(data stored in SCRATCH zone)

SWISSPROT: Q3KIX4_PSEPF

ID   Q3KIX4_PSEPF            Unreviewed;       465 AA.
AC   Q3KIX4;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   08-MAY-2019, entry version 113.
DE   RecName: Full=Replicative DNA helicase {ECO:0000256|RuleBase:RU362085};
DE            EC=3.6.4.12 {ECO:0000256|RuleBase:RU362085};
GN   OrderedLocusNames=Pfl01_0538 {ECO:0000313|EMBL:ABA72282.1};
OS   Pseudomonas fluorescens (strain Pf0-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=205922 {ECO:0000313|EMBL:ABA72282.1, ECO:0000313|Proteomes:UP000002704};
RN   [1] {ECO:0000313|EMBL:ABA72282.1, ECO:0000313|Proteomes:UP000002704}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pf0-1 {ECO:0000313|EMBL:ABA72282.1,
RC   ECO:0000313|Proteomes:UP000002704};
RX   PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA   Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA   Jackson R.W., Preston G.M., Zhang X.X., Moon C.D., Gehrig S.M.,
RA   Godfrey S.A., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA   Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA   Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA   Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA   Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT   "Genomic and genetic analyses of diversity and plant interactions of
RT   Pseudomonas fluorescens.";
RL   Genome Biol. 10:R51.1-R51.16(2009).
CC   -!- FUNCTION: Participates in initiation and elongation during
CC       chromosome replication; it exhibits DNA-dependent ATPase activity
CC       and contains distinct active sites for ATP binding, DNA binding,
CC       and interaction with DnaC protein, primase, and other prepriming
CC       proteins. {ECO:0000256|RuleBase:RU362085}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC         Evidence={ECO:0000256|RuleBase:RU362085};
CC   -!- SIMILARITY: Belongs to the helicase family. DnaB subfamily.
CC       {ECO:0000256|RuleBase:RU362085}.
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DR   EMBL; CP000094; ABA72282.1; -; Genomic_DNA.
DR   RefSeq; WP_011332193.1; NC_007492.2.
DR   STRING; 205922.Pfl01_0538; -.
DR   PRIDE; Q3KIX4; -.
DR   EnsemblBacteria; ABA72282; ABA72282; Pfl01_0538.
DR   KEGG; pfo:Pfl01_0538; -.
DR   eggNOG; ENOG4105CDU; Bacteria.
DR   eggNOG; COG0305; LUCA.
DR   HOGENOM; HOG000113196; -.
DR   KO; K02314; -.
DR   OMA; FQIAEAR; -.
DR   BioCyc; PFLU205922:G1G4S-545-MONOMER; -.
DR   Proteomes; UP000002704; Chromosome.
DR   GO; GO:1990077; C:primosome complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006269; P:DNA replication, synthesis of RNA primer; IEA:UniProtKB-UniRule.
DR   CDD; cd00984; DnaB_C; 1.
DR   Gene3D; 1.10.860.10; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR036185; DNA_heli_DnaB-like_N_sf.
DR   InterPro; IPR007692; DNA_helicase_DnaB.
DR   InterPro; IPR007694; DNA_helicase_DnaB-like_C.
DR   InterPro; IPR007693; DNA_helicase_DnaB-like_N.
DR   InterPro; IPR016136; DNA_helicase_N/primase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00772; DnaB; 1.
DR   Pfam; PF03796; DnaB_C; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF48024; SSF48024; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00665; DnaB; 1.
DR   PROSITE; PS51199; SF4_HELICASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q3KIX4.
DR   SWISS-2DPAGE; Q3KIX4.
KW   ATP-binding {ECO:0000256|RuleBase:RU362085};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002704};
KW   DNA replication {ECO:0000256|RuleBase:RU362085,
KW   ECO:0000256|SAAS:SAAS00740714};
KW   DNA-binding {ECO:0000256|RuleBase:RU362085,
KW   ECO:0000256|SAAS:SAAS00740674};
KW   Helicase {ECO:0000256|RuleBase:RU362085, ECO:0000313|EMBL:ABA72282.1};
KW   Hydrolase {ECO:0000256|RuleBase:RU362085,
KW   ECO:0000313|EMBL:ABA72282.1};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU362085};
KW   Primosome {ECO:0000256|RuleBase:RU362085}.
FT   DOMAIN      191    458       SF4 helicase. {ECO:0000259|PROSITE:
FT                                PS51199}.
SQ   SEQUENCE   465 AA;  51495 MW;  C34EDB8B0F9DD487 CRC64;
     MNEISAPEQY DLQTAALKVP PHSIEAEQAV LGGLMLDNNA WERVLDQVSD GDFYRHDHRL
     IFRAIAKLAD QNLPIDVVTL AEQLDKEGQT SQVGGLGYLG ELAKNTPSVA NIKAYAQIVR
     QRATLRQLIG ISTEIADSAF NPEGRTAEEI LDEAERQIFA IAEARPKTGG PVGVNDLLTK
     AIDRIDTLFN TADSITGLST GYTDLDEKTS GLQPADLIIV AGRPSMGKTT FAMNLVENAV
     LRSDKVVLVY SLEMPGESLI MRMLSSLGRI DQTKVRSGQL EDDDWPRLTS AVNLLNDRKL
     FIDDTAGISP SEMRARTRRL VREHGDIGLI MIDYLQLMQI PGSSGDNRTN EISEISRSLK
     ALAKEFNCPV VALSQLNRSL EQRPNKRPVN SDLRESGAIE QDADVIMFVY RDEVYHPETE
     HKGIAEIIIG KQRNGPIGFI RLAFIGKYTR FENLAPGSYN FDDDE
//

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