ID   DNAA2_CHLMU             Reviewed;         455 AA.
AC   Q9PKB9;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   14-MAY-2014, entry version 85.
DE   RecName: Full=Chromosomal replication initiator protein DnaA 2;
GN   Name=dnaA2; OrderedLocusNames=TC_0547;
OS   Chlamydia muridarum (strain MoPn / Nigg).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=243161;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MoPn / Nigg;
RX   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: Plays an important role in the initiation and regulation
CC       of chromosomal replication. Binds to the origin of replication; it
CC       binds specifically double-stranded DNA at a 9 bp consensus (dnaA
CC       box): 5'-TTATC[CA]A[CA]A-3'. DnaA binds to ATP and to acidic
CC       phospholipids (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the DnaA family.
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DR   EMBL; AE002160; AAF39386.1; -; Genomic_DNA.
DR   PIR; G81689; G81689.
DR   RefSeq; NP_296924.1; NC_002620.2.
DR   ProteinModelPortal; Q9PKB9; -.
DR   STRING; 243161.TC0547; -.
DR   EnsemblBacteria; AAF39386; AAF39386; TC_0547.
DR   GeneID; 1245907; -.
DR   KEGG; cmu:TC_0547; -.
DR   PATRIC; 20372538; VBIChlMur19118_0585.
DR   eggNOG; COG0593; -.
DR   KO; K02313; -.
DR   OMA; HAIGNRA; -.
DR   OrthoDB; EOG689HR1; -.
DR   BioCyc; CMUR243161:GHYU-568-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003688; F:DNA replication origin binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0017111; F:nucleoside-triphosphatase activity; IEA:InterPro.
DR   GO; GO:0006270; P:DNA replication initiation; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006275; P:regulation of DNA replication; IEA:UniProtKB-HAMAP.
DR   Gene3D; 1.10.1750.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00377; DnaA_bact; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR001957; Chromosome_initiator_DnaA.
DR   InterPro; IPR020591; Chromosome_initiator_DnaA-like.
DR   InterPro; IPR018312; Chromosome_initiator_DnaA_CS.
DR   InterPro; IPR013159; DnaA_C.
DR   InterPro; IPR013317; DnaA_Hda.
DR   InterPro; IPR024633; DnaA_N_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR010921; Trp_repressor/repl_initiator.
DR   Pfam; PF00308; Bac_DnaA; 1.
DR   Pfam; PF08299; Bac_DnaA_C; 1.
DR   Pfam; PF11638; DnaA_N; 1.
DR   PRINTS; PR00051; DNAA.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00760; Bac_DnaA_C; 1.
DR   SUPFAM; SSF48295; SSF48295; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00362; DnaA; 1.
DR   PROSITE; PS01008; DNAA; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Cytoplasm; DNA replication;
KW   DNA-binding; Nucleotide-binding.
FT   CHAIN         1    455       Chromosomal replication initiator protein
FT                                DnaA 2.
FT                                /FTId=PRO_0000114158.
FT   NP_BIND     154    161       ATP (Potential).
SQ   SEQUENCE   455 AA;  51446 MW;  B5347ACF9235A25C CRC64;
     MLTCNDCSTW EQFVNYIKTR CSKTAFENWI APIQVLEESR EKIRLEIPNI FVQSYLLDNY
     KKDLCSFVPL DAEGNPALEF VVSEIKRSSP QIAASVTKPA VEVSEENKDF QLKLNGAYRF
     DNFIEGPSNQ FVKSAALGIA ARPGRSYNPL FIHGGVGLGK THLLHAVGHY VREHHKNLRI
     HCITTEAFIN DLVHHLRVKS IDKMKNFYRS LDLLLVDDIQ FLQNRQNFEE EFCNTFETLI
     HLSKQIVVTS DKPPGQLKLS ERIIARMEWG LVAHVGVPDL ETRVAILQHK AEQKGLNIPN
     EIAFYIADHV YGNVRQLEGA INKLTAYCLL FNKPLTETTV RDTLKELFRT PSKQKVSVES
     ILKSVATVFQ VKIQDLKGTS RAKNVPLARQ VAMYLAKTLI TDSLVAIGAA FGKTHSTVLY
     ACKTIEQKIE KDALLKNQIS LCKNNIAIDS PQHFV
//