ID   COAA_STRP3              Reviewed;         306 AA.
AC   P0DA40; Q8K7C7;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 1.
DT   03-AUG-2022, entry version 52.
DE   RecName: Full=Pantothenate kinase;
DE            EC=2.7.1.33;
DE   AltName: Full=Pantothenic acid kinase;
GN   Name=coaA; OrderedLocusNames=SpyM3_0871;
OS   Streptococcus pyogenes serotype M3 (strain ATCC BAA-595 / MGAS315).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=198466;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-595 / MGAS315;
RX   PubMed=12122206; DOI=10.1073/pnas.152298499;
RA   Beres S.B., Sylva G.L., Barbian K.D., Lei B., Hoff J.S., Mammarella N.D.,
RA   Liu M.-Y., Smoot J.C., Porcella S.F., Parkins L.D., Campbell D.S.,
RA   Smith T.M., McCormick J.K., Leung D.Y.M., Schlievert P.M., Musser J.M.;
RT   "Genome sequence of a serotype M3 strain of group A Streptococcus: phage-
RT   encoded toxins, the high-virulence phenotype, and clone emergence.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:10078-10083(2002).
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;
CC   -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-
CC       pantothenate: step 1/5.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the prokaryotic pantothenate kinase family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE014074; AAM79478.1; -; Genomic_DNA.
DR   RefSeq; WP_011054527.1; NC_004070.1.
DR   AlphaFoldDB; P0DA40; -.
DR   SMR; P0DA40; -.
DR   EnsemblBacteria; AAM79478; AAM79478; SpyM3_0871.
DR   KEGG; spg:SpyM3_0871; -.
DR   HOGENOM; CLU_053818_1_1_9; -.
DR   OMA; RKYTQVS; -.
DR   UniPathway; UPA00241; UER00352.
DR   Proteomes; UP000000564; 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_0000194457"
FT   BINDING         91..98
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   306 AA;  35609 MW;  923271A925E833C7 CRC64;
     MSNKFINFEK 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