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Database: UniProt
Entry: I0XUR0_9LEPT
LinkDB: I0XUR0_9LEPT
Original site: I0XUR0_9LEPT 
ID   I0XUR0_9LEPT            Unreviewed;       435 AA.
AC   I0XUR0;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   16-JAN-2019, entry version 45.
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   ECO:0000313|EMBL:EIE02618.1};
GN   ORFNames=LEP1GSC185_1305 {ECO:0000313|EMBL:EIE02618.1};
OS   Leptospira licerasiae serovar Varillal str. VAR 010.
OC   Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX   NCBI_TaxID=1049972 {ECO:0000313|EMBL:EIE02618.1, ECO:0000313|Proteomes:UP000004889};
RN   [1] {ECO:0000313|EMBL:EIE02618.1, ECO:0000313|Proteomes:UP000004889}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VAR 010 {ECO:0000313|EMBL:EIE02618.1};
RX   PubMed=23145189; DOI=10.1371/journal.pntd.0001853;
RA   Ricaldi J.N., Fouts D.E., Selengut J.D., Harkins D.M., Patra K.P.,
RA   Moreno A., Lehmann J.S., Purushe J., Sanka R., Torres M.,
RA   Webster N.J., Vinetz J.M., Matthias M.A.;
RT   "Whole Genome Analysis of Leptospira licerasiae Provides Insight into
RT   Leptospiral Evolution and Pathogenicity.";
RL   PLoS Negl. Trop. Dis. 6:E1853-E1853(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}.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EIE02618.1}.
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DR   EMBL; AHOO02000005; EIE02618.1; -; Genomic_DNA.
DR   RefSeq; WP_008590074.1; NZ_AHOO02000005.1.
DR   EnsemblBacteria; EIE02618; EIE02618; LEP1GSC185_1305.
DR   GeneID; 35862230; -.
DR   PATRIC; fig|1049972.3.peg.626; -.
DR   OrthoDB; 219876at2; -.
DR   Proteomes; UP000004889; 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; 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.
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:UP000004889};
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:UP000004889}.
FT   DOMAIN      129    259       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      343    411       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     137    144       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   435 AA;  50577 MW;  87254ADF0CE97D57 CRC64;
     MDPSWKRVLE EVSKEIPPTY FDKFIYTLQL ESLTDDRCIL IAPSSNIKTH VEKKYQNHIE
     EAIFRASGNR VPVEIILESA SNLSEVLQEK FKDKSYSFNP DYSFDNFIVG NTNRLAFSAA
     MECVKNPAEI NPLYLFGKVG VGKTHLLHSI GSEILKKEPW KTVHYIDIKS FMSEFLFALQ
     SRDSIESFKI KYQSYNCLLI DDIQLLNTGA EKTQEEFFSI FNFLFERKRQ IVIASDRPSS
     ELPLHERLKS RFVTGVQADI QPPDKDIRIG ILEKNCQILN LGLSQEHIQF IADLIEDDTR
     ALLGALNDLA LHKRAFSHLF FTTTMIEEIL KNRIFRKKNF QLSQDKVIEH ISSLYNLDPN
     EVMGKSRKPE YVIPRHLCMY VLHKGFRLNK SQVGRMFSAE HTTVIHAVRN IENKIKDDKE
     FSIKVEEVLN RFRFQ
//
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