LACC_STAA8
ID LACC_STAA8 Reviewed; 310 AA.
AC P0A0B9; P11099; Q2G2R2;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 107.
DE RecName: Full=Tagatose-6-phosphate kinase {ECO:0000255|HAMAP-Rule:MF_01557};
DE EC=2.7.1.144 {ECO:0000255|HAMAP-Rule:MF_01557};
DE AltName: Full=Phosphotagatokinase {ECO:0000255|HAMAP-Rule:MF_01557};
GN Name=lacC {ECO:0000255|HAMAP-Rule:MF_01557};
GN OrderedLocusNames=SAOUHSC_02453;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2543958; DOI=10.1093/nar/17.10.3980;
RA Rosey E.L., Stewart G.C.;
RT "The nucleotide sequence of the lacC and lacD genes of Staphylococcus
RT aureus.";
RL Nucleic Acids Res. 17:3980-3980(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
RN [3]
RP CHARACTERIZATION.
RX PubMed=1655695; DOI=10.1128/jb.173.19.5992-5998.1991;
RA Rosey E.L., Oskouian B., Stewart G.C.;
RT "Lactose metabolism by Staphylococcus aureus: characterization of lacABCD,
RT the structural genes of the tagatose 6-phosphate pathway.";
RL J. Bacteriol. 173:5992-5998(1991).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-tagatofuranose 6-phosphate = ADP + D-tagatofuranose
CC 1,6-bisphosphate + H(+); Xref=Rhea:RHEA:12420, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58694, ChEBI:CHEBI:58695,
CC ChEBI:CHEBI:456216; EC=2.7.1.144; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01557};
CC -!- PATHWAY: Carbohydrate metabolism; D-tagatose 6-phosphate degradation;
CC D-glyceraldehyde 3-phosphate and glycerone phosphate from D-tagatose 6-
CC phosphate: step 1/2. {ECO:0000255|HAMAP-Rule:MF_01557}.
CC -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family. LacC
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01557}.
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DR EMBL; X14827; CAA32935.1; -; Genomic_DNA.
DR EMBL; CP000253; ABD31473.1; -; Genomic_DNA.
DR PIR; S04358; S04358.
DR RefSeq; WP_000604135.1; NZ_LS483365.1.
DR RefSeq; YP_500920.1; NC_007795.1.
DR PDB; 2JG1; X-ray; 2.00 A; A/B/C/D=1-310.
DR PDB; 2JGV; X-ray; 2.00 A; A/B/C/D=1-310.
DR PDBsum; 2JG1; -.
DR PDBsum; 2JGV; -.
DR AlphaFoldDB; P0A0B9; -.
DR SMR; P0A0B9; -.
DR STRING; 1280.SAXN108_2446; -.
DR EnsemblBacteria; ABD31473; ABD31473; SAOUHSC_02453.
DR GeneID; 3919016; -.
DR KEGG; sao:SAOUHSC_02453; -.
DR PATRIC; fig|93061.5.peg.2212; -.
DR eggNOG; COG1105; Bacteria.
DR HOGENOM; CLU_050013_5_0_9; -.
DR OMA; QLNEPGP; -.
DR BRENDA; 2.7.1.144; 3352.
DR UniPathway; UPA00704; UER00715.
DR EvolutionaryTrace; P0A0B9; -.
DR PRO; PR:P0A0B9; -.
DR Proteomes; UP000008816; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0008662; F:1-phosphofructokinase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008443; F:phosphofructokinase activity; IBA:GO_Central.
DR GO; GO:0009024; F:tagatose-6-phosphate kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:2001059; P:D-tagatose 6-phosphate catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0019512; P:lactose catabolic process via tagatose-6-phosphate; IEA:UniProtKB-UniRule.
DR CDD; cd01164; FruK_PfkB_like; 1.
DR Gene3D; 3.40.1190.20; -; 1.
DR HAMAP; MF_01557; LacC; 1.
DR InterPro; IPR002173; Carboh/pur_kinase_PfkB_CS.
DR InterPro; IPR005926; LacC.
DR InterPro; IPR011611; PfkB_dom.
DR InterPro; IPR029056; Ribokinase-like.
DR InterPro; IPR017583; Tagatose/fructose_Pkinase.
