ID   COAA_STRPF              Reviewed;         306 AA.
AC   Q1J6D9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 1.
DT   03-AUG-2022, entry version 88.
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=MGAS10750_Spy1094;
OS   Streptococcus pyogenes serotype M4 (strain MGAS10750).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=370554;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGAS10750;
RX   PubMed=16636287; DOI=10.1073/pnas.0510279103;
RA   Beres S.B., Richter E.W., Nagiec M.J., Sumby P., Porcella S.F., DeLeo F.R.,
RA   Musser J.M.;
RT   "Molecular genetic anatomy of inter- and intraserotype variation in the
RT   human bacterial pathogen group A Streptococcus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:7059-7064(2006).
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; CP000262; ABF38044.1; -; Genomic_DNA.
DR   RefSeq; WP_010922353.1; NC_008024.1.
DR   AlphaFoldDB; Q1J6D9; -.
DR   SMR; Q1J6D9; -.
DR   EnsemblBacteria; ABF38044; ABF38044; MGAS10750_Spy1094.
DR   GeneID; 57852701; -.
DR   KEGG; spi:MGAS10750_Spy1094; -.
DR   HOGENOM; CLU_053818_1_1_9; -.
DR   OMA; RKYTQVS; -.
DR   UniPathway; UPA00241; UER00352.
DR   Proteomes; UP000002434; 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..306
FT                   /note="Pantothenate kinase"
FT                   /id="PRO_1000043265"
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;  35610 MW;  6230FD2725EC9EA4 CRC64;
     MSNEFINFEK ISRESWKTLH QKAKALLTQE ELKSITSLND NISINDVIDI YLPLINLIQV
     YKIAQENLSF SKSLFLKKDI QLRPFIIGIS GSVAVGKSTT SRLLQLLLSR THPNSQVELV
     TTDGFLYPNQ FLIEQGLLNR KGFPESYNME LLLDFLDSIK NGQTAFAPVY SHDIYDIIPN
     QKQSFNNPDF LIVEGINVFQ NQQNNRLYMS DYFDFSIYID ADSSHIETWY IERFLSILKL
     AKRDPHNYYA QYAQLPRSEA IAFARNVWKT VNLENLEKFI EPTRNRAELI LHKSADHKID
     EIYLKK