PTLCB_STAHJ
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 03-AUG-2022, entry version 120.
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=SH0847;
OS Staphylococcus haemolyticus (strain JCSC1435).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=279808;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCSC1435;
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., Lee J.C.,
RA 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 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; AP006716; BAE04156.1; -; Genomic_DNA.
DR RefSeq; WP_011275159.1; NC_007168.1.
DR AlphaFoldDB; Q4L869; -.
DR SMR; Q4L869; -.
DR STRING; 279808.SH0847; -.
DR PRIDE; Q4L869; -.
DR EnsemblBacteria; BAE04156; BAE04156; SH0847.
DR KEGG; sha:SH0847; -.
DR eggNOG; COG1440; Bacteria.
DR eggNOG; COG1455; Bacteria.
DR HOGENOM; CLU_029688_0_0_9; -.
DR OMA; ISAMPFM; -.
DR OrthoDB; 425893at2; -.
DR Proteomes; UP000000543; 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..583
FT /note="PTS system lactose-specific EIICB component"
FT /id="PRO_0000186594"
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 480..583
FT /note="PTS EIIB type-3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00423"
FT REGION 453..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 487
FT /note="Phosphocysteine intermediate; for EIIB activity"
FT /evidence="ECO:0000250|UniProtKB:P11162"
FT MOD_RES 487
FT /note="Phosphocysteine; by EIIA"
FT /evidence="ECO:0000250|UniProtKB:P11162,
FT ECO:0000255|PROSITE-ProRule:PRU00423"
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
