位置:首页 > 蛋白库 > PTMCB_STAHJ
PTMCB_STAHJ
ID   PTMCB_STAHJ             Reviewed;         519 AA.
AC   Q4L9Y1;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=PTS system mannitol-specific EIICB component {ECO:0000250|UniProtKB:P28008};
DE   AltName: Full=EIICB-Mtl {ECO:0000250|UniProtKB:P28008};
DE            Short=EII-Mtl {ECO:0000250|UniProtKB:P28008};
DE   Includes:
DE     RecName: Full=Mannitol permease IIC component {ECO:0000250|UniProtKB:P28008};
DE     AltName: Full=PTS system mannitol-specific EIIC component {ECO:0000250|UniProtKB:P28008};
DE   Includes:
DE     RecName: Full=Mannitol-specific phosphotransferase enzyme IIB component {ECO:0000250|UniProtKB:P28008};
DE              EC=2.7.1.197 {ECO:0000250|UniProtKB:P00550, ECO:0000250|UniProtKB:P28008};
DE     AltName: Full=PTS system mannitol-specific EIIB component {ECO:0000250|UniProtKB:P28008};
GN   Name=mtlA; OrderedLocusNames=SH0235;
OS   Staphylococcus haemolyticus (strain JCSC1435).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=279808;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCSC1435;
RX   PubMed=16237012; DOI=10.1128/jb.187.21.7292-7308.2005;
RA   Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA   Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA   Hiramatsu K.;
RT   "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT   extreme plasticity of its genome and the evolution of human-colonizing
RT   staphylococcal species.";
RL   J. Bacteriol. 187:7292-7308(2005).
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 CmtAB PTS system is involved in D-mannitol transport.
CC       {ECO:0000250|UniProtKB:P28008}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-mannitol(out) + N(pros)-phospho-L-histidyl-[protein] = D-
CC         mannitol 1-phosphate(in) + L-histidyl-[protein];
CC         Xref=Rhea:RHEA:33363, Rhea:RHEA-COMP:9745, Rhea:RHEA-COMP:9746,
CC         ChEBI:CHEBI:16899, ChEBI:CHEBI:29979, ChEBI:CHEBI:61381,
CC         ChEBI:CHEBI:64837; EC=2.7.1.197;
CC         Evidence={ECO:0000250|UniProtKB:P00550,
CC         ECO:0000250|UniProtKB:P28008};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P28008}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC       ProRule:PRU00427}; Multi-pass membrane protein {ECO:0000255|PROSITE-
CC       ProRule:PRU00427}.
CC   -!- DOMAIN: The EIIC type-2 domain forms the PTS system translocation
CC       channel and contains the specific substrate-binding site.
CC       {ECO:0000255|PROSITE-ProRule:PRU00427}.
CC   -!- DOMAIN: The PTS EIIB type-2 domain is phosphorylated by phospho-EIIA on
CC       a cysteinyl residue. Then, it transfers the phosphoryl group to the
CC       sugar substrate concomitantly with the sugar uptake processed by the
CC       PTS EIIC type-2 domain. {ECO:0000255|PROSITE-ProRule:PRU00422}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AP006716; BAE03544.1; -; Genomic_DNA.
DR   RefSeq; WP_011274564.1; NC_007168.1.
DR   AlphaFoldDB; Q4L9Y1; -.
DR   SMR; Q4L9Y1; -.
DR   STRING; 279808.SH0235; -.
DR   EnsemblBacteria; BAE03544; BAE03544; SH0235.
DR   KEGG; sha:SH0235; -.
DR   eggNOG; COG2213; Bacteria.
DR   HOGENOM; CLU_028721_2_0_9; -.
DR   OMA; GWAIKRF; -.
DR   OrthoDB; 554815at2; -.
DR   Proteomes; UP000000543; 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:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0022872; F:protein-N(PI)-phosphohistidine-mannitol phosphotransferase system transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd05567; PTS_IIB_mannitol; 1.
