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Database: UniProt
Entry: A0A0X8JU92_9FUSO
LinkDB: A0A0X8JU92_9FUSO
Original site: A0A0X8JU92_9FUSO 
ID   A0A0X8JU92_9FUSO        Unreviewed;       457 AA.
AC   A0A0X8JU92;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-SEP-2017, entry version 13.
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   ORFNames=AXF11_05445 {ECO:0000313|EMBL:AMD95072.1};
OS   Leptotrichia sp. oral taxon 847.
OC   Bacteria; Fusobacteria; Fusobacteriales; Leptotrichiaceae;
OC   Leptotrichia.
OX   NCBI_TaxID=1785996 {ECO:0000313|EMBL:AMD95072.1, ECO:0000313|Proteomes:UP000065271};
RN   [1] {ECO:0000313|EMBL:AMD95072.1, ECO:0000313|Proteomes:UP000065271}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0260 {ECO:0000313|EMBL:AMD95072.1,
RC   ECO:0000313|Proteomes:UP000065271};
RA   Wen L., He K., Yang H.;
RL   Submitted (FEB-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: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; CP014231; AMD95072.1; -; Genomic_DNA.
DR   RefSeq; WP_068155637.1; NZ_CP014231.1.
DR   EnsemblBacteria; AMD95072; AMD95072; AXF11_05445.
DR   KEGG; lot:AXF11_05445; -.
DR   KO; K02313; -.
DR   Proteomes; UP000065271; 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:UP000065271};
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:UP000065271}.
FT   DOMAIN      146    285       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      362    433       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     154    161       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
FT   COILED       47     85       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   457 AA;  52845 MW;  FFF13045D35C15DC CRC64;
     MVEAEKLWEK LKKLIRKSVE EVIFETFFQN VKAVNIVENT LFLSCNSKVI KKNVENYKAE
     MEEILELVTD EKMEIKIDVK KQKKEIKQPE MKIFPTKEME KTKIQKEKPK NTGLNPKHRL
     DNFVVGENSR LAYNACLAVV NNPKPVYNPL FIFGSSGLGK THLMQAVGNE ILRKDPEKRV
     YYSTSEEFAN EFFKVLNSGR IQNFRDIFRN LDVLLLDDIQ FFEKVFGRGE GTVEEEFFHT
     FNKLQELGKQ IIMISDKSPK EIKNLSKRLE SRFLSGLTVE IQRPGFETRM MILKNIAKNQ
     DIEIGDDILE YISDAVVSNV RELEGILTNL NARAKLLNEP ITIEQVQEML SHNIKRERSK
     ITAQKVIEMI SSHYGISVAD MKSKKRQKKI VKSRQIAMFI LKNNAELDLS LTAIGGLFGG
     KDHSTVISSI RKVEKSKKED IVFKKEVEDL NRKIFKM
//
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