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Database: UniProt
Entry: A0A0C1VR94_9ACTN
LinkDB: A0A0C1VR94_9ACTN
Original site: A0A0C1VR94_9ACTN 
ID   A0A0C1VR94_9ACTN        Unreviewed;       575 AA.
AC   A0A0C1VR94;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   05-JUL-2017, entry version 22.
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:KIF06608.1};
GN   ORFNames=PL81_06610 {ECO:0000313|EMBL:KIF06608.1};
OS   Streptomyces sp. RSD-27.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1571774 {ECO:0000313|EMBL:KIF06608.1, ECO:0000313|Proteomes:UP000031573};
RN   [1] {ECO:0000313|EMBL:KIF06608.1, ECO:0000313|Proteomes:UP000031573}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RSD-27 {ECO:0000313|EMBL:KIF06608.1,
RC   ECO:0000313|Proteomes:UP000031573};
RA   Debnath R., Saikia R.;
RT   "Streptomyces sp. RSD-27 isolated from Se La Pass, Arunachal Pradesh,
RT   India.";
RL   Submitted (DEC-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: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}.
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:KIF06608.1}.
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DR   EMBL; JWZS01000400; KIF06608.1; -; Genomic_DNA.
DR   RefSeq; WP_042810515.1; NZ_JWZS01000400.1.
DR   EnsemblBacteria; KIF06608; KIF06608; PL81_06610.
DR   Proteomes; UP000031573; 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; 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:UP000031573};
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:UP000031573}.
FT   DOMAIN      268    396       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      482    551       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     276    283       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   575 AA;  64126 MW;  942B5547E4D7D1AD CRC64;
     MLEKLLGEGQ QGIEPKDKQW VERCQPLALV ADTALLAVPN EWGKRVLEGR LAPLISDALS
     RECGRPIRIA ITVDDSAGEP APPAPPAPSR EAYEPYGGQR PGPGEEQLPT ARPAYPEYQQ
     PRPEPGAWPR GGQDDYGWQQ QRFPERDPYA SPQPGYLQQP EAGGYDQGGY EQQKYEPQQY
     EQQKYEQQKY EQQPYDQPSY EQPAPRPAPG RPTPAPPPSA PSGGSTSGPL EPTARLNPKY
     LFDTFVIGAS NRFAHAAAVA VAEAPAKAYN PLFIYGESGL GKTHLLHAIG HYARSLYPGT
     RVRYVSSEEF TNEFINSIRD GKGDAFRKRY REMDILLVDD IQFLASKEST QEEFFHTFNT
     LHNANKQIVL SSDRPPKQLV TLEDRLRNRF EWGLITDVQP PELETRIAIL RKKAVQEQLN
     APPEVLEFIA SRISRNIREL EGALIRVTAF ASLNRQPVDL GLTEDVLKNL IPGGEDSAPE
     ITAADIMAAT ADYFGLTVDD LCGSSRSRVL VTARQIAMYL CRELTDLSLP KIGAQFGGRD
     HTTVMHADRK IRALMAERRS IYNQVTELTN RIKNG
//
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