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Database: UniProt
Entry: D5EC68_AMICL
LinkDB: D5EC68_AMICL
Original site: D5EC68_AMICL 
ID   D5EC68_AMICL            Unreviewed;       442 AA.
AC   D5EC68;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   16-JAN-2019, entry version 63.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS01081161};
GN   Name=dnaA {ECO:0000256|HAMAP-Rule:MF_00377};
GN   OrderedLocusNames=Amico_0001 {ECO:0000313|EMBL:ADE56150.1};
OS   Aminobacterium colombiense (strain DSM 12261 / ALA-1).
OC   Bacteria; Synergistetes; Synergistia; Synergistales; Synergistaceae;
OC   Aminobacterium.
OX   NCBI_TaxID=572547 {ECO:0000313|EMBL:ADE56150.1, ECO:0000313|Proteomes:UP000002366};
RN   [1] {ECO:0000313|EMBL:ADE56150.1, ECO:0000313|Proteomes:UP000002366}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12261 / ALA-1 {ECO:0000313|Proteomes:UP000002366};
RX   PubMed=21304712;
RA   Chertkov O., Sikorski J., Brambilla E., Lapidus A., Copeland A.,
RA   Glavina Del Rio T., Nolan M., Lucas S., Tice H., Cheng J.F., Han C.,
RA   Detter J.C., Bruce D., Tapia R., Goodwin L., Pitluck S., Liolios K.,
RA   Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA   Spring S., Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Aminobacterium colombiense type strain
RT   (ALA-1).";
RL   Stand. Genomic Sci. 2:280-289(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:SAAS00756121}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
CC       ECO:0000256|SAAS:SAAS01082709}.
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; CP001997; ADE56150.1; -; Genomic_DNA.
DR   RefSeq; WP_013047416.1; NC_014011.1.
DR   ProteinModelPortal; D5EC68; -.
DR   STRING; 572547.Amico_0001; -.
DR   EnsemblBacteria; ADE56150; ADE56150; Amico_0001.
DR   KEGG; aco:Amico_0001; -.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   HOGENOM; HOG000235658; -.
DR   KO; K02313; -.
DR   OMA; REFNPLF; -.
DR   OrthoDB; 219876at2; -.
DR   BioCyc; ACOL572547:G1GHU-1-MONOMER; -.
DR   Proteomes; UP000002366; 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   Gene3D; 3.30.300.180; -; 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; IPR038454; DnaA_N_sf.
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:SAAS00756129};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002366};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|SAAS:SAAS01082702};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU004227, ECO:0000256|SAAS:SAAS00756116};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS01082706};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00756117};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002366}.
FT   DOMAIN      140    276       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      352    421       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     148    155       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   442 AA;  50253 MW;  038D5D05243D2AD3 CRC64;
     MVDKDINVLW DDILKNIEET MPEGTADLWL KTCVPLSVMN DVLVIDVPNV FVKEQISKRF
     QNVIEDVLMD KGYAQSLELK VASEARKDEQ QRAERAAQHT GTLPRSGLNP NYIFNSFVVG
     KSNRLAHAAS LAVAETPGEA YNPLFIWGGV GLGKTHLMHA IGHYVLNKNN SLKVTYVSSE
     KFINEFIQSI KNNRTQEFKS KYRSVDILLI DDIQFLGNKG SSQEEFFHTF NQLHVSKKQI
     VICSDRPPKE IQNIEDRLVS RFEWGLVTDI QMPDLETRIA ILQKKAQIRN YEVPEDVISF
     LAQNVPSNIR ELEGALNRII ACAELNSEPI TEENATQWLK DIIRHNSKGP VSVDTIQQIV
     AENFSLTVED LVGNRRTSDI ALARQVAMYL CRKLTDISLQ QIGFSFKKKD HTTVLHAQRK
     ISKLVEEQPR MKEIVDNIEA KL
//
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