ID   DNAA_CUTAK              Reviewed;         500 AA.
AC   Q6ABL5;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000255|HAMAP-Rule:MF_00377};
GN   Name=dnaA {ECO:0000255|HAMAP-Rule:MF_00377}; OrderedLocusNames=PPA0001;
OS   Cutibacterium acnes (strain DSM 16379 / KPA171202) (Propionibacterium
OS   acnes).
OC   Bacteria; Actinobacteria; Propionibacteriales; Propionibacteriaceae;
OC   Cutibacterium.
OX   NCBI_TaxID=267747;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16379 / KPA171202;
RX   PubMed=15286373; DOI=10.1126/science.1100330;
RA   Brueggemann H., Henne A., Hoster F., Liesegang H., Wiezer A.,
RA   Strittmatter A., Hujer S., Duerre P., Gottschalk G.;
RT   "The complete genome sequence of Propionibacterium acnes, a commensal of
RT   human skin.";
RL   Science 305:671-673(2004).
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; AE017283; AAT81766.1; -; Genomic_DNA.
DR   RefSeq; WP_002515747.1; NZ_CP025935.1.
DR   AlphaFoldDB; Q6ABL5; -.
DR   SMR; Q6ABL5; -.
DR   STRING; 267747.PPA0001; -.
DR   PRIDE; Q6ABL5; -.
DR   EnsemblBacteria; AAT81766; AAT81766; PPA0001.
DR   GeneID; 66619996; -.
DR   KEGG; pac:PPA0001; -.
DR   eggNOG; COG0593; Bacteria.
DR   HOGENOM; CLU_026910_2_0_11; -.
DR   OMA; REFNPLF; -.
DR   Proteomes; UP000000603; 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; 3.30.300.180; -; 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..500
FT                   /note="Chromosomal replication initiator protein DnaA"
FT                   /id="PRO_0000114232"
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         203..210
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00377"
SQ   SEQUENCE   500 AA;  56018 MW;  4656DA79E051F60C CRC64;
     MSDTPFGDAD HPRPAPIHPD AVLPPPMSSQ SADNDPTEAL NEAWTNILTK VSKPNRAWLS
     NTTPVTMHSS TAMVAVPNEF ARDRLESKMR YELEELLSDH FHKAIHLAIT IDPDLELALG
     APDHEDEEEE VPPAQFVPKV TVGVTEPSAR PTTTIDDDEG NRLNPKYTFD SFVIGASNRF
     AHAAAVAVAE APGKSYNPLL IYGGSGLGKT HLLHAIGRYV MSYYDNVKVK YVSTEELTND
     FINAIGTNRT TEFRRSYRDV DVLLVDDIQF LQSKIQTQEE FFHTFNTLHN AQKQIVMTSD
     RPPKLLEALE PRLRSRFEWG LLTDIQPPDL ETRIAILRRK VAAEKITVEP DVLEFIASRI
     QTNIRELEGA LIRVTAFASL NQQPVDISLA EVVLKDLIPE GRETPVTPER IIAETADYFD
     ISADDLLGTS RAQTLVTARQ IAMYLCRELT DLSLPKIGAE FGGKDHTTVM HADRKIRALM
     GEQRQIFNQV SEITNRIKQY