ID   COAA_LACLA              Reviewed;         306 AA.
AC   Q9CFM3;
DT   06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Pantothenate kinase;
DE            EC=2.7.1.33;
DE   AltName: Full=Pantothenic acid kinase;
GN   Name=coaA; OrderedLocusNames=LL1444; ORFNames=L66222;
OS   Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=272623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IL1403;
RX   PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA   Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "The complete genome sequence of the lactic acid bacterium Lactococcus
RT   lactis ssp. lactis IL1403.";
RL   Genome Res. 11:731-753(2001).
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}.
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DR   EMBL; AE005176; AAK05542.1; -; Genomic_DNA.
DR   PIR; D86805; D86805.
DR   RefSeq; NP_267600.1; NC_002662.1.
DR   RefSeq; WP_003130461.1; NC_002662.1.
DR   AlphaFoldDB; Q9CFM3; -.
DR   SMR; Q9CFM3; -.
DR   STRING; 272623.L66222; -.
DR   PaxDb; Q9CFM3; -.
DR   EnsemblBacteria; AAK05542; AAK05542; L66222.
DR   KEGG; lla:L66222; -.
DR   PATRIC; fig|272623.7.peg.1552; -.
DR   eggNOG; COG1072; Bacteria.
DR   HOGENOM; CLU_053818_1_1_9; -.
DR   OMA; RKYTQVS; -.
DR   UniPathway; UPA00241; UER00352.
DR   Proteomes; UP000002196; 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..306
FT                   /note="Pantothenate kinase"
FT                   /id="PRO_0000194432"
FT   BINDING         90..97
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   306 AA;  35992 MW;  87241BDFC3FC9DB8 CRC64;
     MNEFINFDEI SRKTWQNLYN TSIAPLTHDE LESIRSLNDE ISLQDVEDVY LPLIHLLRLY
     KKNLEDMSYS KGLFLQKIVK TPPLIIGISG SVAVGKSTTA RLLQLLLSRA FPKLTVDLVT
     TDGFLYTTND LKNMGILDRK GFPESYDMEK LTSFLYHVKN GEKFEVPIYS HETYDILPNQ
     SQIIDSPDIL IVEGINVLQN PQNQLLYISD FYDFSIYVDA DEKLIEKWYL ERFDSLLKLA
     KYDQTNFYHQ FTKMPEDKVI NLAREIWARV NRVNLREYIE PTRNRAEIIL HKTENHYIDK
     IYLKKF