ID   COAA_STRPJ              Reviewed;         306 AA.
AC   B8ZNP1;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 72.
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=SPN23F07600;
OS   Streptococcus pneumoniae (strain ATCC 700669 / Spain 23F-1).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=561276;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700669 / Spain 23F-1;
RX   PubMed=19114491; DOI=10.1128/jb.01343-08;
RA   Croucher N.J., Walker D., Romero P., Lennard N., Paterson G.K., Bason N.C.,
RA   Mitchell A.M., Quail M.A., Andrew P.W., Parkhill J., Bentley S.D.,
RA   Mitchell T.J.;
RT   "Role of conjugative elements in the evolution of the multidrug-resistant
RT   pandemic clone Streptococcus pneumoniae Spain23F ST81.";
RL   J. Bacteriol. 191:1480-1489(2009).
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; FM211187; CAR68600.1; -; Genomic_DNA.
DR   RefSeq; WP_000180492.1; NC_011900.1.
DR   AlphaFoldDB; B8ZNP1; -.
DR   SMR; B8ZNP1; -.
DR   KEGG; sne:SPN23F07600; -.
DR   HOGENOM; CLU_053818_1_1_9; -.
DR   OMA; RKYTQVS; -.
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   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..306
FT                   /note="Pantothenate kinase"
FT                   /id="PRO_1000124810"
FT   BINDING         91..98
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00215"
SQ   SEQUENCE   306 AA;  35555 MW;  307002C489933CCE CRC64;
     MTNEFLHFEK ISRQTWQSLH RKTTPPLTEE ELESIKSFND QISLQDVTDI YLPLAHLIQI
     YKRTKEDLAF SKGIFLQRES KSQPFIIGVS GSVAVGKSTT SRLLQILLSR TFTDATVELV
     TTDGFLYPNQ TLIEQGILNR KGFPESYDME ALLNFLDRIK NGQDVDIPVY SHEVYDIVPE
     KKQSVKAADF VIVEGINVFQ NPQNDRLYIT DFFDFSIYVD AGVDDIESWY LDRFLKMLSL
     AQNDPDSYYY RFTQMPIGEV ESFAHQVWIS INLTNLQNYI EPTRNRAEVI LHKSKNHEID
     EIYLKK