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Database: UniProt
Entry: V9XLB7_9NOCA
LinkDB: V9XLB7_9NOCA
Original site: V9XLB7_9NOCA 
ID   V9XLB7_9NOCA            Unreviewed;       601 AA.
AC   V9XLB7;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   25-OCT-2017, entry version 33.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU000577};
GN   Name=dnaA {ECO:0000256|HAMAP-Rule:MF_00377};
GN   ORFNames=Y013_16495 {ECO:0000313|EMBL:AHD22132.1};
OS   Rhodococcus pyridinivorans SB3094.
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=1435356 {ECO:0000313|EMBL:AHD22132.1, ECO:0000313|Proteomes:UP000018781};
RN   [1] {ECO:0000313|EMBL:AHD22132.1, ECO:0000313|Proteomes:UP000018781}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SB3094 {ECO:0000313|EMBL:AHD22132.1};
RX   PubMed=24874690;
RA   Dueholm M.S., Albertsen M., D'Imperio S., Tale V.P., Lewis D.,
RA   Nielsen P.H., Nielsen J.L.;
RT   "Complete Genome of Rhodococcus pyridinivorans SB3094, a Methyl-Ethyl-
RT   Ketone-Degrading Bacterium Used for Bioaugmentation.";
RL   Genome Announc. 2:e00525-14(2014).
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:SAAS00735475}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
CC       ECO:0000256|SAAS:SAAS00911680}.
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; CP006996; AHD22132.1; -; Genomic_DNA.
DR   RefSeq; WP_024102542.1; NC_023150.1.
DR   EnsemblBacteria; AHD22132; AHD22132; Y013_16495.
DR   GeneID; 29937623; -.
DR   KEGG; rpy:Y013_16495; -.
DR   PATRIC; fig|1435356.3.peg.3329; -.
DR   KO; K02313; -.
DR   Proteomes; UP000018781; 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; 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   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:SAAS00747950};
KW   Complete proteome {ECO:0000313|Proteomes:UP000018781};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|SAAS:SAAS00911664};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU004227, ECO:0000256|SAAS:SAAS00747996};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00911684};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00747895};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018781}.
FT   DOMAIN      294    422       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      506    574       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     302    309       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   601 AA;  67669 MW;  F6F30D6324095E85 CRC64;
     MSDEPNALAD VWTDVVSELT IDDGMLTKSQ KAWLALVKPI TLAQGFALLS VPSTLAQQSI
     ERDLREPILR TLNRHLGHRV EGLGVRVEPR ERMDDPAEDP YAEPRDTLPL EGLPEDAQPV
     NPRTAEPRSR DPRTAEPRSR DPRTAEPRSR DPRTAEPRSR DLRRDPPMPR DVAGARDGAV
     ARDGVGPRDG GFTRDGMLPG EGAAYRRRLI SSREHDMLEA DHGELEEVDD DREAMTAVRE
     SWPSYFTQPP PPETPPIGSS SLNAKYTFDT FVIGASNRFA HAAAVAIAEA PARAYNPLFI
     WGASGLGKTH LLHAAGHYAQ RLFPGMRVKY VSTEEFTNDF INSLRDDRKV AFKRRYRETD
     ILLVDDIQFI EGKEGIQEEF FHTFNTLHNA NKQIVVSSDR PPKQLATLEE RLRTRFEWGL
     ITDVQPPELE TRIAILSKKA RMDGLNVPHD VLELIASRIE RNIRELEGAL IRVTAFASLN
     RQPLDLTLAE VVLRDLMPDS SALEINAATI MAVTAEYFGT SIDDLCGPGK ARPLAQARQI
     AMYLCRELTD LSLPKIGQTF GRDHTTVMYA DKKIRKEMTE RRKVYDQVQE LTARIKQRSK
     R
//
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