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Database: UniProt
Entry: S7U033_9DELT
LinkDB: S7U033_9DELT
Original site: S7U033_9DELT 
ID   S7U033_9DELT            Unreviewed;       474 AA.
AC   S7U033;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   25-OCT-2017, entry version 33.
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=dsx2_2663 {ECO:0000313|EMBL:EPR42746.1};
OS   Desulfovibrio sp. X2.
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Desulfovibrio.
OX   NCBI_TaxID=941449 {ECO:0000313|EMBL:EPR42746.1, ECO:0000313|Proteomes:UP000014960};
RN   [1] {ECO:0000313|EMBL:EPR42746.1, ECO:0000313|Proteomes:UP000014960}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=X2 {ECO:0000313|EMBL:EPR42746.1,
RC   ECO:0000313|Proteomes:UP000014960};
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, ECO:0000256|SAAS:SAAS00724167}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
CC       ECO:0000256|SAAS:SAAS00911680}.
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:EPR42746.1}.
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DR   EMBL; ATHV01000019; EPR42746.1; -; Genomic_DNA.
DR   RefSeq; WP_020880543.1; NZ_ATHV01000019.1.
DR   EnsemblBacteria; EPR42746; EPR42746; dsx2_2663.
DR   PATRIC; fig|941449.3.peg.1552; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000014960; 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: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:SAAS00747950};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000014960};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|SAAS:SAAS00911664};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU004227, ECO:0000256|SAAS:SAAS00747996};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00911684};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00747895};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014960}.
FT   DOMAIN      169    306       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      383    451       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     177    184       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
FT   COILED      335    362       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   474 AA;  52445 MW;  8A9DA27D901C56BF CRC64;
     MKHGWDHILN ILEKRLNPGL FKVWIKPLSA TFDDGSLTLI APNDFVASWV RDRLLDTVAE
     AAEQVLGSVK SINVKAQAQK AQVASRAQLV SSAVRTIAAP VDADGHSPRT SDRMPAGMGD
     GLAGAHGQPC SLNGDQSFRW RFSFDDFVVG PSNALAHAAS QSVCQCSLHA DQLFLCSAPG
     LGKTHLIQAI GGHLARAAVN RSVRLRYLTA EEFATRMVVA LKMGEIERFK AEFRESVDLL
     LLEDIHFLQG KEKIQDELLA TLKALQSRGS KVVFTSSFLP RELSGVDSQL ASRFGAGFLA
     VIDRPDFTTR MRIVEQKAQR QHATIIPEDV SALMAERIKT DIRQLESCLQ NLILKAKLLR
     QNITQDLAMQ VLANYAIDAD SPDMERIITA VCRTFQLDAG DLASKSRRQG VVMARNTAFF
     LARKYTDLSL KDIGVRFNRK HSTVLKGITK VEREMTKRTP AGRQFERALD LLEI
//
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