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Database: UniProt
Entry: A0A0X3VN95_9ACTN
LinkDB: A0A0X3VN95_9ACTN
Original site: A0A0X3VN95_9ACTN 
ID   A0A0X3VN95_9ACTN        Unreviewed;       614 AA.
AC   A0A0X3VN95;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   25-OCT-2017, entry version 15.
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   ECO:0000313|EMBL:KUL45847.1};
GN   ORFNames=ADL22_11800 {ECO:0000313|EMBL:KUL45847.1};
OS   Streptomyces sp. NRRL F-4489.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1609095 {ECO:0000313|EMBL:KUL45847.1, ECO:0000313|Proteomes:UP000053256};
RN   [1] {ECO:0000313|EMBL:KUL45847.1, ECO:0000313|Proteomes:UP000053256}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL F-4489 {ECO:0000313|EMBL:KUL45847.1,
RC   ECO:0000313|Proteomes:UP000053256};
RA   Millard Andrew;
RL   Submitted (OCT-2015) 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: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}.
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:KUL45847.1}.
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DR   EMBL; LLZI01000113; KUL45847.1; -; Genomic_DNA.
DR   EnsemblBacteria; KUL45847; KUL45847; ADL22_11800.
DR   Proteomes; UP000053256; 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   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:UP000053256};
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:UP000053256}.
FT   DOMAIN      307    435       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      521    590       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     315    322       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   614 AA;  68200 MW;  304B9A498AA4B2DF CRC64;
     MWPRVLDHLL RAEADGLKPK DQDWLKRTQP LALVADTALL AVPNEFAKGV LEGRLAPLIG
     EALSHECGRP IRIAITVDDS SEEPPAQPPA PPQQHGQHPQ TQTQRDGYDG YEARHDARHD
     SRQGYGHQPD DLPTVRPAYP DYDRPRHEPG AWPQHSVTDA VGPREEYGWQ HHTGYPERET
     SSEQWREPYG SGPPAHLQQH PNDYRSQGPD RGAPRPPEGP RPPYEQQRRD LPELPPPGGR
     PGGPGSPLPA PSGAPGPLAA QPAPATGPGE PTARLNPKYL FDTFVIGASN RFAHAAAVAV
     AEAPAKAYNP LFIYGESGLG KTHLLHAIGH YARSLYPGTR VRYVSSEEFT NEFINSIRDG
     KADAFRKRYR DMDILLVDDI QFLASKESTQ EEFFHTFNTL HNANKQIVLS SDRPPKQLVT
     LEDRLRNRFE WGLITDVQPP ELETRIAILR KKAVQEQLNA PPEVLEFIAS RISRNIRELE
     GALIRVTAFA SLNRQPVDLG LTEIVLKDLI PGGEDTAPEI TATAIMASTA DYFGLTVDDL
     CGSSRSRVLV TARQIAMYLC RELTDLSLPK IGAQFGGRDH TTVMHADRKI RALMAERRSI
     YNQVTELTNR IKNG
//
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