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Database: UniProt
Entry: S7V2S6_DESML
LinkDB: S7V2S6_DESML
Original site: S7V2S6_DESML 
ID   S7V2S6_DESML            Unreviewed;       449 AA.
AC   S7V2S6;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   05-JUL-2017, entry version 28.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU000577};
GN   Name=dnaA {ECO:0000256|HAMAP-Rule:MF_00377};
GN   ORFNames=dsmv_0373 {ECO:0000313|EMBL:EPR38963.1};
OS   Desulfococcus multivorans DSM 2059.
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales;
OC   Desulfobacteraceae; Desulfococcus.
OX   NCBI_TaxID=1121405 {ECO:0000313|EMBL:EPR38963.1, ECO:0000313|Proteomes:UP000014977};
RN   [1] {ECO:0000313|EMBL:EPR38963.1, ECO:0000313|Proteomes:UP000014977}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2059 {ECO:0000313|EMBL:EPR38963.1,
RC   ECO:0000313|Proteomes:UP000014977};
RX   PubMed=23950126;
RA   Brown S.D., Hurt R.A.Jr., Gilmour C.C., Elias D.A.;
RT   "Draft genome sequences for three mercury-methylating, sulfate-
RT   reducing bacteria.";
RL   Genome Announc. 1:e00618-13(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}.
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:EPR38963.1}.
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DR   EMBL; ATHJ01000094; EPR38963.1; -; Genomic_DNA.
DR   RefSeq; WP_020877035.1; NZ_FUWN01000005.1.
DR   EnsemblBacteria; EPR38963; EPR38963; dsmv_0373.
DR   PATRIC; fig|1121405.3.peg.2766; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000014977; 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; 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.
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:UP000014977};
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:UP000014977}.
FT   NP_BIND     154    161       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   449 AA;  51042 MW;  B26CB82DC6A0B0F4 CRC64;
     MEDIWKNVKA VVKKEIPAHS FRMWIEPVEF VKADGNTIVL SCPNFFAKKR VMDHYGAMIE
     ALFKKDTGKN CSISIEIASR QNSVRRRSDA NELRIEPQLE LPSMPPPPSS GRLLRKNFTF
     DRFVVGSNSN FAYSAALSLA SRQGINHNSL FLMSQTGLGK SHLSQAIGHH ILSHFPTENV
     YYITAEDFTN EMIRAFRNDA IEQFKLKYRN QCDVLLLEDV HFLTGKERTQ MELAQALDYL
     IDADKKIIFT SCHLPAEIPN MSEQLKSRLA RSLISHIEIP DFQTRIKILK RKMVEHGCML
     PSSVTEYLAG ELSENVRQLE SGLIGVTAKA SLLGEPIDLR LAESVVRNIT QRKQAITVDY
     IKKLVCRQFK ISVEEIVSPS RKRAIVRPRQ VAIYLARKYT DQPLQAIGKS FNRYHGTALH
     SIAAVEKGIR SDGSLKKQLE FLCERIESH
//
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