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Database: UniProt
Entry: A0A0G3GL67_9CORY
LinkDB: A0A0G3GL67_9CORY
Original site: A0A0G3GL67_9CORY 
ID   A0A0G3GL67_9CORY        Unreviewed;       435 AA.
AC   A0A0G3GL67;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   27-SEP-2017, entry version 17.
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:AKK01899.1};
GN   ORFNames=CEPID_00005 {ECO:0000313|EMBL:AKK01899.1};
OS   Corynebacterium epidermidicanis.
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=1050174 {ECO:0000313|EMBL:AKK01899.1, ECO:0000313|Proteomes:UP000035368};
RN   [1] {ECO:0000313|EMBL:AKK01899.1, ECO:0000313|Proteomes:UP000035368}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45586 {ECO:0000313|EMBL:AKK01899.1,
RC   ECO:0000313|Proteomes:UP000035368};
RA   Ruckert C., Albersmeier A., Winkler A., Tauch A.;
RT   "Complete genome sequence of Corynebacterium epidermidicanis DSM
RT   45586, isolated from the skin of a dog suffering from pruritus.";
RL   Submitted (MAY-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:SAAS00731907}.
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}.
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DR   EMBL; CP011541; AKK01899.1; -; Genomic_DNA.
DR   EnsemblBacteria; AKK01899; AKK01899; CEPID_00005.
DR   KEGG; cei:CEPID_00005; -.
DR   PATRIC; fig|1050174.4.peg.1; -.
DR   KO; K02313; -.
DR   Proteomes; UP000035368; 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:SF12; PTHR30050:SF12; 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:SAAS00731922};
KW   Complete proteome {ECO:0000313|Proteomes:UP000035368};
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:UP000035368}.
FT   DOMAIN      127    261       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      339    408       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     135    142       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   435 AA;  48759 MW;  0BBBBCADFF32E903 CRC64;
     MAKEVVENEL AEPIEQVLQS MLGAHTRLAV SVAPTETLPA ASSPQPVVEK LPDDWAEVHI
     PVAEEPEPPA PVTPVAPEPQ RIAREQRNPR SDVTLNPRYT FENFVIGGSN RFPHAAAVAV
     AESLATAYNP LFIWGGSGLG KTHLLHAIGN YAQVLQPGLR VRYVSSEEFT NDYINSVRDD
     RQEKFKQRYR NLDILMVDDI QFLEGKEGTQ EEFFHTFNAL HQADKQIVLS SDRSPNDLSI
     LTDRLLTRFK AGLIVDIQPP DLETRIAILS KKAKLDGTVV QHDVLELIAS RFDTSIRELE
     GALIRVIAYS SLIREPLDRR TAEIALQDIM PSSEDPEISA TSIIQQTAEY FELNEDALTG
     TGKTRAVAHA RQLAMYLCRE LTDLSLPRIG QFFGGKDHTT VMYAVRKINR EINEKRDTYD
     QIQAITSRIK SKNRS
//
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