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Database: UniProt
Entry: A0A074MKA8_9SPHN
LinkDB: A0A074MKA8_9SPHN
Original site: A0A074MKA8_9SPHN 
ID   A0A074MKA8_9SPHN        Unreviewed;       468 AA.
AC   A0A074MKA8;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   05-JUL-2017, entry version 21.
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   ORFNames=EH32_00745 {ECO:0000313|EMBL:KEO92303.1};
OS   Erythrobacter litoralis.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Erythrobacter.
OX   NCBI_TaxID=39960 {ECO:0000313|EMBL:KEO92303.1, ECO:0000313|Proteomes:UP000027866};
RN   [1] {ECO:0000313|EMBL:KEO92303.1, ECO:0000313|Proteomes:UP000027866}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 8509 {ECO:0000313|EMBL:KEO92303.1,
RC   ECO:0000313|Proteomes:UP000027866};
RA   Zheng Q.;
RT   "A comprehensive comparison of genomes of Erythrobacter spp.
RT   Strains.";
RL   Submitted (APR-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:SAAS00724167}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
CC       ECO:0000256|SAAS:SAAS00756131}.
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:KEO92303.1}.
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DR   EMBL; JMIX01000010; KEO92303.1; -; Genomic_DNA.
DR   EnsemblBacteria; KEO92303; KEO92303; EH32_00745.
DR   Proteomes; UP000027866; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003688; F:DNA replication origin binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006270; P:DNA replication initiation; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006275; P:regulation of DNA replication; IEA:UniProtKB-HAMAP.
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; IPR024633; DnaA_N_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR010921; Trp_repressor/repl_initiator.
DR   PANTHER; PTHR30050:SF12; PTHR30050:SF12; 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:SAAS00731922};
KW   Complete proteome {ECO:0000313|Proteomes:UP000027866};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|SAAS:SAAS00756112};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU004227, ECO:0000256|SAAS:SAAS00731887};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00756124};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00731897};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027866}.
FT   DOMAIN      164    292       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      376    445       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     172    179       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   468 AA;  52358 MW;  DFDDAE4D5B4B4D68 CRC64;
     MMEDAEAVNL AADWADISQG LRKDLGHQLH SQWIRPIQLG GIDKDTGTLD LYLPTEFAAN
     WVNDRFRDRL QLAWKIARSE VRQVRVQVHP GRRQLPELHL EDSRRAANDG ASAIAVAAGT
     IGDSGFTGSV GLDPSLTFAA FVTGEANVLA CNAAQRMAAT EKPQFSPLYL KAATGQGKTH
     LLHAIGHAYL QAHPRARIFY CSAERFMVEF VQALKANQMI EFKGRLRSFD LLLVDDIQFI
     IGKASAQEEL LYTIDALLAE GKRLVFAADR APQALDGVEP RLLSRLSMGL VADIQAADIE
     LRKKILESKL SRFAPLSVPE DVIDFLARTI TRNIRELVGG LNKLIAYAQL TGQEVSLQLA
     EEQLTDILSA NRRRITIDEI QRTVCQFYRI DRSEMSSKRR ARAVVRPRQV AMYLSKVLTP
     RSYPEIGRKF GGRDHSTVIH AVRLIEDLRQ RDADMDGDVR SLLRQLES
//
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