ID   LACC_STAA9              Reviewed;         310 AA.
AC   A5IUY2;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 82.
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=SaurJH9_2224;
OS   Staphylococcus aureus (strain JH9).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=359786;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JH9;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Chain P.,
RA   Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Tomasz A., Richardson P.;
RT   "Complete sequence of chromosome of Staphylococcus aureus subsp. aureus
RT   JH9.";
RL   Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000703; ABQ50005.1; -; Genomic_DNA.
DR   RefSeq; WP_000604134.1; NC_009487.1.
DR   AlphaFoldDB; A5IUY2; -.
DR   SMR; A5IUY2; -.
DR   KEGG; saj:SaurJH9_2224; -.
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_1000087791"
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