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Database: UniProt
Entry: C6RRR8_ACIRA
LinkDB: C6RRR8_ACIRA
Original site: C6RRR8_ACIRA 
ID   C6RRR8_ACIRA            Unreviewed;       460 AA.
AC   C6RRR8;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   30-AUG-2017, entry version 50.
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   ECO:0000313|EMBL:EET81558.1};
GN   ORFNames=ACIRA0001_0590 {ECO:0000313|EMBL:EET81558.1};
OS   Acinetobacter radioresistens SK82.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Acinetobacter.
OX   NCBI_TaxID=596318 {ECO:0000313|EMBL:EET81558.1, ECO:0000313|Proteomes:UP000018419};
RN   [1] {ECO:0000313|EMBL:EET81558.1, ECO:0000313|Proteomes:UP000018419}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SK82 {ECO:0000313|EMBL:EET81558.1,
RC   ECO:0000313|Proteomes:UP000018419};
RA   Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA   Strausberg R.L., Nelson K.E.;
RL   Submitted (JUL-2009) 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:EET81558.1}.
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DR   EMBL; ACVR01000069; EET81558.1; -; Genomic_DNA.
DR   RefSeq; WP_005017523.1; NZ_ACVR01000069.1.
DR   EnsemblBacteria; EET81558; EET81558; ACIRA0001_0590.
DR   GeneID; 23269812; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000018419; Unassembled WGS sequence.
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:0006270; P:DNA replication initiation; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006275; P:regulation of DNA replication; IEA:UniProtKB-HAMAP.
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:UP000018419};
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:UP000018419}.
FT   DOMAIN      157    287       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      368    437       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     165    172       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   460 AA;  52084 MW;  244E0097BAEED46A CRC64;
     MLWTDCLTRL RQELSDNIFA MWIRPLVAEE LEDTLRLYAP NPYWTRYIQE HHLELITILA
     EQMSEGRVRK VEILVDSRPG AILSAAEQPA TTTAALEHPA SMPVSRPKKE KEAEPAKQNK
     KRLLNPLFTF ALFVEGRSNQ MAAETCRKVL TQLGASQHNP LFLYGPTGLG KTHLMQAVGN
     ALLQAKPNAR VMYMTAESFV QDFVSSLQRG KVEEFKKNCR SLDLLLVDDI HLLAGKEASL
     VEFFYTFNAL LDESKQIILT SDRYPKELTE LDPRLVSRFS WGLSVGVEPP DIETRIEILL
     KKAESNEIDL PRNCALFIAQ QVVANVRELE GALNKVVAIS RFKGTAIDLD VVRESLKDVL
     AIRARTISVE NIQRVVSEYF RIPLKELVGP KRTRIYARPR QLAMGLAREL TGDSFPEIGM
     AFGGRDHSTV MHACEKVQSL RAEDPIFNED YKNLLRLLQS
//
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