ID   PTLA_LACLL              Reviewed;         105 AA.
AC   P23532;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   13-SEP-2023, entry version 129.
DE   RecName: Full=PTS system lactose-specific EIIA component {ECO:0000303|PubMed:2125052};
DE   AltName: Full=EIIA-Lac {ECO:0000303|PubMed:2125052};
DE   AltName: Full=EIII-Lac {ECO:0000303|PubMed:2125052};
DE   AltName: Full=Lactose-specific phosphotransferase enzyme IIA component {ECO:0000303|PubMed:2125052};
GN   Name=lacF {ECO:0000303|PubMed:2125052};
OS   Lactococcus lactis subsp. lactis (Streptococcus lactis).
OG   Plasmid pLP712.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=1360;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-23, FUNCTION,
RP   MUTAGENESIS OF GLY-18, SUBUNIT, OPERON STRUCTURE, AND INDUCTION.
RC   STRAIN=MG1820;
RX   PubMed=2125052; DOI=10.1016/s0021-9258(18)45741-9;
RA   de Vos W.M., Boerrigter I.J., van Rooyen R.J., Reiche B., Hengstenberg W.;
RT   "Characterization of the lactose-specific enzymes of the phosphotransferase
RT   system in Lactococcus lactis.";
RL   J. Biol. Chem. 265:22554-22560(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11.
RC   STRAIN=MG1820;
RX   PubMed=1901863; DOI=10.1016/s0021-9258(20)89626-4;
RA   van Rooijen R.J., van Schalkwijk S., de Vos W.M.;
RT   "Molecular cloning, characterization, and nucleotide sequence of the
RT   tagatose 6-phosphate pathway gene cluster of the lactose operon of
RT   Lactococcus lactis.";
RL   J. Biol. Chem. 266:7176-7181(1991).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH MAGNESIUM ION,
RP   COFACTOR, ACTIVE SITE, PHOSPHORYLATION AT HIS-78, AND SUBUNIT.
RX   PubMed=9261069; DOI=10.1016/s0969-2126(97)00232-3;
RA   Sliz P., Engelmann R., Hengstenberg W., Pai E.F.;
RT   "The structure of enzyme IIAlactose from Lactococcus lactis reveals a new
RT   fold and points to possible interactions of a multicomponent system.";
RL   Structure 5:775-788(1997).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS), AND SUBUNIT.
RA   Sliz P., Koch B., Hengstenberg W., Pai E.F.;
RT   "Structure of Asp81Leu Enzyme IIa from the Lactose specific PTS from
RT   Lactococcus lactis.";
RL   Submitted (MAY-1999) to the PDB data bank.
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:0000305|PubMed:2125052}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:9261069};
CC       Note=Binds 1 Mg(2+) ion per trimer. {ECO:0000269|PubMed:9261069};
CC   -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:2125052,
CC       ECO:0000269|PubMed:9261069, ECO:0000269|Ref.4}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- INDUCTION: By lactose. The operon consists of lacABCDFEGX. A second
CC       transcript of only lacF and lacE is also lactose-induced.
CC       {ECO:0000269|PubMed:2125052}.
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   -!- MISCELLANEOUS: This gene was sequenced from pMG820, a laboratory-
CC       derived deletion of the naturally occurring plasmid pLP712.
CC       {ECO:0000269|PubMed:2125052}.
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DR   EMBL; M60447; AAA25181.1; -; Genomic_DNA.
DR   EMBL; M65190; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; A23696; A23696.
DR   RefSeq; WP_014011534.1; NZ_WJUM01000040.1.
DR   RefSeq; YP_004761516.1; NC_015862.1.
DR   PDB; 1E2A; X-ray; 2.30 A; A/B/C=1-105.
DR   PDB; 2E2A; X-ray; 2.10 A; A/B/C=1-105.
DR   PDBsum; 1E2A; -.
DR   PDBsum; 2E2A; -.
DR   AlphaFoldDB; P23532; -.
DR   SMR; P23532; -.
DR   iPTMnet; P23532; -.
DR   EvolutionaryTrace; P23532; -.
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   Gene3D; 1.20.58.80; Phosphotransferase system, lactose/cellobiose-type IIA subunit; 1.
DR   InterPro; IPR003188; PTS_IIA_lac/cel.
DR   InterPro; IPR036542; PTS_IIA_lac/cel_sf.
DR   NCBIfam; TIGR00823; EIIA-LAC; 1.
DR   PANTHER; PTHR34382:SF9; PHOSPHOTRANSFERASE SYSTEM SUGAR-SPECIFIC EII COMPONENT; 1.
DR   PANTHER; PTHR34382; PTS SYSTEM N,N'-DIACETYLCHITOBIOSE-SPECIFIC EIIA COMPONENT; 1.
DR   Pfam; PF02255; PTS_IIA; 1.
DR   PIRSF; PIRSF000699; PTS_IILac_III; 1.
DR   SUPFAM; SSF46973; Enzyme IIa from lactose specific PTS, IIa-lac; 1.
DR   PROSITE; PS51095; PTS_EIIA_TYPE_3; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Direct protein sequencing; Magnesium;
KW   Metal-binding; Phosphoprotein; Phosphotransferase system; Plasmid;
KW   Sugar transport; Transferase; Transport.
FT   CHAIN           1..105
FT                   /note="PTS system lactose-specific EIIA component"
FT                   /id="PRO_0000186597"
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:0000305|PubMed:9261069"
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:0000269|PubMed:9261069"
FT   MOD_RES         78
FT                   /note="Phosphohistidine; by HPr"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00418,
FT                   ECO:0000305|PubMed:9261069"
FT   MUTAGEN         18
FT                   /note="G->E: No activity."
FT                   /evidence="ECO:0000269|PubMed:2125052"
FT   HELIX           3..32
FT                   /evidence="ECO:0007829|PDB:2E2A"
FT   HELIX           36..65
FT                   /evidence="ECO:0007829|PDB:2E2A"
FT   HELIX           74..103
FT                   /evidence="ECO:0007829|PDB:2E2A"
SQ   SEQUENCE   105 AA;  11448 MW;  D2ACDEF3433A8C6B CRC64;
     MNREEMTLLG FEIVAYAGDA RSKLLEALKA AENGDFAKAD SLVVEAGSCI AEAHSSQTGM
     LAREASGEEL PYSVTMMHGQ DHLMTTILLK DVIHHLIELY KRGAK
//