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Database: UniProt
Entry: A0A0M4GJW7_9GAMM
LinkDB: A0A0M4GJW7_9GAMM
Original site: A0A0M4GJW7_9GAMM 
ID   A0A0M4GJW7_9GAMM        Unreviewed;       459 AA.
AC   A0A0M4GJW7;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   16-JAN-2019, entry version 23.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS01081161};
GN   Name=dnaA {ECO:0000256|HAMAP-Rule:MF_00377};
GN   ORFNames=AMQ28_08095 {ECO:0000313|EMBL:ALD02318.1};
OS   Acinetobacter sp. TTH0-4.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Acinetobacter.
OX   NCBI_TaxID=1646498 {ECO:0000313|EMBL:ALD02318.1, ECO:0000313|Proteomes:UP000055186};
RN   [1] {ECO:0000313|EMBL:ALD02318.1, ECO:0000313|Proteomes:UP000055186}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TTH0-4 {ECO:0000313|EMBL:ALD02318.1,
RC   ECO:0000313|Proteomes:UP000055186};
RA   Zhang G.;
RT   "Acinetobacter qinghaiensis sp. nov., isolated from active layer of
RT   permafrost region.";
RL   Submitted (SEP-2015) 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:SAAS00756121}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
CC       ECO:0000256|SAAS:SAAS01082709}.
CC   -!- SIMILARITY: Belongs to the DnaA family. {ECO:0000256|HAMAP-
CC       Rule:MF_00377, ECO:0000256|RuleBase:RU004227,
CC       ECO:0000256|SAAS:SAAS00555179}.
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DR   EMBL; CP012608; ALD02318.1; -; Genomic_DNA.
DR   RefSeq; WP_053579164.1; NZ_CP012608.1.
DR   EnsemblBacteria; ALD02318; ALD02318; AMQ28_08095.
DR   KEGG; att:AMQ28_08095; -.
DR   PATRIC; fig|1646498.3.peg.1636; -.
DR   KO; K02313; -.
DR   OrthoDB; 219876at2; -.
DR   Proteomes; UP000055186; 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   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 {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00756129};
KW   Complete proteome {ECO:0000313|Proteomes:UP000055186};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|SAAS:SAAS01082702};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU004227, ECO:0000256|SAAS:SAAS00756116};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS01082706};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00756117};
KW   Reference proteome {ECO:0000313|Proteomes:UP000055186}.
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;  51880 MW;  B92D1B158EA7E667 CRC64;
     MLWTDCLTRL RQELSGNVFT MWIRPLVAEE LNDTLRLYAP NPYWTRYIQE HHLELITILA
     EQMSEGRVRK VEILVDSRPG AILSAHEQPA TTTAALQSNP APVIKPKKEK DETSSKNTRK
     RLLNPLFTFS LFVEGRSNQM AAETCRKVLT QLGASQHNPL FLYGPTGLGK THLMQAVGNA
     LLQAKPNARV MYMTAESFVQ DFVSSLQQGK VEEFKKNCRS LDLLLVDDIH LLAGKEASLV
     EFFYTFNALL DESKQIILTS DRYPKELTEL DARLVSRFSW GLSVGVEPPD IETRIEILLK
     KAENSGVDLP RNCALFVAQQ VVANVRELEG ALNKVVAISR FKGTAIDLDV VRESLKDVLA
     IRARTISTEN IQRVVSEYFR IPLKEIVGPK RTRIYARPRQ LAMGLARELT GDSFPEIGMA
     FGGRDHSTVM HACEKVLSLR EQDPIFNEDY KNLQRLLQS
//
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