ID   PTLCB_STAHJ             Reviewed;         583 AA.
AC   Q4L869;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   16-JUN-2009, entry version 32.
DE   RecName: Full=PTS system lactose-specific EIICB component;
DE   AltName: Full=EIICB-Lac;
DE            Short=EII-Lac;
DE   Includes:
DE     RecName: Full=Lactose permease IIC component;
DE     AltName: Full=PTS system lactose-specific EIIC component;
DE   Includes:
DE     RecName: Full=Lactose-specific phosphotransferase enzyme IIB component;
DE              EC=2.7.1.69;
DE     AltName: Full=PTS system lactose-specific EIIB component;
GN   Name=lacE; OrderedLocusNames=SH0847;
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 lactose transport.
CC   -!- CATALYTIC ACTIVITY: Protein EIIB N(pi)-phospho-L-
CC       histidine/cysteine + sugar = protein EIIB + sugar phosphate.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC       (Probable).
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-3 domain.
CC   -!- SIMILARITY: Contains 1 PTS EIIC type-3 domain.
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DR   EMBL; AP006716; BAE04156.1; -; Genomic_DNA.
DR   RefSeq; YP_252762.1; -.
DR   GeneID; 3482144; -.
DR   GenomeReviews; AP006716_GR; SH0847.
DR   KEGG; sha:SH0847; -.
DR   NMPDR; fig|279808.3.peg.860; -.
DR   HOGENOM; Q4L869; -.
DR   OMA; Q4L869; WSKDIEN.
DR   BioCyc; SHAE279808:SH0847-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:0005529; F:sugar binding; IEA:InterPro.
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; IPR014350; PTrfase_system_EIIB_3_subgr.
DR   InterPro; IPR013012; PTS_EIIB_3.
DR   InterPro; IPR003352; PTS_EIIC.
DR   InterPro; IPR003501; PTS_IIB_lac.
DR   InterPro; IPR004501; PTS_IIC_lac.
DR   InterPro; IPR004801; PTS_IIC_lac_spec.
DR   Pfam; PF02378; PTS_EIIC; 1.
DR   Pfam; PF02302; PTS_IIB; 1.
DR   TIGRFAMs; TIGR00394; lac_pts_IIC; 1.
DR   TIGRFAMs; TIGR00410; lacE; 1.
DR   TIGRFAMs; TIGR00853; pts-lac; 1.
DR   PROSITE; PS51100; PTS_EIIB_TYPE_3; 1.
DR   PROSITE; PS51105; PTS_EIIC_TYPE_3; 1.
PE   4: Predicted;
KW   Cell membrane; Complete proteome; Kinase; Membrane;
KW   Phosphotransferase system; Sugar transport; Transferase;
KW   Transmembrane; Transport.
FT   CHAIN         1    583       PTS system lactose-specific EIICB
FT                                component.
FT                                /FTId=PRO_0000186594.
FT   TRANSMEM     29     49       Potential.
FT   TRANSMEM     60     80       Potential.
FT   TRANSMEM    101    121       Potential.
FT   TRANSMEM    130    150       Potential.
FT   TRANSMEM    173    193       Potential.
FT   TRANSMEM    218    238       Potential.
FT   TRANSMEM    277    297       Potential.
FT   TRANSMEM    333    353       Potential.
FT   TRANSMEM    374    394       Potential.
FT   DOMAIN      480    583       PTS EIIB type-3.
FT   ACT_SITE    487    487       Phosphocysteine intermediate; for EIIB
FT                                activity (By similarity).
SQ   SEQUENCE   583 AA;  64211 MW;  DCBDAECEF9CB5654 CRC64;
     MNKLIAWIEK GKPFFEKISR NIYLRAIRDG FIAAIPIILF SSIFILITYV PNVFGFTWSK
     TMEGILMKPY NYTMGIVGLI VAGTTAKSLT DSYNRKLDKT NQINFISTMM AAMSGFLFLA
     ADPIKEGGFL SAFMGTKGLL TAFISAFITV IVYNFFIKRN ITIKMPKEVP PNISQVFKDI
     FPLSAVIIII YALDLLSRTF IHTNVANAVL KIFEPLFTAA DGWIGVTLIF GAFAFFWFVG
     IHGPSIVEPA IAAITYANLE TNLNLIQAGE HADKIITPGT QMFVATMGGT GATLVVPFMF
     MWLTKSKRNK AIGRASVVPT FFGVNEPILF GAPLVLNPVF FIPFIFAPIV NVWIFKFFVD
     VLKMNSFSIF LPWTTPGPLG IVMGTGFAFW SFVLAIVLIV VDVMIYYPFL KVYDEQILEE
     ERGNKEVNNE LKEKVSANFD TKKADAILAT AGANETTTTE SAPSDEEVSA KNSSNSINEQ
     TNVLVLCAGG GTSGLLANAL NKAAEEYQVP VKAAAGGYGA HMDIMKDYQL IILAPQVASN
     YEDIKQDTDR LGIKLAKTQG VEYINLTRDG KAALDFVQQQ FEK
//