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Database: UniProt
Entry: A0A081SJB8_9CHLB
LinkDB: A0A081SJB8_9CHLB
Original site: A0A081SJB8_9CHLB 
ID   A0A081SJB8_9CHLB        Unreviewed;       484 AA.
AC   A0A081SJB8;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   05-JUL-2017, entry version 23.
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=HY22_01275 {ECO:0000313|EMBL:KER11021.1};
OS   Chlorobium sp. GBChlB.
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC   Chlorobium/Pelodictyon group; Chlorobium.
OX   NCBI_TaxID=1519464 {ECO:0000313|EMBL:KER11021.1, ECO:0000313|Proteomes:UP000028104};
RN   [1] {ECO:0000313|EMBL:KER11021.1, ECO:0000313|Proteomes:UP000028104}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Stamps B.W., Stevenson B.S.;
RT   "Binning of Metagenomic Samples from Little Hot Creek.";
RL   Submitted (JUL-2014) 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:KER11021.1}.
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DR   EMBL; JPGV01000006; KER11021.1; -; Genomic_DNA.
DR   EnsemblBacteria; KER11021; KER11021; HY22_01275.
DR   PATRIC; fig|1519464.4.peg.266; -.
DR   Proteomes; UP000028104; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000028104};
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:UP000028104}.
FT   DOMAIN      178    308       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      389    458       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     186    193       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
FT   COILED      458    484       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   484 AA;  54739 MW;  6865BBF6B2F9DBC3 CRC64;
     MNHTPTTHSD TQSAERQAAQ DAWKKCLAII EDNINSQSFK TWFEPIVPLR LSGEELTIQV
     PSQFFYEWIE ENYYSLLKRT ILDVIGRNAK LTYSVVVQQS PVEPVTIKLP QQQSELPPPE
     PRPIAVSRAA QDFYKANVHR FEGYLKPTHT FDNFIKGDCN ALALAAAKSV AETPGKNNFN
     PLVVYGGVGL GKTHLVQAIG NYVKVKRKAE FILYVSSEKF TIDFVSAIQS GKISEFSAFY
     RNIDLLIIDD VQFFEKKEKT QEEIFHIFNA LHQSGKQIVL SCDRPLKELR GLEERLLSRF
     QWGLSTDLQA PDFETRLAIL RRKMDDNGTT LPPDVINFIA TNVTSNVREM EGCLIKLLAT
     ASMLGRDIDL PLTKSILKDI IRDKAMNISL EMIEKAVCDY FKISPNDIKG KSRKQEIALA
     RQVAMYLGKQ LTGSSLKTIG LHFGGRDHST VIHACQTIEE AQQNSADLRK DLEELKKRLD
     IMSL
//
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