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Database: UniProt
Entry: A0A074M257_ERYLO
LinkDB: A0A074M257_ERYLO
Original site: A0A074M257_ERYLO 
ID   A0A074M257_ERYLO        Unreviewed;       486 AA.
AC   A0A074M257;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   05-JUL-2017, entry version 23.
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=EH31_16535 {ECO:0000313|EMBL:KEO88566.1};
OS   Erythrobacter longus.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Erythrobacter.
OX   NCBI_TaxID=1044 {ECO:0000313|EMBL:KEO88566.1, ECO:0000313|Proteomes:UP000027647};
RN   [1] {ECO:0000313|EMBL:KEO88566.1, ECO:0000313|Proteomes:UP000027647}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6997 {ECO:0000313|EMBL:KEO88566.1,
RC   ECO:0000313|Proteomes:UP000027647};
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:KEO88566.1}.
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DR   EMBL; JMIW01000009; KEO88566.1; -; Genomic_DNA.
DR   RefSeq; WP_034962104.1; NZ_JMIW01000009.1.
DR   EnsemblBacteria; KEO88566; KEO88566; EH31_16535.
DR   Proteomes; UP000027647; 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:UP000027647};
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:UP000027647}.
FT   DOMAIN      182    310       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      394    463       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     190    197       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   486 AA;  54353 MW;  D8E55762F56CDC45 CRC64;
     MGYNTDKART TRRKADDDLM EDAEAVNLAA DWADISQGLK KDLGHQLHSQ WIKPIQVGGI
     TKETGTLDLF LPTEFSANWV KDRFHDRLQL AWKIMRSDVR TVNIQVHPGR RQLPELRLDD
     GRRPANDGAS AIAVAAGSIN DSGFTSSVGL DPSLTFQAFI TGEANVLACN AAQRMAATEQ
     PQFSPLYLKA ATGQGKTHLL HAIGHGFLAS HPRARIFYCS AERFMVEFVQ ALKANQMIEF
     KARLRSFDLL LVDDIQFIIG KASAQEELLY TIDALLAEGK RLVFAADRAP QALDGVEPRL
     LSRLSMGLVA DIQAADIELR KKVLVSKLAR FAPLSVPEDV IDFLARTITR NVRELIGGLN
     KLIAYAQLTG QEVSLQLAEE QLTDILSANR RRITIDEIQR TVCQFYRIDR SEMSSKRRAR
     AVVRPRQVAM YLSKVLTPRS YPEIGRKFGG RDHSTVIHAV RLIEDLRTRD ADMDGDVRSL
     LRQLES
//
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