ID   PTLA_STAAW              Reviewed;         103 AA.
AC   P0A0D5; P02909;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 96.
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=MW2117;
OS   Staphylococcus aureus (strain MW2).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=196620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MW2;
RX   PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA   Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA   Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT   "Genome and virulence determinants of high virulence community-acquired
RT   MRSA.";
RL   Lancet 359:1819-1827(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: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; BA000033; BAB95982.1; -; Genomic_DNA.
DR   RefSeq; WP_001078309.1; NC_003923.1.
DR   AlphaFoldDB; P0A0D5; -.
DR   SMR; P0A0D5; -.
DR   EnsemblBacteria; BAB95982; BAB95982; BAB95982.
DR   KEGG; sam:MW2117; -.
DR   HOGENOM; CLU_152490_1_0_9; -.
DR   OMA; HAHTIQT; -.
DR   Proteomes; UP000000418; 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_0000186603"
FT   DOMAIN          4..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