ID G4NPA9_CHLT4 Unreviewed; 205 AA.
AC G4NPA9;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 24-JAN-2024, entry version 55.
DE RecName: Full=Dephospho-CoA kinase {ECO:0000256|HAMAP-Rule:MF_00376};
DE EC=2.7.1.24 {ECO:0000256|HAMAP-Rule:MF_00376};
DE AltName: Full=Dephosphocoenzyme A kinase {ECO:0000256|HAMAP-Rule:MF_00376};
GN Name=coaE {ECO:0000256|HAMAP-Rule:MF_00376};
GN OrderedLocusNames=CTO_0539 {ECO:0000313|EMBL:AEP35355.1};
OS Chlamydia trachomatis serovar A (strain A2497).
OC Bacteria; Chlamydiota; Chlamydiia; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=580047 {ECO:0000313|EMBL:AEP35355.1, ECO:0000313|Proteomes:UP000009287};
RN [1] {ECO:0000313|EMBL:AEP35355.1, ECO:0000313|Proteomes:UP000009287}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A2497 {ECO:0000313|EMBL:AEP35355.1,
RC ECO:0000313|Proteomes:UP000009287};
RX PubMed=21987657; DOI=10.1084/jem.20111266;
RA Kari L., Whitmire W.M., Olivares-Zavaleta N., Goheen M.M., Taylor L.D.,
RA Carlson J.H., Sturdevant G.L., Lu C., Bakios L.E., Randall L.B.,
RA Parnell M.J., Zhong G., Caldwell H.D.;
RT "A live-attenuated chlamydial vaccine protects against trachoma in nonhuman
RT primates.";
RL J. Exp. Med. 208:2217-2223(2011).
CC -!- FUNCTION: Catalyzes the phosphorylation of the 3'-hydroxyl group of
CC dephosphocoenzyme A to form coenzyme A. {ECO:0000256|HAMAP-
CC Rule:MF_00376}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-dephospho-CoA + ATP = ADP + CoA + H(+);
CC Xref=Rhea:RHEA:18245, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57328, ChEBI:CHEBI:456216;
CC EC=2.7.1.24; Evidence={ECO:0000256|HAMAP-Rule:MF_00376};
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-
CC pantothenate: step 5/5. {ECO:0000256|HAMAP-Rule:MF_00376}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00376}.
CC -!- SIMILARITY: Belongs to the CoaE family. {ECO:0000256|HAMAP-
CC Rule:MF_00376}.
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DR EMBL; CP002401; AEP35355.1; -; Genomic_DNA.
DR AlphaFoldDB; G4NPA9; -.
DR KEGG; cra:CTO_0539; -.
DR PATRIC; fig|580047.4.peg.545; -.
DR OMA; VTEIWVV; -.
DR UniPathway; UPA00241; UER00356.
DR Proteomes; UP000009287; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004140; F:dephospho-CoA 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; cd02022; DPCK; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_00376; Dephospho_CoA_kinase; 1.
DR InterPro; IPR001977; Depp_CoAkinase.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR00152; dephospho-CoA kinase; 1.
DR PANTHER; PTHR10695:SF46; BIFUNCTIONAL COENZYME A SYNTHASE-RELATED; 1.
DR PANTHER; PTHR10695; DEPHOSPHO-COA KINASE-RELATED; 1.
DR Pfam; PF01121; CoaE; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51219; DPCK; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00376}; Coenzyme A biosynthesis {ECO:0000256|HAMAP-Rule:MF_00376};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00376};
KW Kinase {ECO:0000256|HAMAP-Rule:MF_00376, ECO:0000313|EMBL:AEP35355.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00376}; Transferase {ECO:0000256|HAMAP-Rule:MF_00376}.
FT BINDING 17..22
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00376"
SQ SEQUENCE 205 AA; 23238 MW; BDA560EED60AD290 CRC64;
MGGMLDLLKI SVTGDPSSGK TEACQVFEDL GAYVISADKV SHSFLVPYTS VGQRIIDLLG
PEIIIENTLS RKAIAEKVFG NRDLLLSLEE ILHPEVCRFV DEKYAYVVQE QKYPLFIAEF
PLLYEIQYAD WFDQVILISA DKGIRKERFL KKTGGSDTSF DLRCARFSSL EEKILRADVV
IENNGTKEEF RRKVKQCFKA LKGTI
//