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Database: UniProt
Entry: A0A0N1KFK1_9ACTN
LinkDB: A0A0N1KFK1_9ACTN
Original site: A0A0N1KFK1_9ACTN 
ID   A0A0N1KFK1_9ACTN        Unreviewed;       672 AA.
AC   A0A0N1KFK1;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   25-OCT-2017, entry version 16.
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=ADL27_01105 {ECO:0000313|EMBL:KPC96953.1};
OS   Streptomyces sp. NRRL F-6602.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1609099 {ECO:0000313|EMBL:KPC96953.1, ECO:0000313|Proteomes:UP000037856};
RN   [1] {ECO:0000313|EMBL:KPC96953.1, ECO:0000313|Proteomes:UP000037856}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL F-6602 {ECO:0000313|EMBL:KPC96953.1,
RC   ECO:0000313|Proteomes:UP000037856};
RA   Noorani M.;
RL   Submitted (JUL-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}.
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:KPC96953.1}.
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DR   EMBL; LGKH01000001; KPC96953.1; -; Genomic_DNA.
DR   EnsemblBacteria; KPC96953; KPC96953; ADL27_01105.
DR   PATRIC; fig|1609099.3.peg.235; -.
DR   Proteomes; UP000037856; Unassembled WGS sequence.
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:UP000037856};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037856}.
FT   DOMAIN      365    493       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      579    648       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     373    380       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   672 AA;  75235 MW;  430BFAA34CCAB680 CRC64;
     MADLPADLAA VWPRVLEQLL REGQGVEAKD QRWLRDCQPL VLVSGTALLG VPNEYAKGVL
     EGRLAPLITE ALSRECQQPI RLAITVTGPA PEAPTPPAPQ TPSIPSPTPA PEQQHQQHQP
     PQREGSYEVG YDTYPPRETY ESYEQRGDHG GPPHGSGPSP QQNPQSPREP QGQQQGQPER
     YEQPDRFEQY ENREMPGARS AYQDYAQSPL PAPGPGSWQQ QQQQRRDPYA PQHQQRHQPY
     DHRQQGGYEQ QSPYDQQPYE QQGYDQQNYE QQSYEPYEQQ HQQRPRPQVP PQGRPPAPHY
     DSPSQLPAPS GAPGPLAAQP APATGPGEPT ARLNPKYLFD TFVIGASNRF AHAAAVAVAE
     APAKAYNPLF IYGESGLGKT HLLHAIGHYA RSLYPGTRVR YVSSEEFTNE FINSIRDGKA
     DAFRKRYRDM DILLVDDVQF LADKESTQEE FFHTFNTLHN ANKQIVLSSD RPPKALETLE
     DRLRNRFEWG LITDVQPPEL ETRIAILRKK AVQEQLNAPP EVLEFIASRI SRNIRELEGA
     LIRVTAFASL NRQPVDLGLT EIVLKDLIPG GEDATPEITA PAIMAATADY FGLTVDDLCG
     SSRSRVLVTA RQIAMYLCRE LTDLSLPKIG GQFGGRDHTT VMHADRKIRA LMAERRSIYN
     QVTELTNRIK NG
//
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