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Database: UniProt
Entry: R9AJ53_9GAMM
LinkDB: R9AJ53_9GAMM
Original site: R9AJ53_9GAMM 
ID   R9AJ53_9GAMM            Unreviewed;       459 AA.
AC   R9AJ53;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-SEP-2017, entry version 33.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00724181};
GN   Name=dnaA {ECO:0000256|HAMAP-Rule:MF_00377};
GN   ORFNames=I593_03979 {ECO:0000313|EMBL:EOR02145.1};
OS   Acinetobacter tandoii DSM 14970 = CIP 107469.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Acinetobacter.
OX   NCBI_TaxID=1120927 {ECO:0000313|EMBL:EOR02145.1, ECO:0000313|Proteomes:UP000016201};
RN   [1] {ECO:0000313|EMBL:EOR02145.1, ECO:0000313|Proteomes:UP000016201}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIP 107469 {ECO:0000313|EMBL:EOR02145.1,
RC   ECO:0000313|Proteomes:UP000016201};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA   Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA   Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA   Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA   Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA   Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Acinetobacter tandoii CIP 107469.";
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000256|HAMAP-Rule:MF_00377,
CC       ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00724167}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
CC       ECO:0000256|SAAS:SAAS00756131}.
CC   -!- SIMILARITY: Belongs to the DnaA family. {ECO:0000256|HAMAP-
CC       Rule:MF_00377, ECO:0000256|RuleBase:RU004227,
CC       ECO:0000256|SAAS:SAAS00555179}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EOR02145.1}.
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DR   EMBL; AQFM01000049; EOR02145.1; -; Genomic_DNA.
DR   RefSeq; WP_016168946.1; NZ_KE007371.1.
DR   EnsemblBacteria; EOR02145; EOR02145; I593_03979.
DR   PATRIC; fig|1120927.3.peg.3873; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000016201; Unassembled WGS sequence.
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   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; IPR027417; P-loop_NTPase.
DR   InterPro; IPR010921; Trp_repressor/repl_initiator.
DR   PANTHER; PTHR30050:SF12; PTHR30050:SF12; 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 {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00731922};
KW   Complete proteome {ECO:0000313|Proteomes:UP000016201};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|SAAS:SAAS00756112};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU004227, ECO:0000256|SAAS:SAAS00731887};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00756124};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00731897};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016201}.
FT   DOMAIN      156    286       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      367    436       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     164    171       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   459 AA;  51838 MW;  4E1956D5340AA6DE CRC64;
     MLWTDCLTRL RQELSGNVFT MWIRPLVAEE LEDTLRLYAP NPYWTRYIQE HHLELITILA
     EQLSEGRVRH VEIMVDSRPG AILSPSEQPA TTTAALETSP PVPAVKPKKE KDDSSLKNKK
     RLLNPLFTFS LFVEGRSNQM AAETCRKVLT QLGASQHNPL FLYGPTGLGK THLMQAVGNA
     LLQAKPNARV MYMTAESFVQ DFVSSLQQGK VEEFKKNCRS LDLLLVDDIH LLAGKEASLV
     EFFYTFNALL DESKQIILTS DRYPKELTEL DARLVSRFSW GLSVGVEPPD IETRIEILLK
     KAQSSGVDLP RNCALFIAQQ VVANVRELEG ALNKVVAISR FKGTSIDLDV VRESLKDVLA
     IRARTISTEN IQRVVSEYFR IPLKELIGPK RTRIYARPRQ LAMGLARELT GDSFPEIGMA
     FGGRDHSTVM HACEKVQSLR EDDPIFNEDY KNLQRLLQS
//
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