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Database: UniProt
Entry: A0A168FKW8_9MICO
LinkDB: A0A168FKW8_9MICO
Original site: A0A168FKW8_9MICO 
ID   A0A168FKW8_9MICO        Unreviewed;       476 AA.
AC   A0A168FKW8;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   25-OCT-2017, entry version 14.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU000577};
GN   Name=dnaA {ECO:0000256|HAMAP-Rule:MF_00377,
GN   ECO:0000313|EMBL:ANC32041.1};
GN   ORFNames=I598_2507 {ECO:0000313|EMBL:ANC32041.1};
OS   Isoptericola dokdonensis DS-3.
OC   Bacteria; Actinobacteria; Micrococcales; Promicromonosporaceae;
OC   Isoptericola.
OX   NCBI_TaxID=1300344 {ECO:0000313|EMBL:ANC32041.1, ECO:0000313|Proteomes:UP000076794};
RN   [1] {ECO:0000313|EMBL:ANC32041.1, ECO:0000313|Proteomes:UP000076794}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS-3 {ECO:0000313|EMBL:ANC32041.1,
RC   ECO:0000313|Proteomes:UP000076794};
RA   Kwon S.-K., Kim J.F.;
RT   "Complete genome sequence of a soil Actinobacterium, Isoptericola
RT   dokdonensis DS-3.";
RL   Submitted (JAN-2016) 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:SAAS00735475}.
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; CP014209; ANC32041.1; -; Genomic_DNA.
DR   RefSeq; WP_068203227.1; NZ_CP014209.1.
DR   EnsemblBacteria; ANC32041; ANC32041; I598_2507.
DR   KEGG; ido:I598_2507; -.
DR   PATRIC; fig|1300344.3.peg.2515; -.
DR   KO; K02313; -.
DR   Proteomes; UP000076794; 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; 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   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:UP000076794};
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:UP000076794}.
FT   DOMAIN      167    295       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      380    449       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     175    182       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   476 AA;  53079 MW;  891CB086523A7E87 CRC64;
     MAQSDANITD VWSQTLATLE ARSDISARQL AFIRLAKPMA ILEDTVFIAV PHEQTRTYLE
     TSARDQLVSA MSSTLGRDVR FGITVDPELS HESLTGPAQD YAPPVETPTE PDTPAAMPVS
     PLPADRKDRV EPTRLHPKYI FETFVIGSSN RFAHAAAVAV AEAPAKAYNP LFIYGDSGLG
     KTHLLHAIGH YAHNLYPHVR VRYVNSEEFT NDFINSIGDG RTGAFQRRYR DVDVLLIDDI
     QFLQGKEQTM EEFFHTFNAL HNADKQVVIT SDVPPKKLDG FEDRLRSRFE WGLITDVQPP
     DLETRIAILR KKAASERLDV PAEVLSYIGS RISTNIRELE GALIRVTAFA NLNKQQVDLA
     LAEIVLKDLL TDDDQAAEIT PAVVIAQTAA YFGLTIEDLC GTSRSRVLVT ARQIAMYLCR
     ELTDLSLPKI GQQFGGRDHT TVMHANRKIA GQMAERRSTY NQVTELTSRI KQQHRG
//
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