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Database: UniProt
Entry: Q3A8M8_PELCD
LinkDB: Q3A8M8_PELCD
Original site: Q3A8M8_PELCD 
ID   Q3A8M8_PELCD            Unreviewed;       450 AA.
AC   Q3A8M8;
DT   22-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 2.
DT   05-JUL-2017, entry version 99.
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:ABA87264.2};
GN   OrderedLocusNames=Pcar_0001 {ECO:0000313|EMBL:ABA87264.2};
OS   Pelobacter carbinolicus (strain DSM 2380 / NBRC 103641 / GraBd1).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC   Desulfuromonadaceae; Pelobacter.
OX   NCBI_TaxID=338963 {ECO:0000313|EMBL:ABA87264.2, ECO:0000313|Proteomes:UP000002534};
RN   [1] {ECO:0000313|Proteomes:UP000002534}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2380 / NBRC 103641 / GraBd1
RC   {ECO:0000313|Proteomes:UP000002534};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Chertkov O., Schmutz J., Larimer F.,
RA   Land M., Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of Pelobacter carbinolicus DSM 2380.";
RL   Submitted (OCT-2005) 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; CP000142; ABA87264.2; -; Genomic_DNA.
DR   RefSeq; WP_011339646.1; NC_007498.2.
DR   STRING; 338963.Pcar_0001; -.
DR   EnsemblBacteria; ABA87264; ABA87264; Pcar_0001.
DR   KEGG; pca:Pcar_0001; -.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   HOGENOM; HOG000235658; -.
DR   KO; K02313; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000002534; Chromosome.
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; 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   Complete proteome {ECO:0000313|Proteomes:UP000002534};
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:UP000002534}.
FT   DOMAIN      147    275       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      358    427       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     155    162       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   450 AA;  50877 MW;  93BD820F71D76BE0 CRC64;
     MEKIWQKTLD SLKQSLTPQH FATWIKPIRF IGVHNDVVEL EVPNRFVLDW LKKHYYGTIQ
     ECWSNTAGAA YKISLTVASK TAKEPVPAAE TSPPATPAPK PKQEKTPPRA NAYNLNSRYT
     FETFVLGSSN QFASAAATAV ANNPATTYNP LFIYGGVGLG KTHLVNAVGN AILKKNPEMK
     VCYYTSEKFM NELINSLRYA KMDEFRTKFR SMDVLLIDDV QFIAGKERTQ EEFFHTFNAL
     YDSHKQIVVT SDKFPKEIPG LEERLRSRFE WGLIADIQAP DMETKQAILK MKAEQNGIDL
     PKEVALFLAS AVSSNIRELE GYLVRIGAYA SLTATPITLS MAQEVLKDIL VEKRRELTVE
     EIQKLVATHY SIKISDLKSA KRMKALVLPR QIAMYLSRQL TSCSYPEIGE RFGGKDHSTI
     IHAIKKIEKA MDEDYQLRSV INNLKKELSI
//
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