COAW_STAA8
ID COAW_STAA8 Reviewed; 267 AA.
AC Q2FWC7;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Type II pantothenate kinase;
DE EC=2.7.1.33;
DE AltName: Full=PanK-II;
DE AltName: Full=Pantothenic acid kinase;
GN Name=coaW; Synonyms=coaA; OrderedLocusNames=SAOUHSC_02371;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
RN [2]
RP PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES,
RP AND ACTIVITY REGULATION.
RX PubMed=12760898; DOI=10.1128/aac.47.6.2051-2055.2003;
RA Choudhry A.E., Mandichak T.L., Broskey J.P., Egolf R.W., Kinsland C.,
RA Begley T.P., Seefeld M.A., Ku T.W., Brown J.R., Zalacain M., Ratnam K.;
RT "Inhibitors of pantothenate kinase: novel antibiotics for staphylococcal
RT infections.";
RL Antimicrob. Agents Chemother. 47:2051-2055(2003).
RN [3]
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND ACTIVITY REGULATION.
RX PubMed=15548531; DOI=10.1074/jbc.m411608200;
RA Leonardi R., Chohnan S., Zhang Y.-M., Virga K.G., Lee R.E., Rock C.O.,
RA Jackowski S.;
RT "A pantothenate kinase from Staphylococcus aureus refractory to feedback
RT regulation by coenzyme A.";
RL J. Biol. Chem. 280:3314-3322(2005).
CC -!- FUNCTION: Catalyzes the phosphorylation of pantothenate (Pan), the
CC first step in CoA biosynthesis. {ECO:0000269|PubMed:12760898}.
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 -!- ACTIVITY REGULATION: Not regulated by feedback inhibition by CoA and
CC its thioesters as described for many other pantothenate kinases.
CC Competitively inhibited by N-pentylpantothenamide (N5-Pan) and N-
CC heptylpantothenamide (N7-Pan), although these compounds can also act as
CC substrates, being converted to inactive CoA analogs which inhibit a
CC number of cellular targets, especially fatty acid biosynthesis.
CC {ECO:0000269|PubMed:12760898, ECO:0000269|PubMed:15548531}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=27 uM for pantothenate {ECO:0000269|PubMed:12760898,
CC ECO:0000269|PubMed:15548531};
CC KM=93 uM for ATP {ECO:0000269|PubMed:12760898,
CC ECO:0000269|PubMed:15548531};
CC KM=3 uM for N-pentylpantothenamide {ECO:0000269|PubMed:12760898,
CC ECO:0000269|PubMed:15548531};
CC KM=8 uM for N-heptylpantothenamide {ECO:0000269|PubMed:12760898,
CC ECO:0000269|PubMed:15548531};
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-
CC pantothenate: step 1/5.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15548531}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the type II pantothenate kinase family.
CC {ECO:0000305}.
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DR EMBL; CP000253; ABD31402.1; -; Genomic_DNA.
DR RefSeq; WP_000862727.1; NZ_LS483365.1.
DR RefSeq; YP_500848.1; NC_007795.1.
DR PDB; 5ELZ; X-ray; 1.80 A; A=1-267.
DR PDB; 5JIC; X-ray; 1.40 A; A=1-267.
DR PDB; 6AVP; X-ray; 2.30 A; A/B/C/D=1-265.
DR PDB; 6AWG; X-ray; 2.40 A; A/B/C/D=1-266.
DR PDB; 6AWH; X-ray; 1.90 A; A/B/C/D=1-266.
DR PDB; 6AWI; X-ray; 1.80 A; A/B/C/D=1-266.
DR PDB; 6AWJ; X-ray; 2.50 A; A/B/C/D=1-266.
DR PDB; 6EBV; X-ray; 3.00 A; A/B/C/D=1-267.
DR PDBsum; 5ELZ; -.
DR PDBsum; 5JIC; -.
DR PDBsum; 6AVP; -.
DR PDBsum; 6AWG; -.
DR PDBsum; 6AWH; -.
DR PDBsum; 6AWI; -.
DR PDBsum; 6AWJ; -.
DR PDBsum; 6EBV; -.
DR AlphaFoldDB; Q2FWC7; -.
DR SMR; Q2FWC7; -.
DR STRING; 1280.SAXN108_2375; -.
DR EnsemblBacteria; ABD31402; ABD31402; SAOUHSC_02371.
DR GeneID; 3919414; -.
