PTLA_STAAU
ID PTLA_STAAU Reviewed; 103 AA.
AC P0A0D6; P02909;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=PTS system lactose-specific EIIA component {ECO:0000303|PubMed:2824493};
DE AltName: Full=EIIA-Lac {ECO:0000303|PubMed:2824493};
DE AltName: Full=EIII-Lac {ECO:0000303|PubMed:2824493};
DE AltName: Full=Lactose-specific phosphotransferase enzyme IIA component {ECO:0000303|PubMed:2824493};
GN Name=lacF {ECO:0000303|PubMed:2824493};
OS Staphylococcus aureus.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1280;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=2824493; DOI=10.1016/s0021-9258(18)49276-9;
RA Breidt F. Jr., Hengstenberg W., Finkeldei U., Stewart G.C.;
RT "Identification of the genes for the lactose-specific components of the
RT phosphotransferase system in the lac operon of Staphylococcus aureus.";
RL J. Biol. Chem. 262:16444-16449(1987).
RN [2]
RP PROTEIN SEQUENCE OF 1-31, AND SUBUNIT.
RX PubMed=4684715; DOI=10.1016/s0021-9258(19)44356-1;
RA Hays J.B., Simoni R.D., Roseman S.;
RT "Sugar transport. V. A trimeric lactose-specific phosphocarrier protein of
RT the Staphylococcus aureus phosphotransferase system.";
RL J. Biol. Chem. 248:941-956(1973).
RN [3]
RP PROTEIN SEQUENCE OF 1-38, AND SUBUNIT.
RX PubMed=7138836; DOI=10.1021/bi00263a006;
RA Deutscher J., Beyreuther K., Sobek H.M., Stuber K., Hengstenberg W.;
RT "Phosphoenolpyruvate-dependent phosphotransferase system of Staphylococcus
RT aureus: factor IIIlac, a trimeric phospho-carrier protein that also acts as
RT a phase transfer catalyst.";
RL Biochemistry 21:4867-4873(1982).
RN [4]
RP PROTEIN SEQUENCE.
RX PubMed=4096897; DOI=10.1021/bi00326a016;
RA Stuber K., Deutscher J., Sobek H.M., Hengstenberg W., Beyreuther K.;
RT "Amino acid sequence of the amphiphilic phosphocarrier protein factor
RT IIILac of the lactose-specific phosphotransferase system of
RT Staphylococcus.";
RL Biochemistry 24:1164-1168(1985).
RN [5]
RP INDUCTION.
RX PubMed=14086091; DOI=10.1128/jb.86.6.1211-1215.1963;
RA McClatchy J.K., Rosenblum E.D.;
RT "Induction of lactose utilization in Staphylococcus aureus.";
RL J. Bacteriol. 86:1211-1215(1963).
RN [6]
RP INDUCTION.
RX PubMed=5665876; DOI=10.1016/0006-291x(68)90634-7;
RA Simoni R.D., Smith M.F., Roseman S.;
RT "Resolution of a staphylococcal phosphotransferase system into four protein
RT components and its relation to sugar transport.";
RL Biochem. Biophys. Res. Commun. 31:804-811(1968).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
RX PubMed=4567791; DOI=10.1016/s0021-9258(19)44355-x;
RA Simoni R.D., Nakazawa T., Hays J.B., Roseman S.;
RT "Sugar transport. IV. Isolation and characterization of the lactose
RT phosphotransferase system in Staphylococcus aureus.";
RL J. Biol. Chem. 248:932-940(1973).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND REACTION MECHANISM.
RX PubMed=4684716; DOI=10.1016/s0021-9258(19)44357-3;
RA Simoni R.D., Hays J.B., Nakazawa T., Roseman S.;
RT "Sugar transport. VI. Phosphoryl transfer in the lactose phosphotransferase
RT system of Staphylococcus aureus.";
RL J. Biol. Chem. 248:957-965(1973).
RN [9]
RP ACTIVE SITE, AND PHOSPHORYLATION AT HIS-78.
