ID   DNAA_CORA7              Reviewed;         546 AA.
AC   C3PE72;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000255|HAMAP-Rule:MF_00377};
GN   Name=dnaA {ECO:0000255|HAMAP-Rule:MF_00377}; OrderedLocusNames=cauri_0001;
OS   Corynebacterium aurimucosum (strain ATCC 700975 / DSM 44827 / CIP 107346 /
OS   CN-1) (Corynebacterium nigricans).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=548476;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700975 / DSM 44827 / CIP 107346 / CN-1;
RX   PubMed=20137072; DOI=10.1186/1471-2164-11-91;
RA   Trost E., Gotker S., Schneider J., Schneiker-Bekel S., Szczepanowski R.,
RA   Tilker A., Viehoever P., Arnold W., Bekel T., Blom J., Gartemann K.H.,
RA   Linke B., Goesmann A., Puhler A., Shukla S.K., Tauch A.;
RT   "Complete genome sequence and lifestyle of black-pigmented Corynebacterium
RT   aurimucosum ATCC 700975 (formerly C. nigricans CN-1) isolated from a
RT   vaginal swab of a woman with spontaneous abortion.";
RL   BMC Genomics 11:91-91(2010).
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; CP001601; ACP31600.1; -; Genomic_DNA.
DR   RefSeq; WP_010188097.1; NZ_ACLH01000030.1.
DR   AlphaFoldDB; C3PE72; -.
DR   SMR; C3PE72; -.
DR   STRING; 548476.cauri_0001; -.
DR   EnsemblBacteria; ACP31600; ACP31600; cauri_0001.
DR   GeneID; 31922627; -.
DR   KEGG; car:cauri_0001; -.
DR   eggNOG; COG0593; Bacteria.
DR   HOGENOM; CLU_026910_2_1_11; -.
DR   OMA; REFNPLF; -.
DR   OrthoDB; 219876at2; -.
DR   Proteomes; UP000002077; 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;
KW   Reference proteome.
FT   CHAIN           1..546
FT                   /note="Chromosomal replication initiator protein DnaA"
FT                   /id="PRO_1000189792"
FT   REGION          96..209
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        98..113
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        121..151
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        168..183
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        191..209
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         246..253
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00377"
SQ   SEQUENCE   546 AA;  60676 MW;  3A6CC0B5722F2AD3 CRC64;
     MSDPQAALRA SWKAVVSDLL AQSEQPNSDV PNFSHSQRLN LQLVEPIMIG DGYALIAAPH
     ENAKTVIETE LGEYITRALS QHMGRPCSLA VTIAAPPQPA PQEEPPAPAP QRPIQTEAPE
     HGMGHQTQAF QQPTQSTQPA PASQPETPNH HQPRSWEAAH SPASLDELAQ HYSEQQSTAP
     SGYPEATGAR IPREEPAHNP NREKSLNPKH TFENFVIGSS NRFANGAAVA VAENPARAYN
     PLFIWGGSGL GKTHLLHAAG NYAQVLHPGL RVKYVSSEEF TNDYINSLRD DRQESFKRRY
     RNLDILMVDD IQFLEGKEST QEEFFHTFNA LHQANKQIIL SSDRPPKQLT TLEDRLRTRF
     EGGLITDIQP PDLETRIAIL MKKASADGTD VDRSVLELIA SRFESSIREL EGALIRVSAY
     SSLVNEPISL EMAEIALHDL APDSADRQIT AAAIIEVTAD YFNIDVDTLR GSGKKRAVAH
     ARQLAMYLCR ELTELSLPKI GDQFGGKDHT TVIYADRKIR KEMTENRNTY DEIQALTQRV
     KNHNQR