COAW_STAAW
ID COAW_STAAW Reviewed; 267 AA.
AC Q8NVG0;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Type II pantothenate kinase {ECO:0000255|HAMAP-Rule:MF_01273};
DE EC=2.7.1.33 {ECO:0000255|HAMAP-Rule:MF_01273};
DE AltName: Full=PanK-II {ECO:0000255|HAMAP-Rule:MF_01273};
DE AltName: Full=Pantothenic acid kinase {ECO:0000255|HAMAP-Rule:MF_01273};
GN Name=coaW {ECO:0000255|HAMAP-Rule:MF_01273}; OrderedLocusNames=MW2054;
OS Staphylococcus aureus (strain MW2).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=196620;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MW2;
RX PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT "Genome and virulence determinants of high virulence community-acquired
RT MRSA.";
RL Lancet 359:1819-1827(2002).
CC -!- FUNCTION: Catalyzes the phosphorylation of pantothenate (Pan), the
CC first step in CoA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01273}.
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_01273};
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-
CC pantothenate: step 1/5. {ECO:0000255|HAMAP-Rule:MF_01273}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01273}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01273}.
CC -!- SIMILARITY: Belongs to the type II pantothenate kinase family.
CC {ECO:0000255|HAMAP-Rule:MF_01273}.
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DR EMBL; BA000033; BAB95919.1; -; Genomic_DNA.
DR RefSeq; WP_000862727.1; NC_003923.1.
DR PDB; 4M7X; X-ray; 1.42 A; A=1-267.
DR PDB; 4M7Y; X-ray; 1.80 A; A/B=1-267.
DR PDBsum; 4M7X; -.
DR PDBsum; 4M7Y; -.
DR AlphaFoldDB; Q8NVG0; -.
DR SMR; Q8NVG0; -.
DR DNASU; 1004170; -.
DR EnsemblBacteria; BAB95919; BAB95919; BAB95919.
DR KEGG; sam:MW2054; -.
DR HOGENOM; CLU_087521_1_0_9; -.
DR OMA; VKHIYKD; -.
DR UniPathway; UPA00241; UER00352.
DR Proteomes; UP000000418; 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 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; Kinase;
KW Nucleotide-binding; Transferase.
FT CHAIN 1..267
FT /note="Type II pantothenate kinase"
FT /id="PRO_0000261348"
FT ACT_SITE 70
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01273"
FT BINDING 6..13
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01273"
FT BINDING 99
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01273"
FT BINDING 121..125
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01273"
FT BINDING 137
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01273"
FT BINDING 225
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01273"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:4M7X"
FT STRAND 9..17
FT /evidence="ECO:0007829|PDB:4M7X"
FT STRAND 22..28
FT /evidence="ECO:0007829|PDB:4M7X"
FT HELIX 29..31
FT /evidence="ECO:0007829|PDB:4M7X"
FT HELIX 32..40
FT /evidence="ECO:0007829|PDB:4M7X"
FT STRAND 47..51
FT /evidence="ECO:0007829|PDB:4M7X"
FT HELIX 54..59
FT /evidence="ECO:0007829|PDB:4M7X"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:4M7Y"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:4M7X"
FT HELIX 70..84
FT /evidence="ECO:0007829|PDB:4M7X"
FT STRAND 92..106
FT /evidence="ECO:0007829|PDB:4M7X"
FT STRAND 111..118
FT /evidence="ECO:0007829|PDB:4M7X"
FT HELIX 121..132
FT /evidence="ECO:0007829|PDB:4M7X"
FT HELIX 137..144
FT /evidence="ECO:0007829|PDB:4M7X"
FT TURN 150..152
FT /evidence="ECO:0007829|PDB:4M7X"
FT HELIX 156..160
FT /evidence="ECO:0007829|PDB:4M7X"
FT STRAND 171..174
FT /evidence="ECO:0007829|PDB:4M7X"
FT TURN 175..178
FT /evidence="ECO:0007829|PDB:4M7X"
FT HELIX 179..181
FT /evidence="ECO:0007829|PDB:4M7X"
FT HELIX 189..215
FT /evidence="ECO:0007829|PDB:4M7X"
FT STRAND 219..224
FT /evidence="ECO:0007829|PDB:4M7X"
FT HELIX 225..227
FT /evidence="ECO:0007829|PDB:4M7X"
FT HELIX 231..243
FT /evidence="ECO:0007829|PDB:4M7X"
FT STRAND 247..250
FT /evidence="ECO:0007829|PDB:4M7X"
FT HELIX 254..256
FT /evidence="ECO:0007829|PDB:4M7X"
FT HELIX 257..267
FT /evidence="ECO:0007829|PDB:4M7X"
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
