ID   COAW_STAAB              Reviewed;         267 AA.
AC   Q2YUM3;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Type II pantothenate kinase {ECO:0000255|HAMAP-Rule:MF_01273};
DE            EC=2.7.1.33 {ECO:0000255|HAMAP-Rule:MF_01273};
DE   AltName: Full=PanK-II {ECO:0000255|HAMAP-Rule:MF_01273};
DE   AltName: Full=Pantothenic acid kinase {ECO:0000255|HAMAP-Rule:MF_01273};
GN   Name=coaW {ECO:0000255|HAMAP-Rule:MF_01273}; OrderedLocusNames=SAB2014;
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   -!- FUNCTION: Catalyzes the phosphorylation of pantothenate (Pan), the
CC       first step in CoA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01273}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP +
CC         H(+); Xref=Rhea:RHEA:16373, ChEBI:CHEBI:10986, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29032, ChEBI:CHEBI:30616, ChEBI:CHEBI:456216;
CC         EC=2.7.1.33; Evidence={ECO:0000255|HAMAP-Rule:MF_01273};
CC   -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-
CC       pantothenate: step 1/5. {ECO:0000255|HAMAP-Rule:MF_01273}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01273}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01273}.
CC   -!- SIMILARITY: Belongs to the type II pantothenate kinase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01273}.
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DR   EMBL; AJ938182; CAI81703.1; -; Genomic_DNA.
DR   RefSeq; WP_000862722.1; NC_007622.1.
DR   AlphaFoldDB; Q2YUM3; -.
DR   SMR; Q2YUM3; -.
DR   KEGG; sab:SAB2014; -.
DR   HOGENOM; CLU_087521_1_0_9; -.
DR   OMA; VKHIYKD; -.
DR   UniPathway; UPA00241; UER00352.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004594; F:pantothenate kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0015937; P:coenzyme A biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   HAMAP; MF_01273; Pantothen_kinase_2; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR004567; Type_II_PanK.
DR   InterPro; IPR011602; Type_II_PanK_bac.
DR   PANTHER; PTHR12280; PTHR12280; 1.
DR   Pfam; PF03630; Fumble; 1.
DR   PIRSF; PIRSF036940; PanK_bac_aCoA; 1.
DR   SUPFAM; SSF53067; SSF53067; 1.
DR   TIGRFAMs; TIGR00555; panK_eukar; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Coenzyme A biosynthesis; Cytoplasm; Kinase;
KW   Nucleotide-binding; Transferase.
FT   CHAIN           1..267
FT                   /note="Type II pantothenate kinase"
FT                   /id="PRO_0000261343"
FT   ACT_SITE        70
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01273"
FT   BINDING         6..13
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01273"
FT   BINDING         99
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01273"
FT   BINDING         121..125
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01273"
FT   BINDING         137
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01273"
FT   BINDING         225
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01273"
SQ   SEQUENCE   267 AA;  29111 MW;  3C50BBC6D81F2D9A CRC64;
     MKVGIDAGGT LIKIIQEQDN QRTFKTELTK NIDQVVEWLN QQQIEKLCLT GGNAGVIAEN
     INIPAQIFVE FDAASQGLGI LLKEQGHDLA DYIFANVGTG TSLHYFDGQS QRRVGGIGTG
     GGMIQGLGYL LSQITDYKQL TDMAQHGDRN TIDLKVRHIY KDTEPPIPGD LTAANFGHVL
     HHLDADFTPS NKLAAVIGVV GEVVTTMAIT VAREFKTENI VYIGSSFHNN ALLRKVVEDY
     TVLRGCKPYY VENGAFSGAI GALYLEK