GenomeNet

Database: UniProt
Entry: W4S4L0_9XANT
LinkDB: W4S4L0_9XANT
Original site: W4S4L0_9XANT 
ID   W4S4L0_9XANT            Unreviewed;       442 AA.
AC   W4S4L0;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   16-JAN-2019, entry version 39.
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:GAE50874.1};
GN   ORFNames=XPU_2406 {ECO:0000313|EMBL:GAE50874.1};
OS   Xanthomonas arboricola pv. pruni str. MAFF 311562.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=1414836 {ECO:0000313|EMBL:GAE50874.1, ECO:0000313|Proteomes:UP000019143};
RN   [1] {ECO:0000313|EMBL:GAE50874.1, ECO:0000313|Proteomes:UP000019143}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MAFF 311562 {ECO:0000313|Proteomes:UP000019143};
RA   Fujikawa T., Nakazono-Nagaoka E.;
RT   "Genome sequence and analysis of Xanthomonas arboricola pv. pruni.";
RL   Submitted (JAN-2014) 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:GAE50874.1}.
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DR   EMBL; BAVB01000277; GAE50874.1; -; Genomic_DNA.
DR   EnsemblBacteria; GAE50874; GAE50874; XPU_2406.
DR   Proteomes; UP000019143; 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:UP000019143};
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      139    270       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      350    419       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     147    154       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
FT   COILED      301    321       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   442 AA;  49571 MW;  0A47499C6A12CFCD CRC64;
     MDAWPRCLER LEAEFPPEDV HTWLKPLQAE DRGDSIVLYA PNAFIVDQVR ERYLPRIREL
     VAYFVGNGEV ALAVGSRPRA PEPQPAPMAA PSAPVAAPIV PFAGNLDSHY TFANFVEGRS
     NQLGLAAAIQ AAQKPGDRAH NPLLLYGSTG LGKTHLMFAA GNALRQANPA AKVMYLRSEQ
     FFSAMIRALQ DKAMDQFKRQ FQQIDALLID DIQFFAGKDR TQEEFFHTFN ALFDGRQQII
     LTCDRYPREV EGLEPRLKSR LAWGLSVAID PPDFETRAAI VLAKARERGA EIPDDVAFLI
     AKKMRSNVRD LEGALNTLVA RANFTGRSIT VEFAQETLRD LLRAQQQAIG IPNIQKTVAD
     YYGLQMKDLL SKRRTRSLAR PRQVAMALAK ELTEHSLPEI GDAFAGRDHT TVLHACRQIR
     TLMEADGKLR EDWEKLIRKL SE
//
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