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Database: UniProt
Entry: A0A1V3LBJ0_9PAST
LinkDB: A0A1V3LBJ0_9PAST
Original site: A0A1V3LBJ0_9PAST 
ID   A0A1V3LBJ0_9PAST        Unreviewed;       454 AA.
AC   A0A1V3LBJ0;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   16-JAN-2019, entry version 14.
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   ECO:0000313|EMBL:OOF86998.1};
GN   ORFNames=BKG88_02985 {ECO:0000313|EMBL:OOF86998.1};
OS   Rodentibacter ratti.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Rodentibacter.
OX   NCBI_TaxID=1906745 {ECO:0000313|EMBL:OOF86998.1, ECO:0000313|Proteomes:UP000189353};
RN   [1] {ECO:0000313|EMBL:OOF86998.1, ECO:0000313|Proteomes:UP000189353}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ppn158 {ECO:0000313|EMBL:OOF86998.1,
RC   ECO:0000313|Proteomes:UP000189353};
RA   Christensen H.;
RT   "Rodentibacter gen. nov. and new species.";
RL   Submitted (OCT-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: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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:OOF86998.1}.
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DR   EMBL; MLAI01000011; OOF86998.1; -; Genomic_DNA.
DR   Proteomes; UP000189353; Unassembled WGS sequence.
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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000189353};
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}.
FT   DOMAIN      152    280       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      363    431       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     160    167       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
FT   COILED      314    334       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   454 AA;  52009 MW;  F5B1AEE91939B8DD CRC64;
     MSLSNLWQDC LSQLQDQVSA TDLSTWLRPL QADTVSQDKI VLYASNMFVK GWVETHYLKQ
     IHQICQTLSQ NPNLQIILKE GVKPTPQAAI KPTMQSTESA VNSYDKPEVA KPLKFDSHLN
     TKHVFENFVE GKSNQLARAV GQKLAQAPGE ATANPFFLYG GTGLGKTHLL HAIGNGILAN
     KPNARVLYIH ANNFMQHMVK AMRDNNMDQF KKFYRSLDAL LVDDIQFFAE KEKTQEEFFH
     IFNNLFETGR QIILTSDRYP KEIEKIEERL KSRFGWGLTT AIEPPDLETR VAILLKKAEE
     HQMHLPEEVA FFIAQRLRTN VRELEGALNR VKAMQDFKGG EINIDFVRDT LKDILALQER
     LVTIDNIQKT VAEYYRIKVS DLKSKSRQRS VTRPRQIAMA LAKELTNRSL PEIGRAFDRD
     HTTVLNACRE VPKFREKDNS IQEDWANLIR TLSA
//
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