DR   InterPro; IPR036095; PTS_EIIB-like_sf.
DR   InterPro; IPR013011; PTS_EIIB_2.
DR   InterPro; IPR003501; PTS_EIIB_2/3.
DR   InterPro; IPR029503; PTS_EIIB_mannitol.
DR   InterPro; IPR003352; PTS_EIIC.
DR   InterPro; IPR013014; PTS_EIIC_2.
DR   InterPro; IPR004718; PTS_IIC_mtl.
DR   Pfam; PF02378; PTS_EIIC; 1.
DR   Pfam; PF02302; PTS_IIB; 1.
DR   SUPFAM; SSF52794; SSF52794; 1.
DR   TIGRFAMs; TIGR00851; mtlA; 1.
DR   PROSITE; PS51099; PTS_EIIB_TYPE_2; 1.
DR   PROSITE; PS51104; PTS_EIIC_TYPE_2; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Kinase; Membrane; Phosphoprotein; Phosphotransferase system;
KW   Sugar transport; Transferase; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..519
FT                   /note="PTS system mannitol-specific EIICB component"
FT                   /id="PRO_0000186627"
FT   TOPO_DOM        1..30
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P00550"
FT   TRANSMEM        31..52
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P00550"
FT   TOPO_DOM        53..56
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P00550"
FT   TRANSMEM        57..77
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P00550"
FT   TOPO_DOM        78..141
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P00550"
FT   TRANSMEM        142..163
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P00550"
FT   TOPO_DOM        164..172
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P00550"
FT   TRANSMEM        173..193
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P00550"
FT   TOPO_DOM        194..280
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P00550"
FT   TRANSMEM        281..300
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P00550"
FT   TOPO_DOM        301..320
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P00550"
FT   TRANSMEM        321..342
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P00550"
FT   TOPO_DOM        343..519
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P00550"
FT   DOMAIN          19..351
FT                   /note="PTS EIIC type-2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT   DOMAIN          425..519
FT                   /note="PTS EIIB type-2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00422"
FT   REGION          366..406
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        431
FT                   /note="Phosphocysteine intermediate; for EIIB activity"
FT                   /evidence="ECO:0000250|UniProtKB:P00550,
FT                   ECO:0000250|UniProtKB:P28008"
FT   MOD_RES         431
FT                   /note="Phosphocysteine; by EIIA"
FT                   /evidence="ECO:0000250|UniProtKB:P00550,
FT                   ECO:0000250|UniProtKB:P28008, ECO:0000255|PROSITE-
FT                   ProRule:PRU00422"
SQ   SEQUENCE   519 AA;  55663 MW;  A74770C9BEB765A2 CRC64;
     MAQTETQEKK GLGRKVQAFG SFLSSMIMPN IGAFIAWGFI AAIFIDNGWY PNKELSQLAG
     PMITYLIPLL IAFSGGRLIH DLRGGIVAAT ATMGVIVALP DTPMLLGAMI MGPLVGWLMK
     KVDQFLQPRT PQGFEMLFNN FSAGILAFIM TILGFKLLAP IMQFIMHILS VAVEFLVHLH
     LLPIVSIIVE PAKILFLNNA INHGVFTPLG TDQAASAGQS ILFAIESNPG PGIGILLAYM
     IFGKGTAKAT SYGAGIIHFF GGIHEIYFPY VLMRPLLFIA VILGGMTGVA TYQATGFGFK
     SPASPGSFIV YCLNAPKGEF LHMVLGVFLA ALVSFVVAAL IMKFTKEPKQ DLEAATAKME
     STKGKKSSVS SKLTGATTGT GAAGVAANKA NGEDQNEASS EDEEEDLLDN YNTEDVDAHD
     YSNVDHVIFA CDAGMGSSAM GASMLRNKFK KAGISDVNVT NTAINQLPNN AQLVITQKTL
     TDRAIKQVPN AIHISVDNFL NSPRYEELLN NLKKDQDKA
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024