PTLCB_STRMU
ID PTLCB_STRMU Reviewed; 568 AA.
AC P50976;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=PTS system lactose-specific EIICB component {ECO:0000303|PubMed:1400164};
DE AltName: Full=EIICB-Lac {ECO:0000303|PubMed:1400164};
DE Short=EII-Lac {ECO:0000303|PubMed:1400164};
DE Includes:
DE RecName: Full=PTS system lactose-specific EIIC component {ECO:0000303|PubMed:1400164};
DE AltName: Full=Lactose permease IIC component {ECO:0000303|PubMed:1400164};
DE Includes:
DE RecName: Full=PTS system lactose-specific EIIB component {ECO:0000303|PubMed:1400164};
DE EC=2.7.1.207 {ECO:0000250|UniProtKB:P24400};
DE AltName: Full=Lactose-specific phosphotransferase enzyme IIB component {ECO:0000303|PubMed:1400164};
GN Name=lacE {ECO:0000303|PubMed:1400164}; OrderedLocusNames=SMU_1491;
OS Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=210007;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC 700611 / UA130 / Serotype c;
RX PubMed=1400164; DOI=10.1128/jb.174.19.6159-6170.1992;
RA Rosey E.L., Stewart G.C.;
RT "Nucleotide and deduced amino acid sequences of the lacR, lacABCD, and
RT lacFE genes encoding the repressor, tagatose 6-phosphate gene cluster, and
RT sugar-specific phosphotransferase system components of the lactose operon
RT of Streptococcus mutans.";
RL J. Bacteriol. 174:6159-6170(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 700611 / UA130 / Serotype c;
RX PubMed=8277252; DOI=10.1099/00221287-139-11-2685;
RA Honeyman A.L., Curtiss R. III;
RT "Isolation, characterization and nucleotide sequence of the Streptococcus
RT mutans lactose-specific enzyme II (lacE) gene of the PTS and the phospho-
RT beta-galactosidase (lacG) gene.";
RL J. Gen. Microbiol. 139:2685-2694(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700610 / UA159;
RX PubMed=12397186; DOI=10.1073/pnas.172501299;
RA Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
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:P24400, ECO:0000305|PubMed:8277252}.
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:P24400};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00428}; Multi-pass membrane protein {ECO:0000255|PROSITE-
CC ProRule:PRU00428}.
CC -!- INDUCTION: Induced by lactose, galactose and galactose-6-P. Repressed
CC by glucose. {ECO:0000250|UniProtKB:P23531}.
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}.
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DR EMBL; L18993; AAA16449.1; -; Unassigned_DNA.
DR EMBL; AE014133; AAN59145.1; -; Genomic_DNA.
DR RefSeq; NP_721839.1; NC_004350.2.
DR RefSeq; WP_002263057.1; NC_004350.2.
DR AlphaFoldDB; P50976; -.
DR SMR; P50976; -.
DR STRING; 210007.SMU_1491; -.
DR PRIDE; P50976; -.
DR EnsemblBacteria; AAN59145; AAN59145; SMU_1491.
DR KEGG; smu:SMU_1491; -.
DR PATRIC; fig|210007.7.peg.1327; -.
DR eggNOG; COG1440; Bacteria.
DR eggNOG; COG1455; Bacteria.
DR HOGENOM; CLU_029688_0_0_9; -.
DR OMA; ISAMPFM; -.
DR PhylomeDB; P50976; -.
DR Proteomes; UP000002512; 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 Reference proteome; Sugar transport; Transferase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..568
FT /note="PTS system lactose-specific EIICB component"
FT /id="PRO_0000186595"
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00428"
FT TRANSMEM 65..85
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 128..148
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00428"
FT TRANSMEM 183..203
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 246..266
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 465..568
FT /note="PTS EIIB type-3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00423"
FT ACT_SITE 472
FT /note="Phosphocysteine intermediate; for EIIB activity"
FT /evidence="ECO:0000250|UniProtKB:P24400"
FT MOD_RES 472
FT /note="Phosphocysteine; by EIIA"
FT /evidence="ECO:0000250|UniProtKB:P24400,
FT ECO:0000255|PROSITE-ProRule:PRU00423"
SQ SEQUENCE 568 AA; 61420 MW; A129FDD14282EAAE CRC64;
MNTLIAQIEK GKPFFEKISR NIYLRAIRDG FISAMPVILF SSIFLLIAYV PNIFGFTWPK
GIENMLMTPY NYTMGIIGFL VAGTTAKSLT DSMNRQLEKT NQINFISTML ASMAGFLIMA
ADPAKEGGFL SAFMGTKGLL TAFIAAFITV NVYKICVKNN VTIRMPEEVP PNISQVFKDI
FPFAFSIIIL YAIQLAIKAV IGVNVAQSIG TLLAPLFSAA DGYLGITIIF GAYALFWFVG
IHGPSIVEPA IAAITYSNVE LNAHLIHAGQ HADKVITSGT QMFIVTMGGT GATLVVPFMF
MWLCKSKRNK AIGRASVVPT FFGVNEPILF GAPIVLNPVF FIPFILAPIV NVWIFKFFVD
TLGMNSFFAN LPWTTPGPIG IVLGTGFAVL SFVLAALLIL VDTVIYYPFV KVYDEQILAE
EAEGKSSSDA LKEKVAANFD TKKADAILEG AESKEEPATH AITEETNVLV LCAGGGTSGL
LANALNKAAE EYGAPVKAAA GSYGAHREIL DQYQLVILAP QVASNYEDMK AETDKLGIKL
AKTEGAQYIG LTRDGKGALA FVEEQFKD
