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Database: UniProt
Entry: V3T3B7_SERS3
LinkDB: V3T3B7_SERS3
Original site: V3T3B7_SERS3 
ID   V3T3B7_SERS3            Unreviewed;       463 AA.
AC   V3T3B7;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   25-OCT-2017, entry version 30.
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=Ser39006_00411 {ECO:0000313|EMBL:ESN63003.1};
OS   Serratia sp. (strain ATCC 39006).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=104623 {ECO:0000313|EMBL:ESN63003.1, ECO:0000313|Proteomes:UP000017700};
RN   [1] {ECO:0000313|EMBL:ESN63003.1, ECO:0000313|Proteomes:UP000017700}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39006 {ECO:0000313|EMBL:ESN63003.1,
RC   ECO:0000313|Proteomes:UP000017700};
RX   PubMed=24336377;
RA   Fineran P.C., Iglesias Cans M.C., Ramsay J.P., Wilf N.M.,
RA   Cossyleon D., McNeil M.B., Williamson N.R., Monson R.E., Becher S.A.,
RA   Stanton J.A., Brugger K., Brown S.D., Salmond G.P.;
RT   "Draft genome sequence of Serratia sp. strain ATCC 39006, a model
RT   bacterium for analysis of the biosynthesis and regulation of
RT   prodigiosin, a carbapenem, and gas vesicles.";
RL   Genome Announc. 1:E01039-E01039(2013).
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: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:ESN63003.1}.
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DR   EMBL; AWXH01000002; ESN63003.1; -; Genomic_DNA.
DR   EnsemblBacteria; ESN63003; ESN63003; Ser39006_00411.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000017700; 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; IPR024633; DnaA_N_dom.
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:SAAS00747950};
KW   Complete proteome {ECO:0000313|Proteomes:UP000017700};
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:UP000017700}.
FT   DOMAIN      160    362       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   463 AA;  52245 MW;  03F297B7A420D43B CRC64;
     MSLSLWQQCL ARLQDELPAT EFSMWIRPLQ AELSDNTLAL YAPNRFVLDW VRDKYLNNIN
     GLLTDFCGID APLLRFEVGS KSVMPVSVSA GNHIAAAAPV APVRVTSPVR PSWDTPRTQT
     EHTYRSNVNP KHTFDNFVEG KSNQLARAAA RQVADNPGGA YNPLFLYGGT GLGKTHLLHA
     VGNGIVTRKP NAKVVYMHSE RFVQDMVKAL QNNAIEEFKR YYRSVDALLI DDIQFFANKE
     RSQEEFFHTF NALLEGNQQI ILTSDRYPKE INGVEDRLKS RFGWGLTVAI EPPELETRVA
     ILMKKADEND IRLPGEVAFF IAKRLRSNVR ELEGALNRVI ANANFTGRSI TIDFVREALR
     DLLALQEKLV TIDNIQKTVA EYYKIKVADL LSKRRSRSVA RPRQMAMALA KELTNHSLPE
     IGDAFGGRDH TTVLHACRKI GQLREESHDI KEDFSNLIRT LSS
//
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