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Database: UniProt
Entry: I7JF89_9LACT
LinkDB: I7JF89_9LACT
Original site: I7JF89_9LACT 
ID   I7JF89_9LACT            Unreviewed;       456 AA.
AC   I7JF89;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   25-OCT-2017, entry version 38.
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   ORFNames=BN193_03265 {ECO:0000313|EMBL:CCK19214.1};
OS   Lactococcus raffinolactis 4877.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=1215915 {ECO:0000313|EMBL:CCK19214.1, ECO:0000313|Proteomes:UP000009323};
RN   [1] {ECO:0000313|EMBL:CCK19214.1, ECO:0000313|Proteomes:UP000009323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4877 {ECO:0000313|EMBL:CCK19214.1,
RC   ECO:0000313|Proteomes:UP000009323};
RA   Meslier V., Lechatelier E., Loux V., Renault P.;
RT   "Genome sequence of Lactococcus raffinolactis 4877.";
RL   Submitted (JUL-2012) 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:SAAS00735475}.
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}.
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:CCK19214.1}.
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DR   EMBL; CALL01000040; CCK19214.1; -; Genomic_DNA.
DR   RefSeq; WP_003137916.1; NZ_HE999912.1.
DR   EnsemblBacteria; CCK19214; CCK19214; BN193_03265.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000009323; 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   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; 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.
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:SAAS00747950};
KW   Complete proteome {ECO:0000313|Proteomes:UP000009323};
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:UP000009323}.
FT   DOMAIN      150    281       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      365    434       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     158    165       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   456 AA;  51884 MW;  60FF0B3846E6D166 CRC64;
     MSLTKDEQKF WARVKALAQN NLGQASYDFF IEPAKLLEIT DHNAKIYLDN NMHRDFWKKQ
     DDLIKTAGFE IFGAEISFAL YSADDINLAD YENADKITET SDIQETNQLV SSELKNGLNH
     KYTFQNFVQG EGNRMTLGAA IAVANDPGGM YNPLFIYGGP GLGKTHLMNA IGNEILNDKP
     DARIKYVSSE NFVNDYVQSS RKNQMQEFTD EYRTLDLLLL DDIQFFAKKE GTINEFFQTF
     NTLHDKGAQI VISSDRPPNE LNEFEDRLKS RFSWGLTTDI TAPNYEDRMA ILLNKVDEMD
     LQVPSETLSY IAGRIDSNVR DLEGALKNLK FYANTYHIDT IDINTAAKAL SNLESTKITQ
     DKDISSQKIQ EEVANFYKIS VADMISKKRP KEIAYPRQIA MYLIREITGK SLPAIGKEFG
     GRDHTTVIYA HKQISDKMKT DTSLQKEMDT IKSHLK
//
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