DR KEGG; sao:SAOUHSC_02371; -.
DR PATRIC; fig|93061.5.peg.2148; -.
DR eggNOG; COG5146; Bacteria.
DR HOGENOM; CLU_087521_1_0_9; -.
DR OMA; VKHIYKD; -.
DR SABIO-RK; Q2FWC7; -.
DR UniPathway; UPA00241; UER00352.
DR PRO; PR:Q2FWC7; -.
DR Proteomes; UP000008816; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004594; F:pantothenate kinase activity; IBA:GO_Central.
DR GO; GO:0015937; P:coenzyme A biosynthetic process; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR HAMAP; MF_01273; Pantothen_kinase_2; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR004567; Type_II_PanK.
DR InterPro; IPR011602; Type_II_PanK_bac.
DR PANTHER; PTHR12280; PTHR12280; 1.
DR Pfam; PF03630; Fumble; 1.
DR PIRSF; PIRSF036940; PanK_bac_aCoA; 1.
DR SUPFAM; SSF53067; SSF53067; 1.
DR TIGRFAMs; TIGR00555; panK_eukar; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Coenzyme A biosynthesis; Cytoplasm;
KW Direct protein sequencing; Kinase; Nucleotide-binding; Reference proteome;
KW Transferase.
FT CHAIN 1..267
FT /note="Type II pantothenate kinase"
FT /id="PRO_0000261350"
FT ACT_SITE 70
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 6..13
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 99
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 121..125
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 137
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 225
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:5JIC"
FT STRAND 9..16
FT /evidence="ECO:0007829|PDB:5JIC"
FT STRAND 23..28
FT /evidence="ECO:0007829|PDB:5JIC"
FT HELIX 29..31
FT /evidence="ECO:0007829|PDB:5JIC"
FT HELIX 32..40
FT /evidence="ECO:0007829|PDB:5JIC"
FT STRAND 47..51
FT /evidence="ECO:0007829|PDB:5JIC"
FT HELIX 54..59
FT /evidence="ECO:0007829|PDB:5JIC"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:6AWI"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:5JIC"
FT HELIX 70..84
FT /evidence="ECO:0007829|PDB:5JIC"
FT STRAND 92..106
FT /evidence="ECO:0007829|PDB:5JIC"
FT STRAND 111..118
FT /evidence="ECO:0007829|PDB:5JIC"
FT HELIX 121..132
FT /evidence="ECO:0007829|PDB:5JIC"
FT HELIX 137..144
FT /evidence="ECO:0007829|PDB:5JIC"
FT TURN 150..152
FT /evidence="ECO:0007829|PDB:5JIC"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:6EBV"
FT HELIX 156..160
FT /evidence="ECO:0007829|PDB:5JIC"
FT STRAND 171..174
FT /evidence="ECO:0007829|PDB:5JIC"
FT TURN 175..178
FT /evidence="ECO:0007829|PDB:5JIC"
FT HELIX 179..181
FT /evidence="ECO:0007829|PDB:5JIC"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:6AWH"
FT HELIX 189..215
FT /evidence="ECO:0007829|PDB:5JIC"
FT STRAND 219..224
FT /evidence="ECO:0007829|PDB:5JIC"
FT HELIX 225..227
FT /evidence="ECO:0007829|PDB:5JIC"
FT HELIX 231..243
FT /evidence="ECO:0007829|PDB:5JIC"
FT STRAND 247..250
FT /evidence="ECO:0007829|PDB:5JIC"
FT HELIX 254..256
FT /evidence="ECO:0007829|PDB:5JIC"
FT HELIX 257..267
FT /evidence="ECO:0007829|PDB:5JIC"
SQ SEQUENCE 267 AA; 29097 MW; 3663BBC6DFBC2D9A CRC64;
MKVGIDAGGT LIKIVQEQDN QRTFKTELTK NIDQVVEWLN QQQIEKLCLT GGNAGVIAEN
INIPAQIFVE FDAASQGLGI LLKEQGHDLA DYIFANVGTG TSLHYFDGQS QRRVGGIGTG
GGMIQGLGYL LSQITDYKQL TDMAQHGDRN TIDLKVRHIY KDTEPPIPGD LTAANFGHVL
HHLDADFTPS NKLAAVIGVV GEVVTTMAIT VAREFKTENI VYIGSSFHNN ALLRKVVEDY
TVLRGCKPYY VENGAFSGAI GALYLEK
