ID   COAA_SALPB              Reviewed;         316 AA.
AC   A9N0I2;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 71.
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}; OrderedLocusNames=SPAB_05126;
OS   Salmonella paratyphi B (strain ATCC BAA-1250 / SPB7).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=1016998;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1250 / SPB7;
RG   The Salmonella enterica serovar Paratyphi B Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Fulton R., Cordes M., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (NOV-2007) 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; CP000886; ABX70411.1; -; Genomic_DNA.
DR   RefSeq; WP_000023069.1; NC_010102.1.
DR   AlphaFoldDB; A9N0I2; -.
DR   SMR; A9N0I2; -.
DR   KEGG; spq:SPAB_05126; -.
DR   PATRIC; fig|1016998.12.peg.4807; -.
DR   HOGENOM; CLU_053818_1_1_6; -.
DR   OMA; RKYTQVS; -.
DR   BioCyc; SENT1016998:SPAB_RS20860-MON; -.
DR   UniPathway; UPA00241; UER00352.
DR   Proteomes; UP000008556; 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; Transferase.
FT   CHAIN           1..316
FT                   /note="Pantothenate kinase"
FT                   /id="PRO_1000078059"
FT   BINDING         95..102
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00215"
SQ   SEQUENCE   316 AA;  36236 MW;  54B030D1540853C9 CRC64;
     MSIKEQSLMT PYLQFDRSQW AALRDSVPMT LTEDEIAQLK GINEDLSLEE VAEIYLPLSR
     LLNFYISSNL RRQAVLEQFL GTNGQRIPYI ISIAGSVAVG KSTTARVLQA LLSRWPEHRR
     VELITTDGFL HPNQVLKERG LMKKKGFPES YDMHRLVKFV SDLKSGVPNV TAPVYSHLIY
     DVIPEGDKTV AQPDILILEG LNVLQSGMDY PHDPHHVFVS DFVDFSIYVD APEELLQTWY
     INRFLKFREG AFTDPDSYFH NYAKLSKEEA VNTATSLWKE INWLNLKQNI LPTRERASLI
     MTKSANHAVE QVRLRK