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Database: UniProt
Entry: U7FSC0_9RHOB
LinkDB: U7FSC0_9RHOB
Original site: U7FSC0_9RHOB 
ID   U7FSC0_9RHOB            Unreviewed;       491 AA.
AC   U7FSC0;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-SEP-2017, entry version 27.
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=Q669_08465 {ECO:0000313|EMBL:ERP88479.1};
OS   Labrenzia sp. C1B10.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Labrenzia.
OX   NCBI_TaxID=1397530 {ECO:0000313|EMBL:ERP88479.1, ECO:0000313|Proteomes:UP000017101};
RN   [1] {ECO:0000313|EMBL:ERP88479.1, ECO:0000313|Proteomes:UP000017101}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C1B10 {ECO:0000313|EMBL:ERP88479.1};
RX   PubMed=24356826;
RA   Overholt W.A., Green S.J., Marks K.P., Venkatraman R., Prakash O.,
RA   Kostka J.E.;
RT   "Draft genome sequences for oil-degrading bacterial strains from beach
RT   sands impacted by the deepwater horizon oil spill.";
RL   Genome Announc. 1:e01015-13(2013).
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:ERP88479.1}.
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DR   EMBL; AXBY01000045; ERP88479.1; -; Genomic_DNA.
DR   EnsemblBacteria; ERP88479; ERP88479; Q669_08465.
DR   PATRIC; fig|1397530.3.peg.4328; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000017101; 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:UP000017101};
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:UP000017101}.
FT   DOMAIN      185    314       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      399    468       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     193    200       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   491 AA;  54819 MW;  2712A98824D58EC8 CRC64;
     MEATMQVQNL AGSDQWDRVK KELRNELGDD VFSNWFGRVK HEETTGDAVR LSVPTRFLKN
     WIQNNYEKQL VGLWKREQDD INRIELTVRG ALRPRQLNVG LAPKAISARR ISGRPGPFSS
     TPQFGASHGM SVIPCLADSN EDAAADFLNG ASLNPKLTFD TFAEGASNSL ACAAVRQMAA
     GHQGTLDLLY IHSSTGIGKT HLLQAAAAEA RKTGRQVAYL SAEFFMYHLV PALRTPAFPV
     LRQAMRSIDL LLVDDLQFLH GKQAADEFSK TLELLMESPT QIIMAADRSP EDLDTLGDAL
     RYRIQKGEVV GIQSTDYALR HDILKKRITA ARRTHPGFSV PEDVADYIAR YVIASARDLE
     GALNRLFAHN QLTKQPVTMD LAEKTLHDLV RIGEPRSIKV EEIQQVVCKH FSVTKADLLS
     SCRARTLVRP RQIAMYIAKV MTGRSLPEIG RRFGNRDHTT VLHAVRKIED MVSKDKTLAQ
     EVELLKRLVH A
//
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