PTLA_STAAR
ID PTLA_STAAR Reviewed; 103 AA.
AC Q6GEN8;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 102.
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=SAR2282;
OS Staphylococcus aureus (strain MRSA252).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=282458;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRSA252;
RX PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT for the rapid evolution of virulence and drug resistance.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
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; BX571856; CAG41260.1; -; Genomic_DNA.
DR RefSeq; WP_001078309.1; NC_002952.2.
DR AlphaFoldDB; Q6GEN8; -.
DR SMR; Q6GEN8; -.
DR KEGG; sar:SAR2282; -.
DR HOGENOM; CLU_152490_1_0_9; -.
DR OMA; HAHTIQT; -.
DR OrthoDB; 2038379at2; -.
DR Proteomes; UP000000596; 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; Sugar transport; Transferase; Transport.
FT CHAIN 1..103
FT /note="PTS system lactose-specific EIIA component"
FT /id="PRO_0000186601"
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 103 AA; 11370 MW; CF2DB98F139E8131 CRC64;
MNREEVQLLG FEIVAFAGDA RSKFLEALTA AQAGDFAKAD ALIEEGNNCI AEAHRAQTSL
LAKEAQGDDI AYSVTMMHGQ DHLMTTILLK DLMKHLLEFY KRG
