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   16-JUN-2009, entry version 30.
DE   RecName: Full=PTS system mannitol-specific EIICB component;
DE   AltName: Full=EIICB-Mtl;
DE            Short=EII-Mtl;
DE   Includes:
DE     RecName: Full=Mannitol permease IIC component;
DE     AltName: Full=PTS system mannitol-specific EIIC component;
DE   Includes:
DE     RecName: Full=Mannitol-specific phosphotransferase enzyme IIB component;
DE              EC=2.7.1.69;
DE     AltName: Full=PTS system mannitol-specific EIIB component;
GN   Name=mtlA; OrderedLocusNames=SH0235;
OS   Staphylococcus haemolyticus (strain JCSC1435).
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=279808;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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.,
RA   Lee J.C., 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
CC       phosphotransferase system (sugar PTS), a major carbohydrate active
CC       -transport system, catalyzes the phosphorylation of incoming sugar
CC       substrates concomitantly with their translocation across the cell
CC       membrane. This system is involved in mannitol transport.
CC   -!- CATALYTIC ACTIVITY: Protein EIIB N(pi)-phospho-L-
CC       histidine/cysteine + sugar = protein EIIB + sugar phosphate.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- DOMAIN: The EIIC domain forms the PTS system translocation channel
CC       and contains the specific substrate-binding site.
CC   -!- DOMAIN: The EIIB domain is phosphorylated by phospho-EIIA on a
CC       cysteinyl or histidyl residue, depending on the transported sugar.
CC       Then, it transfers the phosphoryl group to the sugar substrate
CC       concomitantly with the sugar uptake processed by the EIIC domain.
CC   -!- SIMILARITY: Contains 1 PTS EIIB type-2 domain.
CC   -!- SIMILARITY: Contains 1 PTS EIIC type-2 domain.
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DR   EMBL; AP006716; BAE03544.1; -; Genomic_DNA.
DR   RefSeq; YP_252150.1; -.
DR   GeneID; 3482069; -.
DR   GenomeReviews; AP006716_GR; SH0235.
DR   KEGG; sha:SH0235; -.
DR   NMPDR; fig|279808.3.peg.248; -.
DR   HOGENOM; Q4L9Y1; -.
DR   OMA; Q4L9Y1; ITHKDLT.
DR   BioCyc; SHAE279808:SH0235-MON; -.
DR   GO; GO:0016021; C:integral to 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:0008982; F:protein-N(PI)-phosphohistidine-sugar phosph...; IEA:EC.
DR   GO; GO:0005351; F:sugar:hydrogen symporter activity; IEA:UniProtKB-KW.
DR   GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phospho...; IEA:UniProtKB-KW.
DR   InterPro; IPR013011; PTS_EIIB_2.
DR   InterPro; IPR003352; PTS_EIIC.
DR   InterPro; IPR013014; PTS_EIIC_2.
DR   InterPro; IPR003501; PTS_IIB_lac.
DR   InterPro; IPR004718; PTS_IIC_mtl.
DR   Pfam; PF02378; PTS_EIIC; 1.
DR   Pfam; PF02302; PTS_IIB; 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; Complete proteome; Kinase; Membrane;
KW   Phosphotransferase system; Sugar transport; Transferase;
KW   Transmembrane; Transport.
FT   CHAIN         1    519       PTS system mannitol-specific EIICB
FT                                component.
FT                                /FTId=PRO_0000186627.
FT   TRANSMEM     25     45       Potential.
FT   TRANSMEM     55     75       Potential.
FT   TRANSMEM     95    115       Potential.
FT   TRANSMEM    145    165       Potential.
FT   TRANSMEM    168    188       Potential.
FT   TRANSMEM    221    241       Potential.
FT   TRANSMEM    250    272       Potential.
FT   TRANSMEM    277    299       Potential.
FT   TRANSMEM    321    341       Potential.
FT   DOMAIN       19    351       PTS EIIC type-2.
FT   DOMAIN      425    519       PTS EIIB type-2.
FT   ACT_SITE    431    431       Phosphocysteine intermediate; for EIIB
FT                                activity (By similarity).
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
//