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Database: UniProt
Entry: A0A125S3R7_9FLAO
LinkDB: A0A125S3R7_9FLAO
Original site: A0A125S3R7_9FLAO 
ID   A0A125S3R7_9FLAO        Unreviewed;       472 AA.
AC   A0A125S3R7;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   05-JUL-2017, entry version 13.
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   ORFNames=AXF12_08405 {ECO:0000313|EMBL:AMD85531.1};
OS   Capnocytophaga haemolytica.
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Capnocytophaga.
OX   NCBI_TaxID=45243 {ECO:0000313|EMBL:AMD85531.1, ECO:0000313|Proteomes:UP000065822};
RN   [1] {ECO:0000313|EMBL:AMD85531.1, ECO:0000313|Proteomes:UP000065822}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCUG 32990 {ECO:0000313|EMBL:AMD85531.1,
RC   ECO:0000313|Proteomes:UP000065822};
RA   Wen L., He K., Yang H.;
RL   Submitted (FEB-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: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; CP014227; AMD85531.1; -; Genomic_DNA.
DR   RefSeq; WP_066430205.1; NZ_FOVX01000012.1.
DR   EnsemblBacteria; AMD85531; AMD85531; AXF12_08405.
DR   KEGG; chg:AXF12_08405; -.
DR   KO; K02313; -.
DR   Proteomes; UP000065822; 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:UP000065822};
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:UP000065822}.
FT   DOMAIN      166    299       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      380    449       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     174    181       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   472 AA;  53779 MW;  D63BE26B48817D38 CRC64;
     MKEAAEKVWT KCLEFIHDNI DEAPFNTWFA PIIPMGLENN TLKIKVPSKF FCEWLEENYI
     SLLKSAMTLT LGTGSRLVYI IDTPAARPEQ LPSTNRPELA KQSLPITSES KNPELRNPFV
     IPGIREITID PQLNLHYNFD NFVEGSANRL ARSAAMSVAN KPGKTAFNPL FIFGGVGLGK
     THLAHAIGVD IKEKHPKKKV LYVSAEKFTQ QFIAASTGKD KNALNDFIYF YQLIDVLIVD
     DIQFLAGKVK TQDAFFHIFN HLHQNGRQVI LTSDKAPVDL FDIEQRLLSR FKWGLSAELQ
     APNYEMRFQI LKNKFYTDGA DIDGEIIAYL AENVRTNIRE LEGVSNSLIA QAAFERKEYS
     IELAQSVIER SVKNHRVELT IDHIQQIIAD YFNLDIQSLQ SKTRRRNVVQ ARQLAMFFAK
     KYTKNSLTTI GSQIGQRDHA TVLHACKTVE NLVETDQMFK RYVVELDTKF TE
//
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