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Database: UniProt
Entry: A0A0U4V4C7_9GAMM
LinkDB: A0A0U4V4C7_9GAMM
Original site: A0A0U4V4C7_9GAMM 
ID   A0A0U4V4C7_9GAMM        Unreviewed;       456 AA.
AC   A0A0U4V4C7;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   18-JUL-2018, entry version 20.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00724181};
GN   Name=dnaA {ECO:0000256|HAMAP-Rule:MF_00377,
GN   ECO:0000313|EMBL:ALZ77792.1};
GN   ORFNames=ATY27_02170 {ECO:0000313|EMBL:ALZ77792.1};
OS   Rheinheimera sp. F8.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC   Chromatiaceae; Rheinheimera.
OX   NCBI_TaxID=1763998 {ECO:0000313|EMBL:ALZ77792.1, ECO:0000313|Proteomes:UP000059499};
RN   [1] {ECO:0000313|Proteomes:UP000059499}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F8 {ECO:0000313|Proteomes:UP000059499};
RA   Schuster A.K., Szewzyk U.;
RT   "Draft genome sequence of Rheinheimera sp. F8, a biofilm-forming
RT   strain which produces large amounts of extracellular DNA.";
RL   Submitted (DEC-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:SAAS00724167}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
CC       ECO:0000256|SAAS:SAAS00747961}.
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; CP013656; ALZ77792.1; -; Genomic_DNA.
DR   EnsemblBacteria; ALZ77792; ALZ77792; ATY27_02170.
DR   Proteomes; UP000059499; 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:SAAS00747950};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000059499};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|SAAS:SAAS00747973};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00747996};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00748008};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00747895};
KW   Reference proteome {ECO:0000313|Proteomes:UP000059499}.
FT   DOMAIN      153    284       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      364    433       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     161    168       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
FT   COILED      315    335       {ECO:0000256|SAM:Coils}.
FT   COILED      433    453       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   456 AA;  51654 MW;  0DFF60B77A75F43A CRC64;
     MYQSVWQNCL EALQSELPAQ QFSMWIRPLQ ADSSHDALTL YAPNRFVLDW VRDKYLNRIN
     ELIHDYCGDH SPRLRFEVGS SQKAPKVSPV TTSRIAPVAA APAASAAVAE PAPKTIVRSN
     VRANYTFENF VEGKSNQLAR AAASQVADNP GTAYNPLFLY GGTGLGKTHL LHAVGNGILA
     KKPDAKVIYM HSERFVQDMV KALQNNAIEE FKRYYRSVDA LLIDDIQFFA KKDRSQEEFF
     HTFNALLEGN QQIILTSDRY PKEIDGVEER LKSRFGWGLT IAIEPPELET RVAILMRKAQ
     ENNIRLPEEV AFFVAKRLRS NVRELEGALN RITANANFTG RPITIDFVRE SLRDLLALQD
     KLVTIENIQK TVAEYYKIRV ADLLSKRRSR SVARPRQMAM ALSKELTNHS LPEIGDAFGG
     RDHTTVLHAC RKIESLKEET HEIKEDFQNL IRTLSS
//
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