ID   PTMCB_STAS1             Reviewed;         508 AA.
AC   Q49ZA3;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   16-JUN-2009, entry version 28.
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=SSP0728;
OS   Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 /
OS   DSM 20229).
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=342451;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16135568; DOI=10.1073/pnas.0502950102;
RA   Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K.,
RA   Higashide M., Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S.,
RA   Hattori M., Ohta T.;
RT   "Whole genome sequence of Staphylococcus saprophyticus reveals the
RT   pathogenesis of uncomplicated urinary tract infection.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(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; AP008934; BAE17873.1; -; Genomic_DNA.
DR   RefSeq; YP_300818.1; -.
DR   GeneID; 3615929; -.
DR   GenomeReviews; AP008934_GR; SSP0728.
DR   KEGG; ssp:SSP0728; -.
DR   NMPDR; fig|342451.4.peg.1141; -.
DR   HOGENOM; Q49ZA3; -.
DR   OMA; Q49ZA3; KSARTAN.
DR   BioCyc; SSAP342451:SSP0728-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    508       PTS system mannitol-specific EIICB
FT                                component.
FT                                /FTId=PRO_0000186628.
FT   TRANSMEM     25     45       Potential.
FT   TRANSMEM     55     75       Potential.
FT   TRANSMEM     86    106       Potential.
FT   TRANSMEM    145    165       Potential.
FT   TRANSMEM    168    188       Potential.
FT   TRANSMEM    253    273       Potential.
FT   TRANSMEM    275    295       Potential.
FT   TRANSMEM    321    341       Potential.
FT   DOMAIN       19    351       PTS EIIC type-2.
FT   DOMAIN      420    508       PTS EIIB type-2.
FT   ACT_SITE    426    426       Phosphocysteine intermediate; for EIIB
FT                                activity (By similarity).
SQ   SEQUENCE   508 AA;  54700 MW;  33926C8EA2CE175D CRC64;
     MSQTETQENK GLGRKVQAFG SFLSSMIMPN IGAFIAWGFI AAIFIDGGWW PNKDLSELAG
     PMISYLIPLL IAYSGGRLIH EMRGGIIAAV ATMGVIVALP DTPMLLGAMI MGPLVGWLMK
     KTDEFIQPRT PQGFEMLFNN FSAGILGFIM TIVGFKILAP IMEFIMHILS LAVEALVHAH
     LLPLVSIIVE PAKIVFLNNA INHGVFTPLG ADQAASAGQS ILYTIESNPG PGLGILVAYM
     IFGKGTAKAT SYGAGIIHFL GGIHEIYFPY VLMRPLLFIA VILGGMTGVA TYSLLDFGFK
     SPASPGSFIV YMLNAPKGEF LHMVLGVLLA AIVSFIVAAL ILKFTKEPEE DLEAATEKME
     ASKGKKSSVS SKLKGNEDNN ATSTTASTST SENNEEQSEE ALLDNYDTEN VDAHDYSKVN
     HVIFACDAGM GSSAMGASML RNKFKKAGIQ DVNVTNTAIN QLPSDAQLVI TQKKLTDRAI
     KQVPNAIHIS VDNFLNSPRY DELLENLK
//