ID   COAE_CHLTA              Reviewed;         202 AA.
AC   Q3KLK5;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Dephospho-CoA kinase {ECO:0000255|HAMAP-Rule:MF_00376};
DE            EC=2.7.1.24 {ECO:0000255|HAMAP-Rule:MF_00376};
DE   AltName: Full=Dephosphocoenzyme A kinase {ECO:0000255|HAMAP-Rule:MF_00376};
GN   Name=coaE {ECO:0000255|HAMAP-Rule:MF_00376}; OrderedLocusNames=CTA_0539;
OS   Chlamydia trachomatis serovar A (strain ATCC VR-571B / DSM 19440 / HAR-13).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=315277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-571B / DSM 19440 / HAR-13;
RX   PubMed=16177312; DOI=10.1128/iai.73.10.6407-6418.2005;
RA   Carlson J.H., Porcella S.F., McClarty G., Caldwell H.D.;
RT   "Comparative genomic analysis of Chlamydia trachomatis oculotropic and
RT   genitotropic strains.";
RL   Infect. Immun. 73:6407-6418(2005).
CC   -!- FUNCTION: Catalyzes the phosphorylation of the 3'-hydroxyl group of
CC       dephosphocoenzyme A to form coenzyme A. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00376};
CC   -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-
CC       pantothenate: step 5/5. {ECO:0000255|HAMAP-Rule:MF_00376}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00376}.
CC   -!- SIMILARITY: Belongs to the CoaE family. {ECO:0000255|HAMAP-
CC       Rule:MF_00376}.
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DR   EMBL; CP000051; AAX50767.1; -; Genomic_DNA.
DR   RefSeq; WP_011324753.1; NC_007429.1.
DR   AlphaFoldDB; Q3KLK5; -.
DR   SMR; Q3KLK5; -.
DR   EnsemblBacteria; AAX50767; AAX50767; CTA_0539.
DR   KEGG; cta:CTA_0539; -.
DR   HOGENOM; CLU_057180_3_1_0; -.
DR   OMA; QMDIEQK; -.
DR   UniPathway; UPA00241; UER00356.
DR   Proteomes; UP000002532; 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   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00376; Dephospho_CoA_kinase; 1.
DR   InterPro; IPR001977; Depp_CoAkinase.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF01121; CoaE; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00152; TIGR00152; 1.
DR   PROSITE; PS51219; DPCK; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Coenzyme A biosynthesis; Cytoplasm; Kinase;
KW   Nucleotide-binding; Transferase.
FT   CHAIN           1..202
FT                   /note="Dephospho-CoA kinase"
FT                   /id="PRO_0000243273"
FT   DOMAIN          6..202
FT                   /note="DPCK"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00376"
FT   BINDING         14..19
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00376"
SQ   SEQUENCE   202 AA;  22900 MW;  762AE4D03D9C3935 CRC64;
     MLDLLKISVT GDPSSGKTEA CQVFEDLGAY VISADKVSHS FLVPYTSVGQ RIIDLLGPEI
     IIENTLSRKA IAEKVFGNRD LLLSLEEILH PEVCRFVEEK YAHVVQEQKY PLFIAEFPLL
     YEIQYADWFD QVILISADTG IRKERFLKKT GGSDTSFDLR CARFSSLEEK ILRADVVIEN
     NGTKEEFRCK VKQCFKALKG TI