PTLA_LACCA
ID PTLA_LACCA Reviewed; 112 AA.
AC P11502;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=PTS system lactose-specific EIIA component {ECO:0000303|PubMed:3130296};
DE AltName: Full=EIIA-Lac {ECO:0000303|PubMed:3130296};
DE AltName: Full=EIII-Lac {ECO:0000303|PubMed:3130296};
DE AltName: Full=FIII-Lac {ECO:0000303|PubMed:3130296};
DE AltName: Full=Lactose-specific phosphotransferase enzyme IIA component {ECO:0000303|PubMed:3130296};
GN Name=lacF {ECO:0000303|PubMed:3130296};
OS Lactobacillus casei.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lacticaseibacillus.
OX NCBI_TaxID=1582;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 3-20, FUNCTION,
RP CATALYTIC ACTIVITY, AND SUBUNIT.
RC STRAIN=64H;
RX PubMed=3130296; DOI=10.1016/0378-1119(88)90565-3;
RA Alpert C.-A., Chassy B.M.;
RT "Molecular cloning and nucleotide sequence of the factor IIIlac gene of
RT Lactobacillus casei.";
RL Gene 62:277-288(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 393 / DSM 20011 / BCRC 10697 / JCM 1134 / NBRC 15883 / NCIMB
RC 11970 / NCDO 161 / WDCM 00100;
RX PubMed=9066115; DOI=10.1111/j.1574-6968.1997.tb10271.x;
RA Gosalbes M.J., Monedero V., Alpert C.-A., Perez-Martinez G.;
RT "Establishing a model to study the regulation of the lactose operon in
RT Lactobacillus casei.";
RL FEMS Microbiol. Lett. 148:83-89(1997).
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:0000269|PubMed:3130296}.
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:3130296}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB02558.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; M20150; AAA25239.1; -; Genomic_DNA.
DR EMBL; Z80834; CAB02558.1; ALT_INIT; Genomic_DNA.
DR PIR; B29898; B29898.
DR AlphaFoldDB; P11502; -.
DR SMR; P11502; -.
DR STRING; 1582.AAW28_06700; -.
DR eggNOG; COG1447; Bacteria.
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..112
FT /note="PTS system lactose-specific EIIA component"
FT /id="PRO_0000186596"
FT DOMAIN 6..104
FT /note="PTS EIIA type-3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00418"
FT ACT_SITE 80
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P0A0D6"
FT BINDING 83
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 80
FT /note="Phosphohistidine; by HPr"
FT /evidence="ECO:0000250|UniProtKB:P0A0D6,
FT ECO:0000255|PROSITE-ProRule:PRU00418"
SQ SEQUENCE 112 AA; 12496 MW; 648B7E9D70D79E07 CRC64;
MMATKEEISM VGFALVAYAG DARTAAVHAL DAAEAGDFDK ANELVEKAQQ DINEAHNQQT
QLLSQEAGGA EMDVTFIMVH GQDTLMTTML LIDETRYMIR MFKRIKELEN KQ
