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Database: UniProt
Entry: V6K1N7_STRNV
LinkDB: V6K1N7_STRNV
Original site: V6K1N7_STRNV 
ID   V6K1N7_STRNV            Unreviewed;       597 AA.
AC   V6K1N7;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   25-OCT-2017, entry version 30.
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:EST26042.1};
GN   ORFNames=M877_20245 {ECO:0000313|EMBL:EST26042.1};
OS   Streptomyces niveus NCIMB 11891.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1352941 {ECO:0000313|EMBL:EST26042.1, ECO:0000313|Proteomes:UP000017971};
RN   [1] {ECO:0000313|EMBL:EST26042.1, ECO:0000313|Proteomes:UP000017971}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCIMB 11891 {ECO:0000313|EMBL:EST26042.1};
RX   PubMed=24407644;
RA   Flinspach K., Ruckert C., Kalinowski J., Heide L., Apel A.K.;
RT   "Draft Genome Sequence of Streptomyces niveus NCIMB 11891, Producer of
RT   the Aminocoumarin Antibiotic Novobiocin.";
RL   Genome Announc. 2:e01146-13(2014).
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:EST26042.1}.
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DR   EMBL; AWQW01000140; EST26042.1; -; Genomic_DNA.
DR   EnsemblBacteria; EST26042; EST26042; M877_20245.
DR   PATRIC; fig|1352941.4.peg.4131; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000017971; 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:UP000017971};
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:UP000017971}.
FT   DOMAIN      290    418       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      504    573       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     298    305       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   597 AA;  67325 MW;  BF4F7449C3D67C60 CRC64;
     MLEQLLREGQ QGVEPKDKQW IERCQPLALV ADTALLAVPN EWGKRVLEGR LAPLISETLS
     HECGRPIRIA ITVDDSAGEP VPPLPQQSRY QNSQHDDGRD GRDSRDLRDS RDSRHDDPRP
     DDSRHDDMRP DGGYHPYGRR PSDDDSMPTA RPAYPDYQQQ RPDPGAWPRT QEDLSWQQQR
     LGGFQDRDPY ATARPQQPQH DYRPPQPQES RPYDQQQRPE RHDLDPQQSR HGGRGGATGP
     LGAQASPPPG PGEHHARLNP KYLFDTFVIG ASNRFAHAAA VAVAEAPAKA YNPLFIYGES
     GLGKTHLLHA IGHYARSLYP GTRVRYVSSE EFTNEFINSI RDGKGDTFRK RYRDVDILLV
     DDIQFLASKE STQEEFFHTF NTLHNANKQI VLSSDRPPKQ LITLEDRLRN RFEWGLTTDV
     QPPELETRIA ILRKKAVQEQ LNAPPEVLEF IASRISRNIR ELEGALIRVT AFASLNRQPV
     DLGLTEIVLK DLIPGGEDSA PEITAGAIMA ATADYFGLTV EDLCGSSRSR VLVTARQIAM
     YLCRELTDLS LPKIGAQFGN RDHTTVMHAD RKIRALMAER RSIYNQVTEL TNRIKNG
//
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