ID   PTLCB_LACCA             Reviewed;         577 AA.
AC   P24400;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   16-JUN-2009, entry version 65.
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;
OS   Lactobacillus casei.
OC   Bacteria; Firmicutes; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=1582;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=91093108; PubMed=2125053;
RA   Alpert C.-A., Chassy B.M.;
RT   "Molecular cloning and DNA sequence of lacE, the gene encoding the
RT   lactose-specific enzyme II of the phosphotransferase system of
RT   Lactobacillus casei. Evidence that a cysteine residue is essential for
RT   sugar phosphorylation.";
RL   J. Biol. Chem. 265:22561-22568(1990).
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; M60851; AAA72984.1; -; Genomic_DNA.
DR   PIR; B23697; B23697.
DR   BRENDA; 2.7.1.69; 610.
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; Kinase; Membrane; Phosphotransferase system;
KW   Sugar transport; Transferase; Transmembrane; Transport.
FT   CHAIN         1    577       PTS system lactose-specific EIICB
FT                                component.
FT                                /FTId=PRO_0000186583.
FT   TRANSMEM     27     47       Potential.
FT   TRANSMEM     63     83       Potential.
FT   TRANSMEM    100    120       Potential.
FT   TRANSMEM    133    153       Potential.
FT   TRANSMEM    176    196       Potential.
FT   TRANSMEM    219    239       Potential.
FT   TRANSMEM    280    300       Potential.
FT   TRANSMEM    326    346       Potential.
FT   TRANSMEM    386    406       Potential.
FT   DOMAIN        4    405       PTS EIIC type-3.
FT   DOMAIN      476    577       PTS EIIB type-3.
FT   ACT_SITE    483    483       Phosphocysteine intermediate; for EIIB
FT                                activity (By similarity).
SQ   SEQUENCE   577 AA;  62392 MW;  BE56852CAB0D76E4 CRC64;
     MNKVFDKLKP VFEAIAANKY ISAIRDGFIA CMPIIIFSSI FMMVAYVPNA WGFYWPDNVT
     NTLMVAYNYS MGLLALFVAG TTAKNLTDSK NLELPKTNQI NPVAVIVASE ISFVILSILP
     LKTGVDLTYM GTQGLICAYI VGLIVPNIYY VCIKNNVTIK LPEQVPGNIA QSFKDLIPMG
     LSVTAFWLFG VGFKAATGTV LPRWIIQVLS PLFQASDSYL GLALIAGAMA FFWFCGVQGP
     SIVQPAVVPI MIANTAANLQ QYQAGQHVSH VLAMNTMDYV MNFGGTGATL VVPFIMLFAA
     RSAQLKAVGK AAFVPCTFGV NEPVLFGMPI IMNPMLFIPF LATPIVNVCL FKFFVSVLGM
     NSMMYTMPWT VPGPIGILIS TGFAPLAFVF VLLTLVLDVA IYFPFIRVYD STLLAEEKAK
     EEVIEDDGMA VLASDTVSPS IPTGLTVATA TDDDATHVLP ETAPSAHGEA YFKQNEVDVL
     VLCAGGGTSG ILANALNKLS KERGLKLSAA ARAYGQDMDL IKDMNMVILA PQMESMKGNL
     KKITDKYGVK LVTTTGRQYI ELTNNGDMAL DFVESNL
//