ID   COAE_CHLMU              Reviewed;         202 AA.
AC   Q9PJP9;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 2.
DT   16-JUN-2009, entry version 56.
DE   RecName: Full=Dephospho-CoA kinase;
DE            EC=2.7.1.24;
DE   AltName: Full=Dephosphocoenzyme A kinase;
GN   Name=coaE; OrderedLocusNames=TC_0779;
OS   Chlamydia muridarum.
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae; Chlamydia.
OX   NCBI_TaxID=83560;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MoPn / Nigg;
RX   MEDLINE=20150255; PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA   Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F.,
RA   White O., Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J.,
RA   Bass S., Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C.,
RA   Dodson R.J., Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F.,
RA   McClarty G., Salzberg S.L., Eisen J.A., Fraser C.M.;
RT   "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia
RT   pneumoniae AR39.";
RL   Nucleic Acids Res. 28:1397-1406(2000).
CC   -!- FUNCTION: Catalyzes the phosphorylation of the 3'-hydroxyl group
CC       of dephosphocoenzyme A to form coenzyme A (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + 3'-dephospho-CoA = ADP + CoA.
CC   -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; coenzyme
CC       A from pantothenate: step 5/5.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the coaE family.
CC   -!- SIMILARITY: Contains 1 DPCK (dephospho-CoA kinase) domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AE002160; AAF39582.1; ALT_INIT; Genomic_DNA.
DR   PIR; C81665; C81665.
DR   RefSeq; NP_297152.1; -.
DR   HSSP; P44920; 1JJV.
DR   GeneID; 1246144; -.
DR   GenomeReviews; AE002160_GR; TC_0779.
DR   KEGG; cmu:TC0779; -.
DR   TIGR; TC_0779; -.
DR   HOGENOM; Q9PJP9; -.
DR   BioCyc; CMUR243161:TC_0779-MON; -.
DR   BRENDA; 2.7.1.24; 256349.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0004140; F:dephospho-CoA kinase activity; IEA:HAMAP.
DR   GO; GO:0015937; P:coenzyme A biosynthetic process; IEA:HAMAP.
DR   HAMAP; MF_00376; -; 1.
DR   InterPro; IPR001977; Depp_CoAkinase.
DR   PANTHER; PTHR10695; Depp_CoAkinase; 1.
DR   Pfam; PF01121; CoaE; 1.
DR   ProDom; PD003329; Depp_CoAkinase; 1.
DR   TIGRFAMs; TIGR00152; Depp_CoAkinase; 1.
DR   PROSITE; PS51219; DPCK; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Coenzyme A biosynthesis; Complete proteome; Cytoplasm;
KW   Kinase; Nucleotide-binding; Transferase.
FT   CHAIN         1    202       Dephospho-CoA kinase.
FT                                /FTId=PRO_0000172925.
FT   DOMAIN        6    202       DPCK.
FT   NP_BIND      11     18       ATP (Potential).
SQ   SEQUENCE   202 AA;  22878 MW;  B31A49790EC06C17 CRC64;
     MLDLLKISVT GDPSSGKTEA CQVFEELGAF VISADKVSHS FLVPYTSEGQ RVVDLLGPEI
     IVENTLNRKA IAKKVFGNRD LLLSLEKILH PGVCRFVEEN YTQVVQAQKY SLFVVEVPLL
     YEIQYADWFD RVILISADTE IRKERFLKKT GGSDTSFDLR CARFSSLEEK ILRADVVIEN
     NGTKEEFRHK VKQCFKALKG TI
//