RX PubMed=7306504; DOI=10.1021/bi00524a041;
RA Kalbitzer H.R., Deutscher J., Hengstenberg W., Rosch P.;
RT "Phosphoenolpyruvate-dependent phosphotransferase system of Staphylococcus
RT aureus: 1H nuclear magnetic resonance studies on phosphorylated and
RT unphosphorylated factor IIIlac and its interaction with the phosphocarrier
RT protein HPr.";
RL Biochemistry 20:6178-6185(1981).
RN [10]
RP ACTIVE SITE, PHOSPHORYLATION AT HIS-78, AND MUTAGENESIS OF HIS-78 AND
RP HIS-82.
RX PubMed=1881873; DOI=10.1093/protein/4.4.469;
RA Finkeldei U., Kalbitzer H.R., Eisermann R., Stewart G.C., Hengstenberg W.;
RT "Enzyme IIIlac of the staphylococcal phosphoenolpyruvate-dependent
RT phosphotransferase system: site-specific mutagenesis of histidine residues,
RT biochemical characterization and 1H-NMR studies.";
RL Protein Eng. 4:469-473(1991).
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, but can
CC also use galactose, isopropyl beta-thio-galactopyranoside and
CC thiomethyl beta-D-galactopyranoside (TMG) as substrates.
CC {ECO:0000269|PubMed:4567791, ECO:0000269|PubMed:4684716,
CC ECO:0000305|PubMed:2824493}.
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:0000269|PubMed:4684715,
CC ECO:0000269|PubMed:7138836}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: Induced by lactose, galactose and galactose-6-P. Repressed
CC by glucose. {ECO:0000269|PubMed:14086091, ECO:0000269|PubMed:5665876}.
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}.
CC -!- CAUTION: His-82, rather than His-78 in the same tryptic peptide, was
CC identified in PubMed:7306504 as the probable site of phosphorylation.
CC This misidentification was corrected in later work and confirmed in
CC structural work on the enzyme from Lactococcus lactis.
CC {ECO:0000269|PubMed:1881873, ECO:0000269|PubMed:7138836,
CC ECO:0000269|PubMed:7306504}.
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DR EMBL; J03479; AAA26648.1; -; Genomic_DNA.
DR PIR; A03406; WQSA3L.
DR RefSeq; WP_001078309.1; NZ_WYDB01000011.1.
DR AlphaFoldDB; P0A0D6; -.
DR SMR; P0A0D6; -.
DR TCDB; 4.A.3.1.1; the pts lactose-n,n'-diacetylchitobiose-Beta-glucoside (lac) family.
DR iPTMnet; P0A0D6; -.
DR OMA; HAHTIQT; -.
DR SABIO-RK; P0A0D6; -.
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 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Magnesium; Metal-binding;
KW Phosphoprotein; Phosphotransferase system; Sugar transport; Transferase;
KW Transport.
FT CHAIN 1..103
FT /note="PTS system lactose-specific EIIA component"
FT /id="PRO_0000186604"
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:0000269|PubMed:1881873,
FT ECO:0000269|PubMed:7306504"
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:0000255|PROSITE-ProRule:PRU00418,
FT ECO:0000305|PubMed:1881873, ECO:0000305|PubMed:7306504"
FT MUTAGEN 78
FT /note="H->S: Abolished activity."
FT /evidence="ECO:0000269|PubMed:1881873"
FT MUTAGEN 82
FT /note="H->S: Reduced activity."
FT /evidence="ECO:0000269|PubMed:1881873"
FT CONFLICT 52
FT /note="E -> Q (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 93..95
FT /note="MKH -> HKK (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 103 AA; 11370 MW; CF2DB98F139E8131 CRC64;
MNREEVQLLG FEIVAFAGDA RSKFLEALTA AQAGDFAKAD ALIEEGNNCI AEAHRAQTSL
LAKEAQGDDI AYSVTMMHGQ DHLMTTILLK DLMKHLLEFY KRG
