ID   DNAA_CORJK              Reviewed;         583 AA.
AC   Q4JYF7;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000255|HAMAP-Rule:MF_00377};
GN   Name=dnaA {ECO:0000255|HAMAP-Rule:MF_00377}; OrderedLocusNames=jk0001;
OS   Corynebacterium jeikeium (strain K411).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=306537;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K411;
RX   PubMed=15968079; DOI=10.1128/jb.187.13.4671-4682.2005;
RA   Tauch A., Kaiser O., Hain T., Goesmann A., Weisshaar B., Albersmeier A.,
RA   Bekel T., Bischoff N., Brune I., Chakraborty T., Kalinowski J., Meyer F.,
RA   Rupp O., Schneiker S., Viehoever P., Puehler A.;
RT   "Complete genome sequence and analysis of the multiresistant nosocomial
RT   pathogen Corynebacterium jeikeium K411, a lipid-requiring bacterium of the
RT   human skin flora.";
RL   J. Bacteriol. 187:4671-4682(2005).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CR931997; CAI36150.1; -; Genomic_DNA.
DR   RefSeq; WP_011272776.1; NC_007164.1.
DR   AlphaFoldDB; Q4JYF7; -.
DR   SMR; Q4JYF7; -.
DR   STRING; 306537.jk0001; -.
DR   EnsemblBacteria; CAI36150; CAI36150; jk0001.
DR   GeneID; 56648554; -.
DR   KEGG; cjk:jk0001; -.
DR   PATRIC; fig|306537.10.peg.11; -.
DR   eggNOG; COG0593; Bacteria.
DR   HOGENOM; CLU_026910_2_0_11; -.
DR   OrthoDB; 219876at2; -.
DR   Proteomes; UP000000545; 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..583
FT                   /note="Chromosomal replication initiator protein DnaA"
FT                   /id="PRO_1000060010"
FT   REGION          151..239
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        170..185
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        191..209
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        225..239
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         283..290
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00377"
SQ   SEQUENCE   583 AA;  65014 MW;  AF52C696859E3493 CRC64;
     MSNSNFSIEE HFPDMWDAIM HDWLADSSSA NPDPDLPVIS PKQRSLLRKV TPVGLMGRIV
     VLETPNKWTK ESIEKDLIDP IKHVLKTRLD LSVSLAITST NGESENRAEA ADDSHTRVDA
     VGDTHEGASQ KGSVATADDL SMSQVEELVN KAEQRDGASQ AGVSSAAETA EEAARRREHD
     ADELAGQYSA TENHIDPNPS PTPTRWTNKE TAHRPAPRHT SPHTPSPQPS SSFNDGLDGE
     SLLNKNYTFE NFVVGSSNNF AAAACRAVAE APAKAYNPLF IWGESGLGKT HLLHAIGHYA
     KELQPNMRVK YVSSEELTND FINSIANDTR ESFKRRYRNL DMLIVDDIQF LQNKESTQEE
     FFHTFNALHQ ANKQIVLSSD RPPRQLTTLE DRLRTRFEGG LITDVQTPDL ETRIAILTKK
     AESDNVQLPE DVKVLIASRY EKSIRELDGA LIRVTAYCAL SHEPLTVETA EIALRDISPA
     DQDVEIVPQH VIEVVANYFN LTTDELVGKG RAKKFVQARQ IAMYLCRELT DLSLPKLGSA
     FGGRDHTTVM YAERRVRESL SENKKVFDQV QELTQKIKSH ARD