PTLA_STAEQ
ID PTLA_STAEQ Reviewed; 104 AA.
AC Q5HM39;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=PTS system lactose-specific EIIA component {ECO:0000250|UniProtKB:P0A0D6};
DE AltName: Full=EIIA-Lac {ECO:0000250|UniProtKB:P0A0D6};
DE AltName: Full=EIII-Lac {ECO:0000250|UniProtKB:P0A0D6};
DE AltName: Full=Lactose-specific phosphotransferase enzyme IIA component {ECO:0000250|UniProtKB:P0A0D6};
GN Name=lacF {ECO:0000250|UniProtKB:P0A0D6}; OrderedLocusNames=SERP1791;
OS Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176279;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35984 / RP62A;
RX PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA Fraser C.M.;
RT "Insights on evolution of virulence and resistance from the complete genome
RT analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT strain.";
RL J. Bacteriol. 187:2426-2438(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:P0A0D6}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P23532};
CC Note=Binds 1 Mg(2+) ion per trimer. {ECO:0000250|UniProtKB:P23532};
CC -!- SUBUNIT: Homotrimer. {ECO:0000250|UniProtKB:P0A0D6}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: Induced by lactose, galactose and galactose-6-P. Repressed
CC by glucose. {ECO:0000250|UniProtKB:P0A0D6}.
CC -!- DOMAIN: The PTS EIIA type-3 domain is phosphorylated by phospho-HPr on
CC a histidyl residue. Then, it transfers the phosphoryl group to the PTS
CC EIIB type-3 domain. {ECO:0000255|PROSITE-ProRule:PRU00418}.
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DR EMBL; CP000029; AAW55167.1; -; Genomic_DNA.
DR RefSeq; WP_001829758.1; NC_002976.3.
DR AlphaFoldDB; Q5HM39; -.
DR SMR; Q5HM39; -.
DR STRING; 176279.SERP1791; -.
DR EnsemblBacteria; AAW55167; AAW55167; SERP1791.
DR GeneID; 50018113; -.
DR KEGG; ser:SERP1791; -.
DR eggNOG; COG1447; Bacteria.
DR HOGENOM; CLU_152490_1_0_9; -.
DR OMA; HAHTIQT; -.
DR OrthoDB; 2038379at2; -.
DR Proteomes; UP000000531; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
DR CDD; cd00215; PTS_IIA_lac; 1.
DR InterPro; IPR003188; PTS_IIA_lac/cel.
DR InterPro; IPR036542; PTS_IIA_lac/cel_sf.
DR PANTHER; PTHR34382; PTHR34382; 1.
DR Pfam; PF02255; PTS_IIA; 1.
DR PIRSF; PIRSF000699; PTS_IILac_III; 1.
DR SUPFAM; SSF46973; SSF46973; 1.
DR TIGRFAMs; TIGR00823; EIIA-LAC; 1.
DR PROSITE; PS51095; PTS_EIIA_TYPE_3; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Magnesium; Metal-binding; Phosphoprotein;
KW Phosphotransferase system; Reference proteome; Sugar transport;
KW Transferase; Transport.
FT CHAIN 1..104
FT /note="PTS system lactose-specific EIIA component"
FT /id="PRO_0000186606"
FT DOMAIN 1..102
FT /note="PTS EIIA type-3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00418"
FT ACT_SITE 78
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P0A0D6"
FT BINDING 81
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="ligand shared between all trimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P23532"
FT MOD_RES 78
FT /note="Phosphohistidine; by HPr"
FT /evidence="ECO:0000250|UniProtKB:P0A0D6,
FT ECO:0000255|PROSITE-ProRule:PRU00418"
SQ SEQUENCE 104 AA; 11588 MW; 20FCB5F0CA05C2CF CRC64;
MNRDEVQLLG FEIVAYAGDA RSKLLEALNA AKDSEFDKAE QLVEEANECI ANAHKAQTNL
LAQEAKGEDI AYSITMIHGQ DHLMTTLLLK DLMKHLIELY KKGS
