PTLA_LACLL
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 03-AUG-2022, entry version 125.
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; Firmicutes; 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 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 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
