ID   LACC_STAA1              Reviewed;         310 AA.
AC   A7X575;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 84.
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=SAHV_2177;
OS   Staphylococcus aureus (strain Mu3 / ATCC 700698).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=418127;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mu3 / ATCC 700698;
RX   PubMed=17954695; DOI=10.1128/aac.00534-07;
RA   Neoh H.-M., Cui L., Yuzawa H., Takeuchi F., Matsuo M., Hiramatsu K.;
RT   "Mutated response regulator graR is responsible for phenotypic conversion
RT   of Staphylococcus aureus from heterogeneous vancomycin-intermediate
RT   resistance to vancomycin-intermediate resistance.";
RL   Antimicrob. Agents Chemother. 52:45-53(2008).
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; AP009324; BAF79060.1; -; Genomic_DNA.
DR   RefSeq; WP_000604134.1; NC_009782.1.
DR   AlphaFoldDB; A7X575; -.
DR   SMR; A7X575; -.
DR   KEGG; saw:SAHV_2177; -.
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_1000068935"
SQ   SEQUENCE   310 AA;  33895 MW;  D8B1655F0A37F543 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
     IPTINVLNPV GSGDSTVAGI TSAILNHEND HDLLKKANTL GMLNAQEAQT GYVNLNNYDE
     LFNQIEVLEV