ID   DNAA_ALCBS              Reviewed;         474 AA.
AC   Q0VT30;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000255|HAMAP-Rule:MF_00377};
GN   Name=dnaA {ECO:0000255|HAMAP-Rule:MF_00377}; OrderedLocusNames=ABO_0001;
OS   Alcanivorax borkumensis (strain ATCC 700651 / DSM 11573 / NCIMB 13689 /
OS   SK2).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Alcanivoracaceae; Alcanivorax.
OX   NCBI_TaxID=393595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700651 / DSM 11573 / NCIMB 13689 / SK2;
RX   PubMed=16878126; DOI=10.1038/nbt1232;
RA   Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T., Brecht M.,
RA   Buhrmester J., Chernikova T.N., Denaro R., Ferrer M., Gertler C.,
RA   Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N., Lang S., Linke B.,
RA   McHardy A.C., Meyer F., Nechitaylo T., Puehler A., Regenhardt D., Rupp O.,
RA   Sabirova J.S., Selbitschka W., Yakimov M.M., Timmis K.N., Vorhoelter F.-J.,
RA   Weidner S., Kaiser O., Golyshin P.N.;
RT   "Genome sequence of the ubiquitous hydrocarbon-degrading marine bacterium
RT   Alcanivorax borkumensis.";
RL   Nat. Biotechnol. 24:997-1004(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; AM286690; CAL15449.1; -; Genomic_DNA.
DR   RefSeq; WP_011587299.1; NC_008260.1.
DR   AlphaFoldDB; Q0VT30; -.
DR   SMR; Q0VT30; -.
DR   STRING; 393595.ABO_0001; -.
DR   EnsemblBacteria; CAL15449; CAL15449; ABO_0001.
DR   KEGG; abo:ABO_0001; -.
DR   eggNOG; COG0593; Bacteria.
DR   HOGENOM; CLU_026910_0_1_6; -.
DR   OMA; REFNPLF; -.
DR   OrthoDB; 219876at2; -.
DR   Proteomes; UP000008871; Chromosome.
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;
KW   Reference proteome.
FT   CHAIN           1..474
FT                   /note="Chromosomal replication initiator protein DnaA"
FT                   /id="PRO_1000048601"
FT   REGION          89..138
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        89..107
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        120..138
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         179..186
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00377"
SQ   SEQUENCE   474 AA;  53133 MW;  A6DBFA3A1E8646EF CRC64;
     MSEELWQRCL TRLEDELPSQ QFNMWIRPLQ VAASADGAEL TLFAPNRFVV DWVRDKYLDR
     ISEVLGEMQS GPLPQLRLEV GSTRASTPAA SYFNGSSSSS SNGPITTPAA APAPRQPESD
     SRPQPTSLGG ARKHRSNLNT GFTFSTFVEG KSNRMAAAAA QQVAENPASH GYNPLLLYGG
     VGLGKTHLMH AVGNELLRRN PNAKVVYLHS ERFVADMISA LRNKTINEFK RFYRSVDALL
     IDDIQFFAGK EQSQEEFFHT FNALLENGQQ IILTCDKFPK EVDGLEERLK SRFGWGLSQP
     MEPPELETRV AILKKKAEEA KVDLPNDAAF FIAQRIRSNV RELEGALRRV IAHVRFTGAQ
     IDIGLIKEAL KDLIALQARQ ISIDNIQRIV AEYYKIKIND LLSPRRTRSV ARPRQVAMAL
     SKELTSHSLP EIGENFGGRD HTTVLHACRK VLELRESNPE IEEDYLNLLR TLTS