DNAA_RHOOB
ID DNAA_RHOOB Reviewed; 528 AA.
AC C1B7S7;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000255|HAMAP-Rule:MF_00377};
GN Name=dnaA {ECO:0000255|HAMAP-Rule:MF_00377}; OrderedLocusNames=ROP_34830;
OS Rhodococcus opacus (strain B4).
OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX NCBI_TaxID=632772;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B4;
RA Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT "Comparison of the complete genome sequences of Rhodococcus erythropolis
RT PR4 and Rhodococcus opacus B4.";
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
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.
CC {ECO:0000255|HAMAP-Rule:MF_00377}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00377}.
CC -!- SIMILARITY: Belongs to the DnaA family. {ECO:0000255|HAMAP-
CC Rule:MF_00377}.
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DR EMBL; AP011115; BAH51730.1; -; Genomic_DNA.
DR RefSeq; WP_012690676.1; NC_012522.1.
DR AlphaFoldDB; C1B7S7; -.
DR SMR; C1B7S7; -.
DR STRING; 632772.ROP_34830; -.
DR EnsemblBacteria; BAH51730; BAH51730; ROP_34830.
DR KEGG; rop:ROP_34830; -.
DR PATRIC; fig|632772.20.peg.3648; -.
DR HOGENOM; CLU_026910_2_0_11; -.
DR OMA; REFNPLF; -.
DR OrthoDB; 219876at2; -.
DR Proteomes; UP000002212; 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; 3.40.50.300; -; 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; 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..528
FT /note="Chromosomal replication initiator protein DnaA"
FT /id="PRO_1000189806"
FT REGION 93..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..119
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 229..236
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00377"
SQ SEQUENCE 528 AA; 59121 MW; 03ACB38986D9DA01 CRC64;
MNDDPNALAR IWIDVVADLT SDSPGGDLPP LTRGQKAWLA LVKPLTLAQG FALLSVPSPF
AQEAIERDLR EPILHALGRH LGEQVEGLGV RIAAPVDDEP ESEAPSRERR PDPEPVHTPR
HLEPSVTSSG TFRRRRFGSG DDQPYSDTTD FEEVDDDSEA LASVHESWPS YFTKPPAGPA
PAATGGNSLN AKYTFDTFVI GSSNRFAHAA AVAIAEAPAR AYNPLFIWGA SGLGKTHLLH
AAGHYAQRLF PGMRVKYVST EEFTNDFINS LRDDRKVAFK RRYRETDVLL VDDIQFIEGK
EGIQEEFFHT FNTLHNANKQ IVVSSDRPPK QLATLEERLR TRFEWGLITD VQPPELETRI
AILSKKARMD RLEVPDDVLE LIASRIERNI RELEGALIRV TAFASLNRQP LDLTLAEVVL
RDLMPDSSSL EINAATIMAV TAEYFNMSID DLCGPGKARP LASARQISMY LCRELTDLSL
PKIGQTFGRD HTTVMYADKK IRKEMTERRK VYDQVQELTA RIKQRSKR