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Database: UniProt
Entry: E1QGB0_DESB2
LinkDB: E1QGB0_DESB2
Original site: E1QGB0_DESB2 
ID   E1QGB0_DESB2            Unreviewed;       457 AA.
AC   E1QGB0;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   25-OCT-2017, entry version 53.
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   OrderedLocusNames=Deba_0245 {ECO:0000313|EMBL:ADK83622.1};
OS   Desulfarculus baarsii (strain ATCC 33931 / DSM 2075 / VKM B-1802 /
OS   2st14).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfarculales;
OC   Desulfarculaceae; Desulfarculus.
OX   NCBI_TaxID=644282 {ECO:0000313|EMBL:ADK83622.1, ECO:0000313|Proteomes:UP000009047};
RN   [1] {ECO:0000313|EMBL:ADK83622.1, ECO:0000313|Proteomes:UP000009047}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33931 / DSM 2075 / VKM B-1802 / 2st14
RC   {ECO:0000313|Proteomes:UP000009047};
RX   PubMed=21304732;
RA   Sun H., Spring S., Lapidus A., Davenport K., Del Rio T.G., Tice H.,
RA   Nolan M., Copeland A., Cheng J.F., Lucas S., Tapia R., Goodwin L.,
RA   Pitluck S., Ivanova N., Pagani I., Mavromatis K., Ovchinnikova G.,
RA   Pati A., Chen A., Palaniappan K., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Detter J.C., Han C., Rohde M., Brambilla E., Goker M.,
RA   Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Land M.;
RT   "Complete genome sequence of Desulfarculus baarsii type strain
RT   (2st14).";
RL   Stand. Genomic Sci. 3:276-284(2010).
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}.
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DR   EMBL; CP002085; ADK83622.1; -; Genomic_DNA.
DR   STRING; 644282.Deba_0245; -.
DR   EnsemblBacteria; ADK83622; ADK83622; Deba_0245.
DR   KEGG; dbr:Deba_0245; -.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   HOGENOM; HOG000235659; -.
DR   KO; K02313; -.
DR   OMA; REFNPLF; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000009047; Chromosome.
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   Complete proteome {ECO:0000313|Proteomes:UP000009047};
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:UP000009047}.
FT   DOMAIN      149    275       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      358    427       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     157    164       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   457 AA;  50817 MW;  79908B2F3BF241E9 CRC64;
     MQSDIGRPVL WEQVRQTMRG QVDHREFETW LAPLAMRLEA DWAVISAPNR FFVDWIKDHY
     LSQLEQVISQ CAARPLRLRF ETGNGPVPAS RPVEAQPALA QPAPAAPALT SLAQPTLKPG
     YTFETFIVGT CNELAHAACR AVAQQPGRQY NPLLIFGGAG LGKTHLLHAV GNAFYQRDPR
     AKVLYTTCEA FTNELIQAVR FDSIGRFQEK YRGLDCLLLD DIQFLAGRER TQEELFHTFN
     ALQESGGQIV LTSDDPPREL QGVVKRLRTR FEGGLTADLQ PPPSEIMVAI LQSKALAKGM
     DLSDQVAMFL ARQPESNVRV LEGYLNRIIA VSRFQGVEVT LELARRVVGP LMAQRQVSVE
     EVLQTVAARY GVRVGELKSS RKTRDVTRPR QVAMFLARQL TGQSYPEIGR ALGGKDHSTV
     VKGVKKIQGQ MAREAALAEE IRTLERELLE GGETPVD
//
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