DNAA_RHOE4
ID DNAA_RHOE4 Reviewed; 520 AA.
AC C0ZLE1;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000255|HAMAP-Rule:MF_00377};
GN Name=dnaA {ECO:0000255|HAMAP-Rule:MF_00377}; OrderedLocusNames=RER_00010;
OS Rhodococcus erythropolis (strain PR4 / NBRC 100887).
OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus;
OC Rhodococcus erythropolis group.
OX NCBI_TaxID=234621;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PR4 / NBRC 100887;
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-2005) 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; AP008957; BAH30709.1; -; Genomic_DNA.
DR RefSeq; WP_003942491.1; NC_012490.1.
DR AlphaFoldDB; C0ZLE1; -.
DR SMR; C0ZLE1; -.
DR STRING; 234621.RER_00010; -.
DR EnsemblBacteria; BAH30709; BAH30709; RER_00010.
DR GeneID; 64138034; -.
DR KEGG; rer:RER_00010; -.
DR eggNOG; COG0593; Bacteria.
DR HOGENOM; CLU_026910_2_0_11; -.
DR OMA; REFNPLF; -.
DR Proteomes; UP000002204; 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..520
FT /note="Chromosomal replication initiator protein DnaA"
FT /id="PRO_1000205660"
FT REGION 99..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..149
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 221..228
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00377"
SQ SEQUENCE 520 AA; 58241 MW; 82C55421043B5D6B CRC64;
MNDDPNALAR VWVDVVAELT SDDPGSNLPA LSSKQKAFVR LVRPLTLAQG FALLSVPSPF
AQETIERDLR EPILQALGRH LGGQVEGLGV RIALEDDADA PAEPVEERTG SRQFESVNSS
GAYRRRRFTE GDGEPSDSET AETEEVDDDR EALASVHESW PSYFTKPPAT PSASGSGANS
LNAKYTFDTF VIGSSNRFAH AAAVAIAEAP ARAYNPLFIW GASGLGKTHL LHAAGHYAQR
LFPGMRVKYV STEEFTNDFI NSLRDDRKVA FKRRYRETDV LLVDDIQFIE GKEGIQEEFF
HTFNTLHNAN KQIVVSSDRP PKQLATLEER LRTRFEWGLI TDVQPPELET RIAILSKKAR
MDRLEVPHDV LELIASRIER NIRELEGALI RVTAFASLNR QPLDLTLAEV VLRDLMPDSS
SLEINAATIM AVTAEYFNMS IDDLCGPGKA RPLAQARQIS MYLCRELTDL SLPKIGQTFG
RDHTTVMYAD KKIRKEMTER RKVYDQVQEL TARIKQRSKR