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}.
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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