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Database: UniProt
Entry: A0A1N7JKF2_9RHOB
LinkDB: A0A1N7JKF2_9RHOB
Original site: A0A1N7JKF2_9RHOB 
ID   A0A1N7JKF2_9RHOB        Unreviewed;       456 AA.
AC   A0A1N7JKF2;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   13-FEB-2019, entry version 15.
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   ORFNames=SAMN05421759_10137 {ECO:0000313|EMBL:SIS49843.1};
OS   Roseivivax lentus.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Roseivivax.
OX   NCBI_TaxID=633194 {ECO:0000313|EMBL:SIS49843.1, ECO:0000313|Proteomes:UP000186684};
RN   [1] {ECO:0000313|EMBL:SIS49843.1, ECO:0000313|Proteomes:UP000186684}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 29430 {ECO:0000313|EMBL:SIS49843.1,
RC   ECO:0000313|Proteomes:UP000186684};
RA   Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL   Submitted (JAN-2017) 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}.
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DR   EMBL; FTOQ01000001; SIS49843.1; -; Genomic_DNA.
DR   RefSeq; WP_076443811.1; NZ_FTOQ01000001.1.
DR   BioCyc; GCF_900156805:BW990_RS00185-MONOMER; -.
DR   Proteomes; UP000186684; 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   Complete proteome {ECO:0000313|Proteomes:UP000186684};
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:UP000186684}.
FT   DOMAIN      148    278       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      364    433       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     156    163       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   456 AA;  51476 MW;  E4B8AE1C5A1B8DFD CRC64;
     MTLEQWDTVQ DNLARTLGEN NFATWIKPLK FDECKDGVAV LRAPTHFVGN YVSQNFGDAI
     LAGISHVQPD VRRIQFRVAM DRKIQGQAPV RPAKPAATPT DNVARDASDL LPSAPLEPRL
     NFDNFVVGKP NELANAAARR VAEGGPVTFN PLFLHGGVGL GKTHLMHAIA LELRARNPEL
     NVLYLSAEQF MYRFVQALRD RRMMDFKSLF RSVDVLMVDD VQFIAGKDST QEEFFHTFNT
     LVDQNKQIVI SADRAPDEIK DMENRIRSRL QSGLVVDLHP TDYELRLGIL QSKCESHGVH
     YPDVIIEDGV LAFLAHRISS NVRVLEGALN RLYAFASLVG KPVTLELAQD CLSDVIRASE
     RKISVEEIQR KVAEHYHIRL SDLIGPKRVR NFARPRQVAM YLCKQMTARS LPDIGRRFGG
     RDHTTVMHGV KRIEDLMRSD AQIAEDVELL RRALEE
//
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