DR Pfam; PF00294; PfkB; 1.
DR PIRSF; PIRSF000535; 1PFK/6PFK/LacC; 1.
DR SUPFAM; SSF53613; SSF53613; 1.
DR TIGRFAMs; TIGR03168; 1-PFK; 1.
DR TIGRFAMs; TIGR01231; lacC; 1.
DR PROSITE; PS00583; PFKB_KINASES_1; 1.
DR PROSITE; PS00584; PFKB_KINASES_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Kinase; Lactose metabolism; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..310
FT /note="Tagatose-6-phosphate kinase"
FT /id="PRO_0000203916"
FT STRAND 2..8
FT /evidence="ECO:0007829|PDB:2JG1"
FT STRAND 10..18
FT /evidence="ECO:0007829|PDB:2JG1"
FT STRAND 24..29
FT /evidence="ECO:0007829|PDB:2JG1"
FT STRAND 32..36
FT /evidence="ECO:0007829|PDB:2JG1"
FT HELIX 38..49
FT /evidence="ECO:0007829|PDB:2JG1"
FT STRAND 53..60
FT /evidence="ECO:0007829|PDB:2JG1"
FT HELIX 61..73
FT /evidence="ECO:0007829|PDB:2JG1"
FT STRAND 81..85
FT /evidence="ECO:0007829|PDB:2JG1"
FT STRAND 88..95
FT /evidence="ECO:0007829|PDB:2JG1"
FT STRAND 98..104
FT /evidence="ECO:0007829|PDB:2JG1"
FT HELIX 111..124
FT /evidence="ECO:0007829|PDB:2JG1"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:2JG1"
FT STRAND 129..135
FT /evidence="ECO:0007829|PDB:2JG1"
FT HELIX 145..154
FT /evidence="ECO:0007829|PDB:2JG1"
FT TURN 155..157
FT /evidence="ECO:0007829|PDB:2JG1"
FT STRAND 160..163
FT /evidence="ECO:0007829|PDB:2JG1"
FT HELIX 166..173
FT /evidence="ECO:0007829|PDB:2JG1"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:2JG1"
FT STRAND 180..182
FT /evidence="ECO:0007829|PDB:2JG1"
FT HELIX 186..192
FT /evidence="ECO:0007829|PDB:2JG1"
FT HELIX 201..209
FT /evidence="ECO:0007829|PDB:2JG1"
FT HELIX 211..213
FT /evidence="ECO:0007829|PDB:2JG1"
FT STRAND 217..222
FT /evidence="ECO:0007829|PDB:2JG1"
FT HELIX 224..226
FT /evidence="ECO:0007829|PDB:2JG1"
FT STRAND 228..232
FT /evidence="ECO:0007829|PDB:2JG1"
FT STRAND 235..240
FT /evidence="ECO:0007829|PDB:2JG1"
FT HELIX 252..265
FT /evidence="ECO:0007829|PDB:2JG1"
FT HELIX 270..285
FT /evidence="ECO:0007829|PDB:2JG1"
FT STRAND 287..291
FT /evidence="ECO:0007829|PDB:2JG1"
FT HELIX 295..297
FT /evidence="ECO:0007829|PDB:2JG1"
FT HELIX 298..302
FT /evidence="ECO:0007829|PDB:2JG1"
FT STRAND 306..309
FT /evidence="ECO:0007829|PDB:2JG1"
SQ SEQUENCE 310 AA; 33853 MW; D8A085EA1BD60543 CRC64;
MILTLTLNPS VDISYPLTAL KLDDVNRVQE VSKTAGGKGL NVTRVLAQVG EPVLASGFIG
GELGQFIAKK LDHADIKHAF YNIKGETRNC IAILHEGQQT EILEQGPEID NQEAAGFIKH
FEQLLEKVEA VAISGSLPKG LNQDYYAQII ERCQNKGVPV ILDCSGATLQ TVLENPYKPT
VIKPNISELY QLLNQPLDES LESLKQAVSQ PLFEGIEWII VSLGAQGAFA KHNHTFYRVN
IPTISVLNPV GSGDSTVAGI TSAILNHEND HDLLKKANTL GMLNAQEAQT GYVNLNNYDD
LFNQIEVLEV
