ID V6K1N7_STRNV Unreviewed; 597 AA.
AC V6K1N7;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 28-MAR-2018, entry version 33.
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}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
CC ECO:0000256|SAAS:SAAS00747961}.
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 Gene3D; 3.30.300.180; -; 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; IPR038454; DnaA_N_sf.
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 Coiled coil {ECO:0000256|SAM:Coils};
KW Complete proteome {ECO:0000313|Proteomes:UP000017971};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
KW ECO:0000256|SAAS:SAAS00747973};
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:SAAS00748008};
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}.
FT COILED 573 593 {ECO:0000256|SAM:Coils}.
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
//
