LACC_STAAC
ID LACC_STAAC Reviewed; 310 AA.
AC Q5HE12;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 108.
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=SACOL2184;
OS Staphylococcus aureus (strain COL).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93062;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COL;
RX PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA Fraser C.M.;
RT "Insights on evolution of virulence and resistance from the complete genome
RT analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT strain.";
RL J. Bacteriol. 187:2426-2438(2005).
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; CP000046; AAW37060.1; -; Genomic_DNA.
DR RefSeq; WP_000604135.1; NC_002951.2.
DR PDB; 2Q5R; X-ray; 2.30 A; A/B/C/D=1-310.
DR PDBsum; 2Q5R; -.
DR AlphaFoldDB; Q5HE12; -.
DR SMR; Q5HE12; -.
DR EnsemblBacteria; AAW37060; AAW37060; SACOL2184.
DR KEGG; sac:SACOL2184; -.
DR HOGENOM; CLU_050013_5_0_9; -.
DR OMA; QLNEPGP; -.
DR UniPathway; UPA00704; UER00715.
DR EvolutionaryTrace; Q5HE12; -.
DR Proteomes; UP000000530; Chromosome.
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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Kinase; Lactose metabolism; Nucleotide-binding;
KW Transferase.
FT CHAIN 1..310
FT /note="Tagatose-6-phosphate kinase"
FT /id="PRO_0000203917"
FT STRAND 2..8
FT /evidence="ECO:0007829|PDB:2Q5R"
FT STRAND 10..18
FT /evidence="ECO:0007829|PDB:2Q5R"
FT STRAND 24..29
FT /evidence="ECO:0007829|PDB:2Q5R"
FT STRAND 32..37
FT /evidence="ECO:0007829|PDB:2Q5R"
FT HELIX 38..49
FT /evidence="ECO:0007829|PDB:2Q5R"
FT STRAND 53..59
FT /evidence="ECO:0007829|PDB:2Q5R"
FT HELIX 61..73
FT /evidence="ECO:0007829|PDB:2Q5R"
FT STRAND 88..95
FT /evidence="ECO:0007829|PDB:2Q5R"
FT STRAND 98..104
FT /evidence="ECO:0007829|PDB:2Q5R"
FT HELIX 111..125
FT /evidence="ECO:0007829|PDB:2Q5R"
FT STRAND 129..135
FT /evidence="ECO:0007829|PDB:2Q5R"
FT HELIX 145..156
FT /evidence="ECO:0007829|PDB:2Q5R"
FT STRAND 160..163
FT /evidence="ECO:0007829|PDB:2Q5R"
FT HELIX 166..174
FT /evidence="ECO:0007829|PDB:2Q5R"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:2Q5R"
FT STRAND 180..182
FT /evidence="ECO:0007829|PDB:2Q5R"
FT HELIX 186..193
FT /evidence="ECO:0007829|PDB:2Q5R"
FT HELIX 201..208
FT /evidence="ECO:0007829|PDB:2Q5R"
FT HELIX 211..213
FT /evidence="ECO:0007829|PDB:2Q5R"
FT STRAND 217..222
FT /evidence="ECO:0007829|PDB:2Q5R"
FT STRAND 228..232
FT /evidence="ECO:0007829|PDB:2Q5R"
FT STRAND 235..240
FT /evidence="ECO:0007829|PDB:2Q5R"
FT HELIX 252..265
FT /evidence="ECO:0007829|PDB:2Q5R"
FT HELIX 270..285
FT /evidence="ECO:0007829|PDB:2Q5R"
FT STRAND 287..289
FT /evidence="ECO:0007829|PDB:2Q5R"
FT HELIX 295..297
FT /evidence="ECO:0007829|PDB:2Q5R"
FT HELIX 298..302
FT /evidence="ECO:0007829|PDB:2Q5R"
FT STRAND 306..309
FT /evidence="ECO:0007829|PDB:2Q5R"
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
