GenomeNet

Database: UniProt
Entry: F0LQ67_VIBFN
LinkDB: F0LQ67_VIBFN
Original site: F0LQ67_VIBFN 
ID   F0LQ67_VIBFN            Unreviewed;       468 AA.
AC   F0LQ67;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   16-JAN-2019, entry version 56.
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   OrderedLocusNames=vfu_A00313 {ECO:0000313|EMBL:ADT85540.1};
OS   Vibrio furnissii (strain DSM 14383 / NCTC 11218).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Vibrio.
OX   NCBI_TaxID=903510 {ECO:0000313|EMBL:ADT85540.1, ECO:0000313|Proteomes:UP000007456};
RN   [1] {ECO:0000313|EMBL:ADT85540.1, ECO:0000313|Proteomes:UP000007456}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14383 / NCTC 11218 {ECO:0000313|Proteomes:UP000007456};
RX   PubMed=21217006; DOI=10.1128/JB.01512-10;
RA   Lux T.M., Lee R., Love J.;
RT   "Complete genome sequence of a free-living Vibrio furnissii sp. nov.
RT   strain (NCTC 11218).";
RL   J. Bacteriol. 193:1487-1488(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: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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; CP002377; ADT85540.1; -; Genomic_DNA.
DR   RefSeq; WP_004728727.1; NC_016602.1.
DR   ProteinModelPortal; F0LQ67; -.
DR   STRING; 903510.vfu_A00313; -.
DR   EnsemblBacteria; ADT85540; ADT85540; vfu_A00313.
DR   KEGG; vfu:vfu_A00313; -.
DR   PATRIC; fig|903510.3.peg.295; -.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   KO; K02313; -.
DR   OMA; REFNPLF; -.
DR   OrthoDB; 219876at2; -.
DR   BioCyc; VFUR903510:G1GQK-331-MONOMER; -.
DR   Proteomes; UP000007456; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000007456};
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:UP000007456}.
FT   DOMAIN      165    378       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}.
FT   COILED      327    347       {ECO:0000256|SAM:Coils}.
FT   COILED      445    465       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   468 AA;  53242 MW;  72589713F5EA43C8 CRC64;
     MSSSLWLQCL QQLQEELPAA EFSMWVRPLQ AELNDNTLTL FAPNRFVLDW VRDKYINNIN
     RLLKDFCGHD VPSLRFEVGS RRVVAPKPTQ KRTAADVAAE SSAPAQLAQR KPIHKTWDDD
     AANAPEITYR SNMNPKHKFN NFVEGKSNQL GLAAARQVSD NPGAAYNPLF LYGGTGLGKT
     HLLHAVGNAI VDNNPNAKVV YMHSERFVQD MVKALQNNAI EEFKRYYRSV DALLIDDIQF
     FANKERSQEE FFHTFNALLE GNQQIILTSD RYPKEINGVE DRLKSRFGWG LTVAIEPPEL
     ETRVAILMKK AEDHQIHLPD EVAFFIAKRL RSNVRELEGA LNRVIANANF TGRPITIDFV
     REALRDLLAL QEKLVTIDNI QKTVAEYYKI KVADLLSKRR SRSVARPRQL AMALSKELTN
     HSLPEIGDAF GGRDHTTVLH ACRKIEQLRE ESHDIKEDYS NLIRTLSS
//
DBGET integrated database retrieval system