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Database: UniProt
Entry: Q18C85_PEPD6
LinkDB: Q18C85_PEPD6
Original site: Q18C85_PEPD6 
ID   Q18C85_PEPD6            Unreviewed;       439 AA.
AC   Q18C85;
DT   25-JUL-2006, integrated into UniProtKB/TrEMBL.
DT   25-JUL-2006, sequence version 1.
DT   05-JUL-2017, entry version 95.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00724181};
GN   Name=dnaA {ECO:0000256|HAMAP-Rule:MF_00377,
GN   ECO:0000313|EMBL:CAJ66815.1};
GN   OrderedLocusNames=CD630_00010 {ECO:0000313|EMBL:CAJ66815.1};
OS   Peptoclostridium difficile (strain 630) (Clostridium difficile).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales;
OC   Peptostreptococcaceae; Clostridioides.
OX   NCBI_TaxID=272563 {ECO:0000313|EMBL:CAJ66815.1, ECO:0000313|Proteomes:UP000001978};
RN   [1] {ECO:0000313|EMBL:CAJ66815.1, ECO:0000313|Proteomes:UP000001978}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=630 {ECO:0000313|EMBL:CAJ66815.1,
RC   ECO:0000313|Proteomes:UP000001978};
RX   PubMed=16804543; DOI=10.1038/ng1830;
RA   Sebaihia M., Wren B.W., Mullany P., Fairweather N.F., Minton N.,
RA   Stabler R., Thomson N.R., Roberts A.P., Cerdeno-Tarraga A.M., Wang H.,
RA   Holden M.T.G., Wright A., Churcher C., Quail M.A., Baker S., Bason N.,
RA   Brooks K., Chillingworth T., Cronin A., Davis P., Dowd L., Fraser A.,
RA   Feltwell T., Hance Z., Holroyd S., Jagels K., Moule S., Mungall K.,
RA   Price C., Rabbinowitsch R., Sharp S., Simmonds M., Steven K.,
RA   Unwin L., Whithead S., Dupuy B., Dougan G., Barrell B.and.Parkhill.J.;
RT   "The multidrug-resistant human pathogen Clostridium difficile has a
RT   highly mobile, mosaic genome.";
RL   Nat. Genet. 38:779-786(2006).
CC   -!- FUNCTION: Plays an important role in the initiation and regulation
CC       of chromosomal replication. Binds to the origin of replication; it
CC       binds specifically double-stranded DNA at a 9 bp consensus (dnaA
CC       box): 5'-TTATC[CA]A[CA]A-3'. DnaA binds to ATP and to acidic
CC       phospholipids. {ECO:0000256|HAMAP-Rule:MF_00377,
CC       ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00724167}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
CC       ECO:0000256|SAAS:SAAS00756131}.
CC   -!- SIMILARITY: Belongs to the DnaA family. {ECO:0000256|HAMAP-
CC       Rule:MF_00377, ECO:0000256|RuleBase:RU004227,
CC       ECO:0000256|SAAS:SAAS00555179}.
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DR   EMBL; AM180355; CAJ66815.1; -; Genomic_DNA.
DR   RefSeq; WP_003420483.1; NC_009089.1.
DR   RefSeq; YP_001086464.1; NC_009089.1.
DR   ProteinModelPortal; Q18C85; -.
DR   STRING; 272563.CD0001; -.
DR   EnsemblBacteria; CAJ66815; CAJ66815; CD630_00010.
DR   GeneID; 31351432; -.
DR   GeneID; 4913287; -.
DR   KEGG; cdf:CD630_00010; -.
DR   KEGG; pdc:CDIF630_00001; -.
DR   PATRIC; fig|272563.120.peg.1; -.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   HOGENOM; HOG000235658; -.
DR   KO; K02313; -.
DR   OMA; REFNPLF; -.
DR   BioCyc; PDIF272563:G12WB-1-MONOMER; -.
DR   Proteomes; UP000001978; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003688; F:DNA replication origin binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006270; P:DNA replication initiation; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006275; P:regulation of DNA replication; IEA:UniProtKB-HAMAP.
DR   CDD; cd06571; Bac_DnaA_C; 1.
DR   Gene3D; 1.10.1750.10; -; 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; IPR024633; DnaA_N_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR010921; Trp_repressor/repl_initiator.
DR   PANTHER; PTHR30050:SF12; PTHR30050:SF12; 1.
DR   Pfam; PF00308; Bac_DnaA; 1.
DR   Pfam; PF08299; Bac_DnaA_C; 1.
DR   Pfam; PF11638; DnaA_N; 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 {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00731922};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001978};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|SAAS:SAAS00756112};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU004227, ECO:0000256|SAAS:SAAS00731887};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00756124};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00731897};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001978}.
FT   DOMAIN      135    263       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      347    416       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     143    150       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   439 AA;  50255 MW;  29C904A1C31481BB CRC64;
     MDIVSLWDKT LQLIKGDLTS VSFNTFFKNI VPLKIHLNDL ILLAPSDFNK DILENRYLHL
     IEDAISQLSL KKYNIKFVLS EKEVADLNSD STDLNYRVLY PNLNPKYTFD TFVIGNSNRF
     AHAACVAVAE SPAKAYNPLF LYGGVGLGKT HLMHAIGHHI VSQKKDSKVV YVSSEKFTNE
     LINSIKDDKN EEFRNKYRNV DVLLIDDIQF IAGKERTQEE FFHTFNTLHE ANKQIIISSD
     RPPKDIPTLE DRLRSRFEMG LITDIQAPDF ETRIAILRKK AQLERIDVPN EVMSYIAKNI
     KSNIRELEGA LTRVVAYSSL SNRVISFDLA TEALKDIITT SKNEEINVLR IKEKVSSVFN
     LKMEDFNSKK RTRSIAYPRQ IAMYLTRELT DLSLPKIGEE FGGRDHTTVI HAHDKVSKDI
     EESEEIKTKI DKIISDLKG
//
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