ID   LACC_STAAB              Reviewed;         310 AA.
AC   Q2YYJ5;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 99.
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}; OrderedLocusNames=SAB2074c;
OS   Staphylococcus aureus (strain bovine RF122 / ET3-1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=273036;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=bovine RF122 / ET3-1;
RX   PubMed=17971880; DOI=10.1371/journal.pone.0001120;
RA   Herron-Olson L., Fitzgerald J.R., Musser J.M., Kapur V.;
RT   "Molecular correlates of host specialization in Staphylococcus aureus.";
RL   PLoS ONE 2:E1120-E1120(2007).
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; AJ938182; CAI81763.1; -; Genomic_DNA.
DR   RefSeq; WP_000604148.1; NC_007622.1.
DR   AlphaFoldDB; Q2YYJ5; -.
DR   SMR; Q2YYJ5; -.
DR   KEGG; sab:SAB2074c; -.
DR   HOGENOM; CLU_050013_5_0_9; -.
DR   OMA; QLNEPGP; -.
DR   UniPathway; UPA00704; UER00715.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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   3: Inferred from homology;
KW   ATP-binding; Kinase; Lactose metabolism; Nucleotide-binding; Transferase.
FT   CHAIN           1..310
FT                   /note="Tagatose-6-phosphate kinase"
FT                   /id="PRO_1000068937"
SQ   SEQUENCE   310 AA;  33733 MW;  04A55CB22DCE8362 CRC64;
     MILTLTLNPS VDISYPLTAL KLDDVNRVQE VSKTAGGKGL NVTRVLAQVG EPVLASGFIG
     GELGQFIAKK LDLAGIKHAF YNIKGETRNC IAILHEGQQT EILEQGPEID NQEAAGFIKH
     FEQLLEKVEA VAISGSLPKG LNQDYYAQII ERCQNKGVPV ILDCSGATLQ TVLENPYKPT
     VIKPNISELY QLLNQPLDES LESLKQAVSQ PLFEGVEWII VSLGAQGAFA KHNHTFYRVN
     IPTISVLNPV GSGDSTVAGI TSAILNHEND LDLLKKANTL GMLNAQEAQT GYVNLNNYDD
     LFNQIEVLEV