {ECO:0000303|PubMed:6480107};
DE   AltName: Full=EIII-Lac {ECO:0000303|PubMed:6480107};
DE   AltName: Full=Lactose-specific phosphotransferase enzyme IIA component {ECO:0000303|PubMed:6480107};
GN   Name=lacF {ECO:0000303|PubMed:6480107}; OrderedLocusNames=SMU_1492;
OS   Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=210007;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1400164; DOI=10.1128/jb.174.19.6159-6170.1992;
RA   Rosey E.L., Stewart G.C.;
RT   "Nucleotide and deduced amino acid sequences of the lacR, lacABCD, and
RT   lacFE genes encoding the repressor, tagatose 6-phosphate gene cluster, and
RT   sugar-specific phosphotransferase system components of the lactose operon
RT   of Streptococcus mutans.";
RL   J. Bacteriol. 174:6159-6170(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700610 / UA159;
RX   PubMed=12397186; DOI=10.1073/pnas.172501299;
RA   Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA   Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA   Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT   "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT   pathogen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
RN   [3]
RP   FUNCTION.
RC   STRAIN=ATCC 27352;
RX   PubMed=6480107; DOI=10.1128/iai.46.1.213-219.1984;
RA   Vadeboncoeur C., Proulx M.;
RT   "Lactose transport in Streptococcus mutans: isolation and characterization
RT   of factor IIIlac, a specific protein component of the phosphoenolpyruvate-
RT   lactose phosphotransferase system.";
RL   Infect. Immun. 46:213-219(1984).
CC   -!- FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase
CC       system (sugar PTS), a major carbohydrate active transport system,
CC       catalyzes the phosphorylation of incoming sugar substrates
CC       concomitantly with their translocation across the cell membrane. The
CC       enzyme II LacEF PTS system is involved in lactose transport.
CC       {ECO:0000305|PubMed:6480107}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P23532};
CC       Note=Binds 1 Mg(2+) ion per trimer. {ECO:0000250|UniProtKB:P23532};
CC   -!- SUBUNIT: Homotrimer. {ECO:0000250|UniProtKB:P0A0D6}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- INDUCTION: Induced by lactose, galactose and galactose-6-P. Repressed
CC       by glucose. {ECO:0000250|UniProtKB:P0A0D6}.
CC   -!- DOMAIN: The PTS EIIA type-3 domain is phosphorylated by phospho-HPr on
CC       a histidyl residue. Then, it transfers the phosphoryl group to the PTS
CC       EIIB type-3 domain. {ECO:0000255|PROSITE-ProRule:PRU00418}.
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DR   EMBL; M80797; AAA26908.1; -; Genomic_DNA.
DR   EMBL; AE014133; AAN59146.1; -; Genomic_DNA.
DR   PIR; G43258; G43258.
DR   RefSeq; NP_721840.1; NC_004350.2.
DR   RefSeq; WP_002263056.1; NC_004350.2.
DR   AlphaFoldDB; P26426; -.
DR   SMR; P26426; -.
DR   STRING; 210007.SMU_1492; -.
DR   PRIDE; P26426; -.
DR   EnsemblBacteria; AAN59146; AAN59146; SMU_1492.
DR   GeneID; 66819108; -.
DR   KEGG; smu:SMU_1492; -.
DR   PATRIC; fig|210007.7.peg.1328; -.
DR   eggNOG; COG1447; Bacteria.
DR   HOGENOM; CLU_152490_1_0_9; -.
DR   OMA; HAHTIQT; -.
DR   PhylomeDB; P26426; -.
DR   Proteomes; UP000002512; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
DR   CDD; cd00215; PTS_IIA_lac; 1.
DR   InterPro; IPR003188; PTS_IIA_lac/cel.
DR   InterPro; IPR036542; PTS_IIA_lac/cel_sf.
DR   PANTHER; PTHR34382; PTHR34382; 1.
DR   Pfam; PF02255; PTS_IIA; 1.
DR   PIRSF; PIRSF000699; PTS_IILac_III; 1.
DR   SUPFAM; SSF46973; SSF46973; 1.
DR   TIGRFAMs; TIGR00823; EIIA-LAC; 1.
DR   PROSITE; PS51095; PTS_EIIA_TYPE_3; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Magnesium; Metal-binding; Phosphoprotein;
KW   Phosphotransferase system; Reference proteome; Sugar transport;
KW   Transferase; Transport.
FT   CHAIN           1..104
FT                   /note="PTS system lactose-specific EIIA component"
FT                   /id="PRO_0000186607"
FT   DOMAIN          4..102
FT                   /note="PTS EIIA type-3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00418"
FT   ACT_SITE        78
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P0A0D6"
FT   BINDING         81
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="ligand shared between all trimeric partners"
FT                   /evidence="ECO:0000250|UniProtKB:P23532"
FT   MOD_RES         78
FT                   /note="Phosphohistidine; by HPr"
FT                   /evidence="ECO:0000250|UniProtKB:P0A0D6,
FT                   ECO:0000255|PROSITE-ProRule:PRU00418"
SQ   SEQUENCE   104 AA;  11399 MW;  281CB2F3CB109F5D CRC64;
     MNREEATLLG FEIVAYAGDA RSKLLEALNA AQAGEYDRAE ELVAAADDCI VDAHKAQTSL
     LAKEAQGDDI ELSVTLMHGQ DHLMTTILLK DLMKHLIELY KRGS
 
 
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