PTCB_LACLM
ID PTCB_LACLM Reviewed; 108 AA.
AC A2RIE6;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=PTS system galactose-specific EIIB component {ECO:0000305};
DE AltName: Full=Galactose-specific phosphotransferase enzyme IIB component {ECO:0000305};
DE EC=2.7.1.204 {ECO:0000305|PubMed:30123211};
GN Name=ptcB {ECO:0000303|PubMed:30123211};
GN OrderedLocusNames=llmg_0437 {ECO:0000312|EMBL:CAL97041.1};
OS Lactococcus lactis subsp. cremoris (strain MG1363).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus; Lactococcus cremoris subsp. cremoris.
OX NCBI_TaxID=416870;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MG1363;
RX PubMed=17307855; DOI=10.1128/jb.01768-06;
RA Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C.,
RA Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P.,
RA van Sinderen D., Kok J.;
RT "The complete genome sequence of the lactic acid bacterial paradigm
RT Lactococcus lactis subsp. cremoris MG1363.";
RL J. Bacteriol. 189:3256-3270(2007).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND INDUCTION.
RC STRAIN=MG1363;
RX PubMed=30123211; DOI=10.3389/fmicb.2018.01803;
RA Solopova A., Bachmann H., Teusink B., Kok J., Kuipers O.P.;
RT "Further elucidation of galactose utilization in Lactococcus lactis
RT MG1363.";
RL Front. Microbiol. 9:1803-1803(2018).
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 (By
CC similarity). Involved in galactose transport with PtcA and Lmg_0963
CC (PubMed:30123211). {ECO:0000250|UniProtKB:P69795,
CC ECO:0000269|PubMed:30123211}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-galactose(out) + N(pros)-phospho-L-histidyl-[protein] = D-
CC galactose 6-phosphate(in) + L-histidyl-[protein];
CC Xref=Rhea:RHEA:49260, Rhea:RHEA-COMP:9745, Rhea:RHEA-COMP:9746,
CC ChEBI:CHEBI:4139, ChEBI:CHEBI:29979, ChEBI:CHEBI:64837,
CC ChEBI:CHEBI:91004; EC=2.7.1.204;
CC Evidence={ECO:0000305|PubMed:30123211};
CC -!- INDUCTION: Induced by growth on galactose.
CC {ECO:0000269|PubMed:30123211}.
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; AM406671; CAL97041.1; -; Genomic_DNA.
DR RefSeq; WP_011675488.1; NZ_WJVF01000001.1.
DR AlphaFoldDB; A2RIE6; -.
DR SMR; A2RIE6; -.
DR STRING; 416870.llmg_0437; -.
DR EnsemblBacteria; CAL97041; CAL97041; llmg_0437.
DR GeneID; 61108737; -.
DR KEGG; llm:llmg_0437; -.
DR eggNOG; COG1440; Bacteria.
DR HOGENOM; CLU_147323_1_1_9; -.
DR OMA; YAIPEQN; -.
DR PhylomeDB; A2RIE6; -.
DR BioCyc; LLAC416870:LLMG_RS02225-MON; -.
DR Proteomes; UP000000364; Chromosome.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0008982; F:protein-N(PI)-phosphohistidine-sugar phosphotransferase 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 InterPro; IPR036095; PTS_EIIB-like_sf.
DR InterPro; IPR003501; PTS_EIIB_2/3.
DR InterPro; IPR013012; PTS_EIIB_3.
DR Pfam; PF02302; PTS_IIB; 1.
DR SUPFAM; SSF52794; SSF52794; 1.
DR PROSITE; PS51100; PTS_EIIB_TYPE_3; 1.
PE 1: Evidence at protein level;
KW Kinase; Phosphoprotein; Phosphotransferase system; Sugar transport;
KW Transferase; Transport.
FT CHAIN 1..108
FT /note="PTS system galactose-specific EIIB component"
FT /id="PRO_5002645555"
FT DOMAIN 3..108
FT /note="PTS EIIB type-3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00423"
FT ACT_SITE 10
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P69795"
FT MOD_RES 10
FT /note="Phosphocysteine; by EIIA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00423"
SQ SEQUENCE 108 AA; 11324 MW; D7E8B656BEA4FDED CRC64;
MADKVIALAC AAGMSTSLLV SKMQKAAAEN GKDYEIFAKS TADIDNMLAG TGSPKPDVLL
LGPQVAFMKG EVAKKAEIAG VPMDVIKMQD YGMMRGDKVL AAAENLMN
