ID   COAA_BARBK              Reviewed;         314 AA.
AC   A1UU59;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Pantothenate kinase {ECO:0000255|HAMAP-Rule:MF_00215};
DE            EC=2.7.1.33 {ECO:0000255|HAMAP-Rule:MF_00215};
DE   AltName: Full=Pantothenic acid kinase {ECO:0000255|HAMAP-Rule:MF_00215};
GN   Name=coaA {ECO:0000255|HAMAP-Rule:MF_00215};
GN   OrderedLocusNames=BARBAKC583_1263;
OS   Bartonella bacilliformis (strain ATCC 35685 / NCTC 12138 / KC583).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bartonellaceae; Bartonella.
OX   NCBI_TaxID=360095;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35685 / NCTC 12138 / KC583;
RA   Hendrix L., Mohamoud Y., Radune D., Shvartsbeyn A., Daugherty S.,
RA   Dodson R., Durkin A.S., Harkins D., Huot H., Kothari S.P., Madupu R.,
RA   Li J., Nelson W.C., Shrivastava S., Giglio M.G., Haft D., Selengut J.,
RA   Fraser-Ligget C., Seshadri R.;
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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_00215};
CC   -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-
CC       pantothenate: step 1/5. {ECO:0000255|HAMAP-Rule:MF_00215}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00215}.
CC   -!- SIMILARITY: Belongs to the prokaryotic pantothenate kinase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00215}.
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DR   EMBL; CP000524; ABM44441.1; -; Genomic_DNA.
DR   AlphaFoldDB; A1UU59; -.
DR   SMR; A1UU59; -.
DR   STRING; 360095.BARBAKC583_1263; -.
DR   EnsemblBacteria; ABM44441; ABM44441; BARBAKC583_1263.
DR   KEGG; bbk:BARBAKC583_1263; -.
DR   PATRIC; fig|360095.6.peg.1239; -.
DR   eggNOG; COG1072; Bacteria.
DR   HOGENOM; CLU_053818_1_1_5; -.
DR   OMA; RKYTQVS; -.
DR   UniPathway; UPA00241; UER00352.
DR   Proteomes; UP000000643; 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   CDD; cd02025; PanK; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00215; Pantothen_kinase_1; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR004566; PanK.
DR   InterPro; IPR006083; PRK/URK.
DR   PANTHER; PTHR10285:SF139; PTHR10285:SF139; 1.
DR   Pfam; PF00485; PRK; 1.
DR   PIRSF; PIRSF000545; Pantothenate_kin; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00554; panK_bact; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Coenzyme A biosynthesis; Cytoplasm; Kinase;
KW   Nucleotide-binding; Reference proteome; Transferase.
FT   CHAIN           1..314
FT                   /note="Pantothenate kinase"
FT                   /id="PRO_0000325545"
FT   BINDING         92..99
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00215"
SQ   SEQUENCE   314 AA;  36902 MW;  180A8412A449F191 CRC64;
     MYEKYSPYKV FTAQEWSQFR ADTPLTLTFD EIKHLRSLDD PVDLEEVQRI YLSLARLLSC
     HVEAIQNLFQ KRQQFLHQEN IKKNPFIIGI SGSVAVGKST TARILQELLK RWAFNLKVDL
     ITTDGFLYPN AVLQKKNRMN RKGFPDSYDI KKLLHFLSAI KAGISKVSAP LYSHITYDVL
     EDQKVIIDHP DILIVEGVNV LQVNRFPNDK RIVPFVSDFF DFSIYVDAET DMICYWYLER
     FKRLRKTAFQ NPESYFYRYA LLSEEEALKI AENIWRTINL KNLQENILPT RSRADLILRK
     GKNHLVEYVA LRKL