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Database: UniProt
Entry: J9Z6Z1_LEPFM
LinkDB: J9Z6Z1_LEPFM
Original site: J9Z6Z1_LEPFM 
ID   J9Z6Z1_LEPFM            Unreviewed;       465 AA.
AC   J9Z6Z1;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   25-OCT-2017, entry version 37.
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:AFS52255.1};
GN   OrderedLocusNames=LFML04_0001 {ECO:0000313|EMBL:AFS52255.1};
OS   Leptospirillum ferriphilum (strain ML-04).
OC   Bacteria; Nitrospirae; Nitrospirales; Nitrospiraceae; Leptospirillum.
OX   NCBI_TaxID=1048260 {ECO:0000313|EMBL:AFS52255.1, ECO:0000313|Proteomes:UP000006177};
RN   [1] {ECO:0000313|EMBL:AFS52255.1, ECO:0000313|Proteomes:UP000006177}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ML-04 {ECO:0000313|EMBL:AFS52255.1,
RC   ECO:0000313|Proteomes:UP000006177};
RX   PubMed=22203551; DOI=10.1007/s12275-011-1099-9;
RA   Mi S., Song J., Lin J., Che Y., Zheng H., Lin J.;
RT   "Complete genome of Leptospirillum ferriphilum ML-04 provides insight
RT   into its physiology and environmental adaptation.";
RL   J. Microbiol. 49:890-901(2011).
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:SAAS00747914}.
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; CP002919; AFS52255.1; -; Genomic_DNA.
DR   RefSeq; WP_014959779.1; NC_018649.1.
DR   ProteinModelPortal; J9Z6Z1; -.
DR   EnsemblBacteria; AFS52255; AFS52255; LFML04_0001.
DR   KEGG; lfi:LFML04_0001; -.
DR   PATRIC; fig|1048260.3.peg.1; -.
DR   KO; K02313; -.
DR   OMA; REFNPLF; -.
DR   Proteomes; UP000006177; 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; 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.
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:UP000006177};
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:UP000006177}.
FT   DOMAIN      160    288       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      371    440       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     168    175       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   465 AA;  52653 MW;  46B9BA57EB5128E0 CRC64;
     MSQSLWNRVL ERFCEFGSEP GALERDGILD LLKGAVLEGG KDGYSVLVGS SFIQRLVQNR
     YYKDLLTAFR EVTQNPEISF DVLVQPENVP RKKRKVVRNS GPEGGLSPGK PVPLPLGEDR
     SPSWNSNLNP RYFFENYVVG VCNQFAHAAA FAIANNPSKA YNPFYLFGSV GLGKTHLVSA
     IGNCMIALYP SLKVLYITTE SFLNEMVSAI KFNKMNEFRE RYRKIDVLIM DDVQFLSGKE
     RTQEELFYTF NALYENGKQI ILSSDCMPND IPTLEGRLKS RFGWGLIADI QIPDFETKVE
     ILKGKMAQEK VDLPMDVVYF LANSIKSNIR ELEGAMIRLG AYGNLMGKPI TIEVARNLLS
     DLMPLSRESI SVDRILQEVA DYFKVLPKEI RSKKRHKTLV TARHVAVYLI RELTQKSYPE
     IGRELGGRDH STAIYSFKMV EEKLESDPAL TSDIVYLKKK LEQQG
//
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