ID   DNAA_HYDCU              Reviewed;         467 AA.
AC   Q31JS5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000255|HAMAP-Rule:MF_00377};
GN   Name=dnaA {ECO:0000255|HAMAP-Rule:MF_00377}; OrderedLocusNames=Tcr_0001;
OS   Hydrogenovibrio crunogenus (strain DSM 25203 / XCL-2) (Thiomicrospira
OS   crunogena).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Piscirickettsiaceae; Hydrogenovibrio.
OX   NCBI_TaxID=317025;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 25203 / XCL-2;
RX   PubMed=17105352; DOI=10.1371/journal.pbio.0040383;
RA   Scott K.M., Sievert S.M., Abril F.N., Ball L.A., Barrett C.J., Blake R.A.,
RA   Boller A.J., Chain P.S.G., Clark J.A., Davis C.R., Detter C., Do K.F.,
RA   Dobrinski K.P., Faza B.I., Fitzpatrick K.A., Freyermuth S.K., Harmer T.L.,
RA   Hauser L.J., Huegler M., Kerfeld C.A., Klotz M.G., Kong W.W., Land M.,
RA   Lapidus A., Larimer F.W., Longo D.L., Lucas S., Malfatti S.A., Massey S.E.,
RA   Martin D.D., McCuddin Z., Meyer F., Moore J.L., Ocampo L.H. Jr., Paul J.H.,
RA   Paulsen I.T., Reep D.K., Ren Q., Ross R.L., Sato P.Y., Thomas P.,
RA   Tinkham L.E., Zeruth G.T.;
RT   "The genome of deep-sea vent chemolithoautotroph Thiomicrospira crunogena
RT   XCL-2.";
RL   PLoS Biol. 4:1-17(2006).
CC   -!- FUNCTION: Plays an important role in the initiation and regulation of
CC       chromosomal replication. Binds to the origin of replication; it binds
CC       specifically double-stranded DNA at a 9 bp consensus (dnaA box): 5'-
CC       TTATC[CA]A[CA]A-3'. DnaA binds to ATP and to acidic phospholipids.
CC       {ECO:0000255|HAMAP-Rule:MF_00377}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00377}.
CC   -!- SIMILARITY: Belongs to the DnaA family. {ECO:0000255|HAMAP-
CC       Rule:MF_00377}.
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DR   EMBL; CP000109; ABB40598.1; -; Genomic_DNA.
DR   RefSeq; WP_011369424.1; NC_007520.2.
DR   AlphaFoldDB; Q31JS5; -.
DR   SMR; Q31JS5; -.
DR   STRING; 317025.Tcr_0001; -.
DR   EnsemblBacteria; ABB40598; ABB40598; Tcr_0001.
DR   KEGG; tcx:Tcr_0001; -.
DR   eggNOG; COG0593; Bacteria.
DR   HOGENOM; CLU_026910_0_1_6; -.
DR   OMA; REFNPLF; -.
DR   OrthoDB; 219876at2; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003688; F:DNA replication origin binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006270; P:DNA replication initiation; IEA:UniProtKB-UniRule.
DR   GO; GO:0006275; P:regulation of DNA replication; IEA:UniProtKB-UniRule.
DR   CDD; cd06571; Bac_DnaA_C; 1.
DR   Gene3D; 1.10.1750.10; -; 1.
DR   Gene3D; 3.30.300.180; -; 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; IPR013317; DnaA.
DR   InterPro; IPR013159; DnaA_C.
DR   InterPro; IPR024633; DnaA_N_dom.
DR   InterPro; IPR038454; DnaA_N_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR010921; Trp_repressor/repl_initiator.
DR   PANTHER; PTHR30050:SF2; PTHR30050:SF2; 1.
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; Cytoplasm; DNA replication; DNA-binding; Nucleotide-binding.
FT   CHAIN           1..467
FT                   /note="Chromosomal replication initiator protein DnaA"
FT                   /id="PRO_1000048754"
FT   REGION          87..129
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        99..126
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         172..179
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00377"
SQ   SEQUENCE   467 AA;  53058 MW;  9B5E27D0309D33CE CRC64;
     MTTTLWPQVL KQLEAVLNDQ QFLTWIRPLE AVEEDNTLRL IAPSGFILDW VNKKLLSQIK
     QAVYLVAPVN TPEVTLEVGE YAIESFNEPE NTSVPQPLRE TKAEREAAEK AASSTSKKKS
     DSPPKKTIKH NLNTNFTFDT FVEGKANQLA AAAARQVADN PGGSYNPFFI YGGVGLGKTH
     LMHAIGNELM RRDPNARVVY LHSERFVADM VNALRHNKID EFKRFYRSLD ALLIDDIQFF
     AKKEQSQEEF FHTFNTLLEG NKQVILTSDR FPKEVDGLED RLKSRFGWGL TIAVEPPEFE
     MRVAILMKKA AEFGFLLPDE VAFFIAKRLR GNVRDLEGAL KRVGAFAQFT QQLVTVDLAK
     DALKDLLALQ QKMVTLENIQ KTVADYYKIR VADLLSKRRT RNIARPRQMS MAISKELTSH
     SLPEIGDAFG GRDHTTVLHA VRKINELKET DHRIEEDFNS LIRIITN