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Database: UniProt
Entry: A0A0N9NDL1_9ACTN
LinkDB: A0A0N9NDL1_9ACTN
Original site: A0A0N9NDL1_9ACTN 
ID   A0A0N9NDL1_9ACTN        Unreviewed;       547 AA.
AC   A0A0N9NDL1;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   25-OCT-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   ORFNames=ACH46_00005 {ECO:0000313|EMBL:ALG83188.1};
OS   Gordonia sp. QH-11.
OC   Bacteria; Actinobacteria; Corynebacteriales; Gordoniaceae; Gordonia.
OX   NCBI_TaxID=1136941 {ECO:0000313|EMBL:ALG83188.1, ECO:0000313|Proteomes:UP000063789};
RN   [1] {ECO:0000313|EMBL:ALG83188.1, ECO:0000313|Proteomes:UP000063789}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=QH-11 {ECO:0000313|EMBL:ALG83188.1,
RC   ECO:0000313|Proteomes:UP000063789};
RA   Jin D., Kong X., Bai Z.;
RT   "Complete genome sequence and metabolic analysis of phthalate
RT   degradation pathway in Gordonia sp. QH-11.";
RL   Submitted (JUN-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}.
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DR   EMBL; CP011853; ALG83188.1; -; Genomic_DNA.
DR   RefSeq; WP_062391141.1; NZ_CP011853.1.
DR   EnsemblBacteria; ALG83188; ALG83188; ACH46_00005.
DR   KEGG; goq:ACH46_00005; -.
DR   KO; K02313; -.
DR   Proteomes; UP000063789; 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: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:UP000063789};
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}.
FT   DOMAIN      240    368       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      452    520       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     248    255       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   547 AA;  61036 MW;  3344A3F1E1F42376 CRC64;
     MAGDRENFSN IWNAVVSDLA SGADDAAAEP LTRQQKAWLS LVRPLTMTEG FALLAVPSTV
     VQEQIERNLR ERVSHALSRH VGQSIDIAVR VSEPEEVSGE PGPGSAPSGG VHPQPRVTGA
     TQVTPETYGV PSAYDASPYD SAATAGHIPT PTYPPSPAIP SDEQLAALNY QQQHYPSAPP
     QRPVEPREWS SYFEHRETSA PDNSTTSLHP KYTFDTFVIG ASNRFAHASA VAVAENPARA
     YNPMFIWGES GLGKTHLLHA AGHYAQRLFP GMRVKYVSTE EFTNDFINSL RDDRRVAFKR
     RYRDIDMLLI DDIQFLEGKE GIQEEFFHTF NTLHNANKQI VVSSDRPPKQ LATLEDRLRT
     RFEWGLITDV QPPDLETRIA ILRKKAQMDK MDVPDSVLEL IASKIERNIR ELEGALIRVN
     AFASLNQTQM DASMAEVVMK ALIPDSGPMD ISAASIVAVT ADFYDLSVED LCGPSKVRAL
     TLPRQISMYL CRELTDLSLP KIGETFDRDH STVIHADRKI RKQMHENRNI YDQVQELTAK
     IKQRANR
//
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