ID   COAW_BACC4              Reviewed;         273 AA.
AC   B7H5Z8;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 65.
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};
GN   OrderedLocusNames=BCB4264_A2918;
OS   Bacillus cereus (strain B4264).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=405532;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4264;
RA   Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A.,
RA   Ravel J., Sutton G.;
RT   "Genome sequence of Bacillus cereus B4264.";
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001176; ACK62974.1; -; Genomic_DNA.
DR   RefSeq; WP_000442501.1; NZ_VEHB01000001.1.
DR   AlphaFoldDB; B7H5Z8; -.
DR   SMR; B7H5Z8; -.
DR   EnsemblBacteria; ACK62974; ACK62974; BCB4264_A2918.
DR   KEGG; bcb:BCB4264_A2918; -.
DR   HOGENOM; CLU_087521_1_0_9; -.
DR   OMA; VKHIYKD; -.
DR   UniPathway; UPA00241; UER00352.
DR   Proteomes; UP000007096; Chromosome.
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..273
FT                   /note="Type II pantothenate kinase"
FT                   /id="PRO_1000140208"
FT   ACT_SITE        76
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01273"
FT   BINDING         8..15
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01273"
FT   BINDING         105
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01273"
FT   BINDING         127..131
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01273"
FT   BINDING         143
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01273"
FT   BINDING         230
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01273"
SQ   SEQUENCE   273 AA;  29756 MW;  6838F18378B60592 CRC64;
     MERTIGIDAG GTLTKIAYFN KKKLLTFEKF YSHEQHKIID WIKNNNGIKQ ICITGGKSKL
     LQQLLTGSYK IIELSEFEAT LAGVQFILKE EQHTINNFIL TNIGTGTSIH YVYNEQYIRA
     GGTGVGGGTI MGLSKLLTNI DHFEDIIPLT KVGSRKELDI TVGDIYGGIL SPIDNNLTAS
     NFGKAAITES NNSSSDILAT VQGLVGEVVT ALSLQFAETK NIEHIIYIGS TLCNNVQLQH
     IISSYTEYQN KTPIFLQDGG NSGAIGALLH ATK