GenomeNet

Database: UniProt
Entry: A0A091ATV0_9GAMM
LinkDB: A0A091ATV0_9GAMM
Original site: A0A091ATV0_9GAMM 
ID   A0A091ATV0_9GAMM        Unreviewed;       442 AA.
AC   A0A091ATV0;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   16-JAN-2019, entry version 34.
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   ECO:0000313|EMBL:KFN42766.1};
GN   ORFNames=N787_03680 {ECO:0000313|EMBL:KFN42766.1};
OS   Arenimonas metalli CF5-1.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Arenimonas.
OX   NCBI_TaxID=1384056 {ECO:0000313|EMBL:KFN42766.1, ECO:0000313|Proteomes:UP000029393};
RN   [1] {ECO:0000313|EMBL:KFN42766.1, ECO:0000313|Proteomes:UP000029393}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CF5-1 {ECO:0000313|EMBL:KFN42766.1,
RC   ECO:0000313|Proteomes:UP000029393};
RA   Chen F., Wang G.;
RT   "Genome sequencing of Arenimonas metalli.";
RL   Submitted (SEP-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: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}.
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:KFN42766.1}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; AVCK01000044; KFN42766.1; -; Genomic_DNA.
DR   RefSeq; WP_034214224.1; NZ_AVCK01000044.1.
DR   EnsemblBacteria; KFN42766; KFN42766; N787_03680.
DR   PATRIC; fig|1384056.3.peg.2243; -.
DR   OrthoDB; 219876at2; -.
DR   Proteomes; UP000029393; 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   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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000029393};
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:UP000029393}.
FT   DOMAIN      139    270       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      350    419       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     147    154       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
FT   COILED      301    321       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   442 AA;  49588 MW;  686BDBC8FC04A43C CRC64;
     MDAAWPRCLE RLEAELPAEE IHAWLRPLQA EARADGLTLY APNAFVVDQV REHYLDRIRE
     LVSHFAGGPA PVALAVGSIK RAEAPMAGTA PAAARPAPPA AAFAGNLDGH YTFDNFVEGR
     SNQLGRAAAL QVAQNPGKAY NPLLLYGGSG LGKTHLMHAA GNLMRQNNPG MRVLYLRSEQ
     FFSAMMKSLQ EKSMDQFKRQ FQQVDALLID DIQFFAGKNT TQEEFFHTFN ALFDGKQQII
     LTCDRYPREV ENLETRLKTR LTWGLSVAIE PPDFETRAAI IAAKAVERGV KLPDDVAYLI
     AKRMRSNVRD LEGALNTLAA RSNFMARPIT AEFAQETLRD LLRAQQQVVS ISNIQKTVAD
     YYQLRMADLL SKRRTRSLAR PRQMAMALSK ELTEHSLPEI GDAFAGRDHT TVMHACKVMR
     ELREIDGKLR EDWDKLLRKL SE
//
DBGET integrated database retrieval system