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Database: UniProt
Entry: A0A1H3PU71_9CLOT
LinkDB: A0A1H3PU71_9CLOT
Original site: A0A1H3PU71_9CLOT 
ID   A0A1H3PU71_9CLOT        Unreviewed;       464 AA.
AC   A0A1H3PU71;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   13-FEB-2019, entry version 11.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS01081161};
GN   Name=dnaA {ECO:0000256|HAMAP-Rule:MF_00377};
GN   ORFNames=SAMN05192546_10790 {ECO:0000313|EMBL:SDZ04491.1};
OS   Tindallia californiensis.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Tindallia.
OX   NCBI_TaxID=159292 {ECO:0000313|EMBL:SDZ04491.1, ECO:0000313|Proteomes:UP000199230};
RN   [1] {ECO:0000313|EMBL:SDZ04491.1, ECO:0000313|Proteomes:UP000199230}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=APO {ECO:0000313|EMBL:SDZ04491.1,
RC   ECO:0000313|Proteomes:UP000199230};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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:SAAS00756121}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
CC       ECO:0000256|SAAS:SAAS01082709}.
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; FNPV01000007; SDZ04491.1; -; Genomic_DNA.
DR   BioCyc; GCF_900107405:BLV55_RS10800-MONOMER; -.
DR   Proteomes; UP000199230; Unassembled WGS sequence.
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   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; 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   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:SAAS00756129};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000199230};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|SAAS:SAAS01082702};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU004227, ECO:0000256|SAAS:SAAS00756116};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS01082706};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00756117};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199230}.
FT   DOMAIN      159    287       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      370    439       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     167    174       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
FT   COILED      439    459       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   464 AA;  53411 MW;  866B6B0341DEF95E CRC64;
     MDQQLSQIWD ETLSVIEQEV TGVSFDTWIK VIEPLRVQDD ANQIIFRAPN QFIKNILSDR
     YLILIKNAIK EVTSCSYDVV FQLPDEVKTV DSTTLVTNTE EEKTGNNQSS TEKTQTATTI
     QTANNNLNPK YIFDTFVVGN SNRFAHAASV AVSEAPAKAY NPLFIYGGVG LGKTHLMHAI
     GHHILQSNKQ MKVFYSSSET FTNELINSIR DDKNIEFRNK YRNVDVLLID DIQFIANKER
     TQEEFFHTFN ALHQYNKQII ISSDRPPKEI PTLEERLRSR FEWGLIADIQ PPDYETRIAI
     LRKKAHLEQL NVSDDVLLFI AKKIQSNIRE LEGALNRIVV HCKLNNNELN IDTASRIINE
     VFTTQSKQIN VGFIKEYISN QYSIKAEDLD STKRTRSIAF PRQIAMYLTR ELTDLSLPKI
     GKEFGNRDHT TVMHAHDKIV KEMEKDDRLK QRVEEMLREI KGGD
//
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