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Database: UniProt
Entry: A4XFI1_CALS8
LinkDB: A4XFI1_CALS8
Original site: A4XFI1_CALS8 
ID   A4XFI1_CALS8            Unreviewed;       454 AA.
AC   A4XFI1;
DT   29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2007, sequence version 1.
DT   25-OCT-2017, entry version 82.
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=Csac_0001 {ECO:0000313|EMBL:ABP65666.1};
OS   Caldicellulosiruptor saccharolyticus (strain ATCC 43494 / DSM 8903 /
OS   Tp8T 6331).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacterales Family III. Incertae Sedis;
OC   Caldicellulosiruptor.
OX   NCBI_TaxID=351627 {ECO:0000313|EMBL:ABP65666.1, ECO:0000313|Proteomes:UP000000256};
RN   [1] {ECO:0000313|Proteomes:UP000000256}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43494 / DSM 8903 / Tp8T 6331
RC   {ECO:0000313|Proteomes:UP000000256};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A.,
RA   van de Werken H.J.G., Verhaart M.R.A., VanFossen A.L., Lewis D.L.,
RA   Nichols J.D., Goorissen H.P., van Niel E.W.J., Stams F.J.M.,
RA   Willquist K.U., Ward D.E., van der Oost J., Kelly R.M., Kengen S.M.W.,
RA   Richardson P.;
RT   "Genome sequence of the thermophilic hydrogen-producing bacterium
RT   Caldicellulosiruptor saccharolyticus DSM 8903.";
RL   Submitted (APR-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; CP000679; ABP65666.1; -; Genomic_DNA.
DR   RefSeq; WP_011915633.1; NC_009437.1.
DR   ProteinModelPortal; A4XFI1; -.
DR   STRING; 351627.Csac_0001; -.
DR   EnsemblBacteria; ABP65666; ABP65666; Csac_0001.
DR   KEGG; csc:Csac_0001; -.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   HOGENOM; HOG000235658; -.
DR   KO; K02313; -.
DR   OMA; REFNPLF; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000000256; 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:UP000000256};
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:UP000000256}.
FT   DOMAIN      146    274       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      360    429       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     154    161       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   454 AA;  52451 MW;  658909657D90C87A CRC64;
     MVDYDVNKVW EDIKEVIKKE LNPSPTDISY NTWVETLVPI CFDENDTFIL KAFADFHRDI
     VINRYSLLIL NALRQLYSPH LSLKVILPNE VEKYKKYIKQ KQEEKVEVTT TLNPKYTFET
     FVVGNNNRLA HAAALAVAET PPGEKTYNPL FIYGGVGLGK THLMHAIGHH VLKLYPDTKV
     MYVTSEIFTN ELIAAIRDEK TDEFRMKYRN VDVLLIDDIQ FLGGKERTQE EFFHTFNTLY
     EANKKIILSS DRPPKEINTL EDRLRSRFEW GLITDIQPPD FETRIAILSK KCQLEGTPVP
     QHILEFIASK IETNIRELEG ALNKILAYSK LMAPDKEITL ELAEKALKEF IDTNTKKELT
     IEDIQAEVAG YFNIKLEDFK SSRRSRNVAF PRQIAMYLAR ELTNVSLPKI GEAFGGKDHT
     TVLHACEKIK ELINKDTNIR NTVENLKKRL INRE
//
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