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Database: UniProt
Entry: B1I1H4_DESAP
LinkDB: B1I1H4_DESAP
Original site: B1I1H4_DESAP 
ID   B1I1H4_DESAP            Unreviewed;       445 AA.
AC   B1I1H4;
DT   29-APR-2008, integrated into UniProtKB/TrEMBL.
DT   29-APR-2008, sequence version 1.
DT   25-OCT-2017, entry version 78.
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   OrderedLocusNames=Daud_0001 {ECO:0000313|EMBL:ACA58570.1};
OS   Desulforudis audaxviator (strain MP104C).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Candidatus Desulforudis.
OX   NCBI_TaxID=477974 {ECO:0000313|EMBL:ACA58570.1, ECO:0000313|Proteomes:UP000008544};
RN   [1] {ECO:0000313|Proteomes:UP000008544}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MP104C {ECO:0000313|Proteomes:UP000008544};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Bruce D., Pitluck S., Lowry S.R., Larimer F.,
RA   Land M.L., Hauser L., Kyrpides N., Ivanova N.N., Richardson P.;
RT   "Complete sequence of chromosome of Desulforudis audaxviator MP104C.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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:SAAS00911680}.
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; CP000860; ACA58570.1; -; Genomic_DNA.
DR   RefSeq; WP_012301164.1; NC_010424.1.
DR   ProteinModelPortal; B1I1H4; -.
DR   STRING; 477974.Daud_0001; -.
DR   EnsemblBacteria; ACA58570; ACA58570; Daud_0001.
DR   KEGG; dau:Daud_0001; -.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   HOGENOM; HOG000235658; -.
DR   KO; K02313; -.
DR   OMA; REFNPLF; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000008544; 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   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:SF2; PTHR30050:SF2; 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:SAAS00747950};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008544};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|SAAS:SAAS00911664};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU004227, ECO:0000256|SAAS:SAAS00747996};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00911684};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00747895};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008544}.
FT   DOMAIN      139    267       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      352    421       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     147    154       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   445 AA;  51260 MW;  5745610D8BD789D3 CRC64;
     MVPPEIMSIW QQLMQGLEKS VNRQSYDYWL KPLRPAAYHN KTLLIEVPNH FSRDWLHERY
     APLLKHSFET LAGHEVAIKF LLAREVPEVK KYLSRPLDKL STDLSALNPK YTFDSFVVGN
     SNRFAHAAAF AVADTPVKAY NPLFLYGGVG LGKTHLMHAI GHHILGNHSR YRIAYVTSER
     FTNDLINAIK DDQTPQFRSK YRSIDILLID DIQFLAGKER TQEEFFHTFN SLYEDAKQIV
     ISSDRPPKEI PTLEERLRSR FEWGLITDIQ PPDLETRIAI LRKKLQSEEN SLVPDETILY
     IADRIQSNIR ELEGAFIRVS AYASLNRTIV SPENAAEILK NILPPHKPKQ ITCSLIQQVV
     AGYYKLRPED LKAKKRTRNV AYPRQIAMYL TRELTDLSLP KIGDEFGGRD HTTVLHACEK
     INQEIQADPS VQEIINELIR RIQKP
//
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