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Database: UniProt
Entry: R4I1Z6_9GAMM
LinkDB: R4I1Z6_9GAMM
Original site: R4I1Z6_9GAMM 
ID   R4I1Z6_9GAMM            Unreviewed;       466 AA.
AC   R4I1Z6;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-SEP-2017, entry version 35.
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   ECO:0000313|EMBL:AEW44853.1};
GN   ORFNames=SCc_756 {ECO:0000313|EMBL:AEW44853.1};
OS   Serratia symbiotica str. 'Cinara cedri'.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia; Serratia symbiotica.
OX   NCBI_TaxID=568817 {ECO:0000313|EMBL:AEW44853.1, ECO:0000313|Proteomes:UP000013561};
RN   [1] {ECO:0000313|EMBL:AEW44853.1, ECO:0000313|Proteomes:UP000013561}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Cinara cedri {ECO:0000313|EMBL:AEW44853.1,
RC   ECO:0000313|Proteomes:UP000013561};
RA   Lamelas A., Gosalbes M.J., Moya A., Latorre A.;
RT   "The genome of Serratia symbiotica from Cinara cedri: A recent primary
RT   endosymbiont involved in the evolution of a microbial consortia.";
RL   Submitted (OCT-2010) 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}.
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DR   EMBL; CP002295; AEW44853.1; -; Genomic_DNA.
DR   EnsemblBacteria; AEW44853; AEW44853; SCc_756.
DR   KEGG; ssz:SCc_756; -.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   KO; K02313; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000013561; 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: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:UP000013561};
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:UP000013561}.
FT   DOMAIN      163    365       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      374    443       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     171    178       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
FT   COILED      436    463       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   466 AA;  52723 MW;  3277C278BECD6FB3 CRC64;
     MEFAVSLSLW QQCLVRLQNE LPATEFSMWI SPLQAQLTDN ILALYAPNRF VLDWVRDKYL
     NNLNSLLNDL CGTDAPLLRF EVGNKPINQI VSQAIAVNLS SVPAAARTAS LRPSWDNNAA
     ALPALSYRSN VNLKHTFDNF VEGKSNQLAR AAARQVSDNP GGAYNPLFLY GDTGLGKTHL
     LHAVGNGIIA RKIYAKVVYM HSERFVQGMV KALQNNAIEE FKRYYRSVDA LLIDDIQFFA
     NKERSQEEFF HTFNALLEGN QQIILTSDRY PKEIHGVEDR LKSRFGWGLT VAIEPPELET
     RVAILMKKAD ESNIYLPHEV AFFIAKRLHS NVRELEGALN RVIANANFTG HSITIDFVRE
     VLRDLLALQA KLVTIDNIQK TVAEYYKIKI SDLLSKRRSR SVARPRQIAM ALAKELTNHS
     LPEIGDAFSG RDHTTVLHAC RKIEQLREEI HDIKEDFSNL IRILSS
//
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