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Database: UniProt
Entry: K4IJ79_BIFAP
LinkDB: K4IJ79_BIFAP
Original site: K4IJ79_BIFAP 
ID   K4IJ79_BIFAP            Unreviewed;       580 AA.
AC   K4IJ79;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   25-OCT-2017, entry version 40.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU000577};
GN   Name=dnaA {ECO:0000256|HAMAP-Rule:MF_00377};
GN   OrderedLocusNames=BAST_0001 {ECO:0000313|EMBL:AFU70607.1};
OS   Bifidobacterium asteroides (strain PRL2011).
OC   Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC   Bifidobacterium.
OX   NCBI_TaxID=1147128 {ECO:0000313|EMBL:AFU70607.1, ECO:0000313|Proteomes:UP000007006};
RN   [1] {ECO:0000313|EMBL:AFU70607.1, ECO:0000313|Proteomes:UP000007006}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PRL2011 {ECO:0000313|EMBL:AFU70607.1,
RC   ECO:0000313|Proteomes:UP000007006};
RX   PubMed=23028506; DOI=10.1371/journal.pone.0044229;
RA   Bottacini F., Milani C., Turroni F., Sanchez B., Foroni E.,
RA   Duranti S., Serafini F., Viappiani A., Strati F., Ferrarini A.,
RA   Delledonne M., Henrissat B., Coutinho P., Fitzgerald G.F.,
RA   Margolles A., van Sinderen D., Ventura M.;
RT   "Bifidobacterium asteroides PRL2011 genome analysis reveals clues for
RT   colonization of the insect gut.";
RL   PLoS ONE 7:E44229-E44229(2012).
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:SAAS00735475}.
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; CP003325; AFU70607.1; -; Genomic_DNA.
DR   EnsemblBacteria; AFU70607; AFU70607; BAST_0001.
DR   KEGG; bast:BAST_0001; -.
DR   PATRIC; fig|1147128.3.peg.1; -.
DR   KO; K02313; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000007006; 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; 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 {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00747950};
KW   Complete proteome {ECO:0000313|Proteomes:UP000007006};
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:UP000007006}.
FT   DOMAIN      270    409       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      485    554       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     278    285       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   580 AA;  64320 MW;  F9A0D53C79FFA4BE CRC64;
     MAQDPLDAAA QAERIWDSVL QVLRYSSSLT SRDKGWLEDI TPEAVFGTTI VLRVSSKATQ
     EAVQGPLSQP LLNALQLVTN QEMFPAIKIV YPEQMAKQMA ADQQKDQRTS ALAGSAPGSG
     EFRQVHSPAQ DPYGDYQRQT GADRTPGSET HSDWQTETAG TSKSPVVSVN DFHEGTYVPM
     TLDMQAELSE PSPAMRSTAG GDADQQSEAD RTASRPAFTV PRFPMSQNRV ERDPQTHLNK
     NATFDTFVPG DSNRFARTVA LAVAEGSGQD FNPLCIYGSS GLGKTHLLNA IGNYALVKDP
     SLKVRYVNSE EFTNEFIDAL QNSTQGSGQI AEFNRRYRQV DVLLIDDIQF LGGKEATLDQ
     FFHTFNALHD ANKRIVIASD VAPKNLKGFE SRLISRFDSG LTVDVKPPDR ETRVAILRMM
     ASMNGVSIPN EVLDLIAERF TENIRELEGA LTRVTAVASL NNQPVTTALA EQTLQDFFST
     DVEIKPTDII SQVAKYFHLT FDDIVGRTRT KNIALARQIA MYLAREMTSM SLVDIGEVFG
     GRDHTTVMHA YTRISNEMQE KREIYNYVME LTVRLKQPQN
//
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