PTLCB_STAES
ID PTLCB_STAES Reviewed; 582 AA.
AC Q8CNF7;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=PTS system lactose-specific EIICB component {ECO:0000250|UniProtKB:P11162};
DE AltName: Full=EIICB-Lac {ECO:0000250|UniProtKB:P11162};
DE Short=EII-Lac {ECO:0000250|UniProtKB:P11162};
DE Includes:
DE RecName: Full=PTS system lactose-specific EIIC component {ECO:0000250|UniProtKB:P11162};
DE AltName: Full=Lactose permease IIC component {ECO:0000250|UniProtKB:P11162};
DE Includes:
DE RecName: Full=PTS system lactose-specific EIIB component {ECO:0000250|UniProtKB:P11162};
DE EC=2.7.1.207 {ECO:0000250|UniProtKB:P11162};
DE AltName: Full=Lactose-specific phosphotransferase enzyme IIB component {ECO:0000250|UniProtKB:P11162};
GN Name=lacE {ECO:0000250|UniProtKB:P11162}; OrderedLocusNames=SE_1782;
OS Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176280;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12228 / FDA PCI 1200;
RX PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT "Genome-based analysis of virulence genes in a non-biofilm-forming
RT Staphylococcus epidermidis strain (ATCC 12228).";
RL Mol. Microbiol. 49:1577-1593(2003).
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 LacEF PTS system is involved in lactose transport.
CC {ECO:0000250|UniProtKB:P11162}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=lactose(out) + N(pros)-phospho-L-histidyl-[protein] = L-
CC histidyl-[protein] + lactose 6-phosphate(in); Xref=Rhea:RHEA:42400,
CC Rhea:RHEA-COMP:9745, Rhea:RHEA-COMP:9746, ChEBI:CHEBI:17716,
CC ChEBI:CHEBI:29979, ChEBI:CHEBI:64837, ChEBI:CHEBI:79080;
CC EC=2.7.1.207; Evidence={ECO:0000250|UniProtKB:P11162};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P11162,
CC ECO:0000255|PROSITE-ProRule:PRU00428}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P11162, ECO:0000255|PROSITE-ProRule:PRU00428}.
CC -!- INDUCTION: Induced by lactose, galactose and galactose-6-P. Repressed
CC by glucose. {ECO:0000250|UniProtKB:P11162}.
CC -!- DOMAIN: The EIIC type-3 domain forms the PTS system translocation
CC channel and contains the specific substrate-binding site.
CC {ECO:0000255|PROSITE-ProRule:PRU00428}.
CC -!- DOMAIN: The PTS EIIB type-3 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-3 domain. {ECO:0000255|PROSITE-ProRule:PRU00423}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE015929; AAO05423.1; -; Genomic_DNA.
DR RefSeq; NP_765337.1; NC_004461.1.
DR RefSeq; WP_001829731.1; NZ_WBME01000007.1.
DR AlphaFoldDB; Q8CNF7; -.
DR SMR; Q8CNF7; -.
DR STRING; 176280.SE_1782; -.
DR EnsemblBacteria; AAO05423; AAO05423; SE_1782.
DR KEGG; sep:SE_1782; -.
DR PATRIC; fig|176280.10.peg.1739; -.
DR eggNOG; COG1440; Bacteria.
DR eggNOG; COG1455; Bacteria.
DR HOGENOM; CLU_029688_0_0_9; -.
DR OMA; ISAMPFM; -.
DR Proteomes; UP000001411; 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:0022869; F:protein-N(PI)-phosphohistidine-lactose phosphotransferase system 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; cd05565; PTS_IIB_lactose; 1.
DR InterPro; IPR004801; LacE.
DR InterPro; IPR036095; PTS_EIIB-like_sf.
DR InterPro; IPR003501; PTS_EIIB_2/3.
DR InterPro; IPR013012; PTS_EIIB_3.
DR InterPro; IPR003352; PTS_EIIC.
DR InterPro; IPR004501; PTS_EIIC_3.
DR InterPro; IPR041713; PTS_IIB.
DR Pfam; PF02378; PTS_EIIC; 1.
DR Pfam; PF02302; PTS_IIB; 1.
DR SUPFAM; SSF52794; SSF52794; 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 3: Inferred from homology;
KW Cell membrane; Kinase; Membrane; Phosphoprotein; Phosphotransferase system;
KW Sugar transport; Transferase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..582
FT /note="PTS system lactose-specific EIICB component"
FT /id="PRO_0000186592"
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00428"
FT TRANSMEM 64..84
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00428"
FT TRANSMEM 103..123
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00428"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00428"
FT TRANSMEM 176..196
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00428"
FT TRANSMEM 222..242
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00428"
FT TRANSMEM 283..303
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00428"
FT TRANSMEM 339..359
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00428"
FT TRANSMEM 381..401
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00428"
FT DOMAIN 8..409
FT /note="PTS EIIC type-3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00428"
FT DOMAIN 479..582
FT /note="PTS EIIB type-3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00423"
FT REGION 453..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..473
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 486
FT /note="Phosphocysteine intermediate; for EIIB activity"
FT /evidence="ECO:0000250|UniProtKB:P11162"
FT MOD_RES 486
FT /note="Phosphocysteine; by EIIA"
FT /evidence="ECO:0000250|UniProtKB:P11162,
FT ECO:0000255|PROSITE-ProRule:PRU00423"
SQ SEQUENCE 582 AA; 63765 MW; 256AC4A2AC536C1B CRC64;
MNKLIAWIEK GKPFFEKISR NIYLRAIRDG FIAAIPIILF SSIFILITYV PNVFGFTWSK
TMEGILMKPY NYTMGIVGLL VAGTTAKSLT DSYNRKLDKT NQINFISTMM AAICGFLFLA
ADPVKDGGFS SAFMGTKGLL TAFISAFITV IVYNFFVKRN ITIKMPKEVP PNISQVFKDI
FPLSAVILIL YALDLLSRAI VHTNVANAVL KVFEPLFTAA DGWIGVTLIF GAFAFFWFVG
IHGPSIVEPA IAAITYANLE TNLHLIQAGE HADKVITPGT QMFVATMGGT GATLVVPFMF
MWLTKSKRNK AIGRASVVPT FFGVNEPILF GAPLVLNPVF FIPFIFAPIV NIWIFKFFVD
VLNMNSFSIF LPWTTPGPLG IVMGTGFAFW SFVLAILLIV VDVIIYYPFL KVYDEQVLEE
ELGNKEANNE LKEKVSANFD TKKADAILAT AGASEADTDD TSSVDETTST SSTDTISEQT
NVLVLCAGGG TSGLLANALN KAAEEYEVPV KAAAGGYGAH MDIMKDYQLI ILAPQVASNF
EDIKQDTDRL GIKLAKTEGA QYIKLTRDGE AALEFVKQQF NN
