DNAA_STRCO
ID DNAA_STRCO Reviewed; 656 AA.
AC P27902; Q9KXX4;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Chromosomal replication initiator protein DnaA;
GN Name=dnaA; OrderedLocusNames=SCO3879; ORFNames=SCH18.16c;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=A3(2) / NRRL B-16638;
RX PubMed=1577691; DOI=10.1128/jb.174.10.3220-3226.1992;
RA Calcutt M.J., Schmidt F.J.;
RT "Conserved gene arrangement in the origin region of the Streptomyces
RT coelicolor chromosome.";
RL J. Bacteriol. 174:3220-3226(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
CC -!- FUNCTION: Plays an important role in the initiation and regulation of
CC chromosomal replication. Binds to the origin of replication; it binds
CC specifically double-stranded DNA at a 9 bp consensus (dnaA box): 5'-
CC TTATC[CA]A[CA]A-3'. DnaA binds to ATP and to acidic phospholipids (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DnaA family. {ECO:0000305}.
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DR EMBL; AF187159; AAA26734.1; -; Genomic_DNA.
DR EMBL; AL939118; CAD55464.1; -; Genomic_DNA.
DR PIR; A41870; A41870.
DR RefSeq; NP_733620.1; NC_003888.3.
DR RefSeq; WP_011029287.1; NZ_VNID01000003.1.
DR AlphaFoldDB; P27902; -.
DR SMR; P27902; -.
DR STRING; 100226.SCO3879; -.
DR PRIDE; P27902; -.
DR GeneID; 1099315; -.
DR KEGG; sco:SCO3879; -.
DR PATRIC; fig|100226.15.peg.3952; -.
DR eggNOG; COG0593; Bacteria.
DR HOGENOM; CLU_026910_2_0_11; -.
DR InParanoid; P27902; -.
DR OMA; FPERDPY; -.
DR PhylomeDB; P27902; -.
DR Proteomes; UP000001973; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003688; F:DNA replication origin binding; IBA:GO_Central.
DR GO; GO:0006260; P:DNA replication; IBA:GO_Central.
DR GO; GO:0006270; P:DNA replication initiation; IBA:GO_Central.
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 Gene3D; 3.40.50.300; -; 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; Cytoplasm; DNA replication; DNA-binding; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..656
FT /note="Chromosomal replication initiator protein DnaA"
FT /id="PRO_0000114271"
FT REGION 91..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..141
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..220
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..271
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..306
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 357..364
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 656 AA; 73183 MW; 6C1D5C0193D3C92B CRC64;
MADVPADLAA VWPRVLEQLL GEGRGQGVES KDEHWIRRCQ PLALVADTAL LAVPNEFAKG
VLEGRLAPIV SETLSRECGR PIRIAITVDD TAGEPAGPAP QAPQSPPSRP QHRYEEPELP
APGQGGREEY RDRDEYEGYG RNRADQLPTA RPAYPQEYQR PEPGSWPRPA QQDDYGWQQQ
RLGFPERDPY ASPNQEPYGQ EPPPPYSHEN RTSYQQDYRP QPPERPSYDA QRGDYEQARG
EYEQPRGDYD KPRGDYDQQR GDYDQRGPRR DLPEPPPGSG HVHRGGPVGP GPATGAPGPL
AAQPAPATGP GEPTARLNPK YLFDTFVIGA SNRFAHAAAV AVAEAPAKAY NPLFIYGESG
LGKTHLLHAI GHYARSLYPG TRVRYVSSEE FTNEFINSIR DGKGDSFRKR YREMDILLVD
DIQFLADKES TQEEFFHTFN TLHNANKQIV LSSDRPPKQL VTLEDRLRNR FEWGLITDVQ
PPELETRIAI LRKKAVQEQL NAPPEVLEFI ASRISRNIRE LEGALIRVTA FASLNRQPVD
LGLTEIVLKD LIPGGEDSAP EITSTAIMGA TADYFGLTVE DLCGTSRGRA LVTARQIAMY
LCRELTDLSL PKIGALFGGR DHTTVMHADR KIRNLMAERR SIYNQVTELT NRIKNG
