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COAA_ECO57
ID   COAA_ECO57              Reviewed;         316 AA.
AC   P0A6I5; P15044;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   29-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Pantothenate kinase;
DE            EC=2.7.1.33;
DE   AltName: Full=Pantothenic acid kinase;
GN   Name=coaA; Synonyms=panK, rts; OrderedLocusNames=Z5545, ECs4901;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG59174.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE005174; AAG59174.1; ALT_INIT; Genomic_DNA.
DR   EMBL; BA000007; BAB38324.1; -; Genomic_DNA.
DR   PIR; E91241; E91241.
DR   RefSeq; NP_312928.1; NC_002695.1.
DR   RefSeq; WP_000023081.1; NZ_SWKA01000005.1.
DR   AlphaFoldDB; P0A6I5; -.
DR   SMR; P0A6I5; -.
DR   STRING; 155864.EDL933_5308; -.
DR   EnsemblBacteria; AAG59174; AAG59174; Z5545.
DR   EnsemblBacteria; BAB38324; BAB38324; ECs_4901.
DR   GeneID; 66672114; -.
DR   GeneID; 914967; -.
DR   KEGG; ece:Z5545; -.
DR   KEGG; ecs:ECs_4901; -.
DR   PATRIC; fig|386585.9.peg.5125; -.
DR   eggNOG; COG1072; Bacteria.
DR   HOGENOM; CLU_053818_1_1_6; -.
DR   OMA; RKYTQVS; -.
DR   UniPathway; UPA00241; UER00352.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; 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..316
FT                   /note="Pantothenate kinase"
FT                   /id="PRO_0000194428"
FT   BINDING         95..102
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        1..6
FT                   /note="MSIKEQ -> PPETCL (in Ref. 1)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   316 AA;  36360 MW;  DDDC1922C5C52A70 CRC64;
     MSIKEQTLMT PYLQFDRNQW AALRDSVPMT LSEDEIARLK GINEDLSLEE VAEIYLPLSR
     LLNFYISSNL RRQAVLEQFL GTNGQRIPYI ISIAGSVAVG KSTTARVLQA LLSRWPEHRR
     VELITTDGFL HPNQVLKERG LMKKKGFPES YDMHRLVKFV SDLKSGVPNV TAPVYSHLIY
     DVIPDGDKTV VQPDILILEG LNVLQSGMDY PHDPHHVFVS DFVDFSIYVD APEDLLQTWY
     INRFLKFREG AFTDPDSYFH NYAKLTKEEA IKTAMTLWKE INWLNLKQNI LPTRERASLI
     LTKSANHAVE EVRLRK
 
 
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