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Database: UniProt
Entry: A0A0B7IS14_9PROT
LinkDB: A0A0B7IS14_9PROT
Original site: A0A0B7IS14_9PROT 
ID   A0A0B7IS14_9PROT        Unreviewed;       468 AA.
AC   A0A0B7IS14;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   16-JAN-2019, entry version 30.
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   ECO:0000313|EMBL:CEN55063.1};
GN   ORFNames=BN1209_0001 {ECO:0000313|EMBL:CEN55063.1};
OS   Candidatus Methylopumilus turicensis.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC   Methylophilaceae; Candidatus Methylopumilus.
OX   NCBI_TaxID=1581680 {ECO:0000313|EMBL:CEN55063.1, ECO:0000313|Proteomes:UP000056322};
RN   [1] {ECO:0000313|EMBL:CEN55063.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=MMS-10A-171 {ECO:0000313|EMBL:CEN55063.1};
RA   Salcher M Michaela;
RL   Submitted (DEC-2014) 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; LN794158; CEN55063.1; -; Genomic_DNA.
DR   RefSeq; WP_045750407.1; NZ_LN794158.1.
DR   EnsemblBacteria; CEN55063; CEN55063; BN1209_0001.
DR   KEGG; mbac:BN1209_0001; -.
DR   KO; K02313; -.
DR   OrthoDB; 219876at2; -.
DR   Proteomes; UP000056322; Chromosome 1.
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   Complete proteome {ECO:0000313|Proteomes:UP000056322};
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   ECO:0000313|EMBL:CEN55063.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00756117};
KW   Reference proteome {ECO:0000313|Proteomes:UP000056322}.
FT   DOMAIN      165    295       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      376    445       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     173    180       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   468 AA;  53669 MW;  5CA2F738FEB18340 CRC64;
     MNNFWVACLG RFEKELSAQQ FNTWIKPLHF KVDDQSLTLF APNRFVQQWV KDKFLSRVID
     FAKENFSHPI SINVVLLESH SDDNIKSIDS LMPIQPAKTT PKPSVSPNTK KLDKSIPKET
     PSNKYKVSEH SGLNPAFNFG NLVTGKANQL ARAAAVQIAE NPGNAYNPLF IYGGVGLGKT
     HLLQAIGNHL KELRPEAKIK YLHAERYVSD VVKAYEHKSF DEFKRLYHSL DMLLIDDIQF
     FAKKTRTQEE FFYAFNSLIE SKKQIIITCD TYPKEIEDMD ERLRTRFSWG LTVAVEPPEL
     EMRVAILLKK AEEANITLSE EVAFFVAKQI RSSVRELEGA LNRIVAMSKF TGHQIDVHLA
     KEALKDLIAV RGRQITIEYI QKTVADYYKI KVAEMYSKKR TRNFARPRQI AMALTRELTN
     HSFPEIGEAF GSRHHTTVMH ACDEIEQLRQ NDQTIARDIA LLVQVIRD
//
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