ID   COAW_BACCR              Reviewed;         273 AA.
AC   Q81C81;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 100.
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=BC_2898;
OS   Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS   15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=226900;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373
RC   / NCTC 2599 / NRRL B-3711;
RX   PubMed=12721630; DOI=10.1038/nature01582;
RA   Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA   Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA   Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA   Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.;
RT   "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT   anthracis.";
RL   Nature 423:87-91(2003).
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; AE016877; AAP09847.1; -; Genomic_DNA.
DR   RefSeq; NP_832646.1; NC_004722.1.
DR   RefSeq; WP_000442504.1; NZ_CP034551.1.
DR   AlphaFoldDB; Q81C81; -.
DR   SMR; Q81C81; -.
DR   STRING; 226900.BC_2898; -.
DR   EnsemblBacteria; AAP09847; AAP09847; BC_2898.
DR   KEGG; bce:BC2898; -.
DR   PATRIC; fig|226900.8.peg.2965; -.
DR   HOGENOM; CLU_087521_1_0_9; -.
DR   OMA; VKHIYKD; -.
DR   UniPathway; UPA00241; UER00352.
DR   Proteomes; UP000001417; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004594; F:pantothenate kinase activity; IBA:GO_Central.
DR   GO; GO:0015937; P:coenzyme A biosynthetic process; IBA:GO_Central.
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; Reference proteome; Transferase.
FT   CHAIN           1..273
FT                   /note="Type II pantothenate kinase"
FT                   /id="PRO_0000261339"
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;  29742 MW;  AB2A618378A4959F CRC64;
     MERTIGIDAG GTLTKIAYFN KKKLLTFEKF YSHEQHKIID WIKNNNGIKQ ICITGGKSKL
     LQQLLTGSYK IIELSEFEAT LAGVQFILKE EQHTINNFIL TNIGTGTSIH YVYNEQYIRA
     GGTGVGGGTI MGLSKLLTNI DHFEDVIPLT KVGSRKELDI TVGDIYGGIL SPIDNNLTAS
     NFGKAAITES NNSSSDILAT VQGLVGEVVT ALSLQFAETK NIEHIIYIGS TLCNNVQLQH
     IISSYTEYQN KTPIFLQDGG NSGAIGALLH ATK