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Database: UniProt
Entry: M4WPH0_9PSED
LinkDB: M4WPH0_9PSED
Original site: M4WPH0_9PSED 
ID   M4WPH0_9PSED            Unreviewed;       510 AA.
AC   M4WPH0;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   16-JAN-2019, entry version 46.
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:AGI21883.1};
GN   ORFNames=H681_00005 {ECO:0000313|EMBL:AGI21883.1};
OS   Pseudomonas sp. ATCC 13867.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1294143 {ECO:0000313|EMBL:AGI21883.1, ECO:0000313|Proteomes:UP000012082};
RN   [1] {ECO:0000313|EMBL:AGI21883.1, ECO:0000313|Proteomes:UP000012082}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13867 {ECO:0000313|EMBL:AGI21883.1,
RC   ECO:0000313|Proteomes:UP000012082};
RX   PubMed=23723394;
RA   Ainala S.K., Somasundar A., Park S.;
RT   "Complete Genome Sequence of Pseudomonas denitrificans ATCC 13867.";
RL   Genome Announc. 1:E00257-13(2013).
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; CP004143; AGI21883.1; -; Genomic_DNA.
DR   RefSeq; WP_015474771.1; NC_020829.1.
DR   EnsemblBacteria; AGI21883; AGI21883; H681_00005.
DR   GeneID; 32561931; -.
DR   KEGG; pdr:H681_00005; -.
DR   PATRIC; fig|1294143.3.peg.1; -.
DR   KO; K02313; -.
DR   OrthoDB; 219876at2; -.
DR   BioCyc; PDEN1294143:G1HG9-1-MONOMER; -.
DR   Proteomes; UP000012082; 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   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:UP000012082};
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      207    416       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      418    487       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     215    222       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   510 AA;  57485 MW;  7FD7BEA37ADA18E8 CRC64;
     MSVELWQQCV ELLRDELPSQ QFNTWIRPLQ VEAEGEELRV YAPNRFVLDW VNEKYMGRML
     ELLSERGNGQ IPALSLLIGS RRSRTPRPAL VPQSHVSVQP TPAPTVVVAP PPVVPVAVAP
     VIPEPQPVQV VAQPLPDLDE SSPGIDPLAA AMPATSVRTE RNVQVEGALK HTSYLNRTFT
     FENFVEGKSN QLARAAAWQV ADNLKHGYNP LFLYGGVGLG KTHLMHAVGN HLLKKNPNAK
     VVYLHSERFV ADMVKALQLN AINEFKRFYR SVDALLIDDI QFFARKERSQ EEFFHTFNAL
     LEGGQQVILT SDRYPKEIEG LEERLKSRFG WGLTVAVEPP ELETRVAILM KKAEQAKVEL
     PHDAAFFIAQ RIRSNVRELE GALKRVIAHS HFMGRPITIE LIRESLKDLL ALQDKLVSID
     NIQRTVAEYY KIKIADLLSK RRSRSVARPR QVAMALSKEL TNHSLPEIGV AFGGRDHTTV
     LHACRKIAQL KESDADIRED YKNLLRTLTT
//
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