DNAA_STRRE
ID DNAA_STRRE Reviewed; 643 AA.
AC Q9ZH76;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Chromosomal replication initiator protein DnaA;
GN Name=dnaA;
OS Streptomyces reticuli.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=1926;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Tu45;
RX PubMed=10095766; DOI=10.1046/j.1432-1327.1999.00168.x;
RA Majka J., Jakimowicz D., Messer W., Schrempf H., Lisowski M.,
RA Zakrzewska-Czerwinska J.;
RT "Interactions of the Streptomyces lividans initiator protein DnaA with its
RT target.";
RL Eur. J. Biochem. 260:325-335(1999).
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; AF071023; AAD08806.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9ZH76; -.
DR SMR; Q9ZH76; -.
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 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.
FT CHAIN 1..643
FT /note="Chromosomal replication initiator protein DnaA"
FT /id="PRO_0000114279"
FT REGION 87..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..268
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..294
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 344..351
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 643 AA; 71318 MW; DB9E173DF24758B5 CRC64;
MADVPADLAA VWPRVLEQLL GEGRGQGVEA KDEHWIRRCQ PLALVADTAL LAVPNEFAKG
VLEGRLAPIV SETLSRECGR PIRIAITVDD SAGEPPPAAP PAQQTPKPRY EEPELPSGPY
EGYGRHRGGA DQLPGTEPRP EQLPSARPDQ LPTVRPAYPS EYHRPEPGAW PRPAQDEYGW
QQPRLGFPER DPYASPSSQD AYGSPSQDYR PQGMDRPPYE QQRGDYDTPR AEYEPARPDY
DSARPDYESA RPEYDQRDPV RRELPEPPAH RGGPGADMPS AGAPGPPAAQ PAPASGPGEP
TARLNPKYLF DTFVIGASNR FAHAAAVAVA EAPAKAYNPL FIYGESGLGK THLLHAIGHY
ARSLYPGTRV RYVSSEEFTN EFINSIRDGK GDSFRKRYRE MDILLVDDIQ FLADKESTQE
EFFHTFNTLH NANKQIVLSS DRPPKQLVTL EDRLRNRFEW GLITDVQPPE LETRIAILRK
KAVQEQLNAP PEVLEFIASR ISRNIRELEG ALIRVTAFAS LNRQPVDLGL TEIVLKDLIP
GGEDSTPEIT ATAIMAATAD YFGLTVDDLC GSSRGRQLVT ARQIAMYLCR ELTDLSLPKI
GAQFGGRDHT TVMHADRKIR ALMAERRSIY NQVTELTNRI KNG