ID   PIF1_BDEBA              Reviewed;         439 AA.
AC   Q6MHJ5;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 109.
DE   RecName: Full=ATP-dependent DNA helicase pif1;
DE            EC=3.6.4.12;
GN   Name=pif1; OrderedLocusNames=Bd3546;
OS   Bdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIMB 9529 /
OS   HD100).
OC   Bacteria; Proteobacteria; Oligoflexia; Bdellovibrionales;
OC   Bdellovibrionaceae; Bdellovibrio.
OX   NCBI_TaxID=264462;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15356 / DSM 50701 / NCIMB 9529 / HD100;
RX   PubMed=14752164; DOI=10.1126/science.1093027;
RA   Rendulic S., Jagtap P., Rosinus A., Eppinger M., Baar C., Lanz C.,
RA   Keller H., Lambert C., Evans K.J., Goesmann A., Meyer F., Sockett R.E.,
RA   Schuster S.C.;
RT   "A predator unmasked: life cycle of Bdellovibrio bacteriovorus from a
RT   genomic perspective.";
RL   Science 303:689-692(2004).
RN   [2]
RP   FUNCTION.
RX   PubMed=23657261; DOI=10.1038/nature12149;
RA   Paeschke K., Bochman M.L., Garcia P.D., Cejka P., Friedman K.L.,
RA   Kowalczykowski S.C., Zakian V.A.;
RT   "Pif1 family helicases suppress genome instability at G-quadruplex
RT   motifs.";
RL   Nature 497:458-462(2013).
CC   -!- FUNCTION: DNA-dependent ATPase and 5'-3' DNA helicase that efficiently
CC       unwinds G-quadruplex (G4) DNA structures. May be involved in resolving
CC       commom issues that arise during DNA replication, recombination, and
CC       repair. {ECO:0000269|PubMed:23657261}.
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the helicase family. PIF1 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; BX842655; CAE78337.1; -; Genomic_DNA.
DR   RefSeq; WP_011165875.1; NC_005363.1.
DR   AlphaFoldDB; Q6MHJ5; -.
DR   SMR; Q6MHJ5; -.
DR   STRING; 264462.Bd3546; -.
DR   EnsemblBacteria; CAE78337; CAE78337; Bd3546.
DR   KEGG; bba:Bd3546; -.
DR   eggNOG; COG0507; Bacteria.
DR   HOGENOM; CLU_001613_7_1_7; -.
DR   OMA; ITLHQFA; -.
DR   OrthoDB; 961809at2; -.
DR   Proteomes; UP000008080; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0000723; P:telomere maintenance; IEA:InterPro.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR010285; DNA_helicase_pif1-like.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF05970; PIF1; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
PE   3: Inferred from homology;
KW   ATP-binding; DNA damage; DNA recombination; DNA repair; DNA-binding;
KW   Helicase; Hydrolase; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..439
FT                   /note="ATP-dependent DNA helicase pif1"
FT                   /id="PRO_0000423710"
SQ   SEQUENCE   439 AA;  49135 MW;  2EC825E12C18018B CRC64;
     MNSESKCYRF YICFARLGSG MIAGLMPVHE IELSPEQASA LDLLRSGENV FLTGGAGSGK
     SFLIRQFMRE LDPKEMPILA STGAAAVLLG GRTFHSFFGL GIMEGGADAT YERASKDKRL
     MSRLRKVEGV IIDEISMIPG QALMIAEALS QRARESKLPW GGMRVIAVGD FAQLPPVTHT
     GQRDWCFLNG VWEVSGFQTV MLSHNQRVSD NLFLDVLSDV RHGKVTERVR EFLNEHVQDH
     DEDDPGTRLF PRKINAEKFN ERKLAEIDET EVVIESIYSG SERHIETLKK ASPIAEKLIL
     KIGCQVMFLQ NDPQRRWVNG TRGTVVDITA DQITVRKDRG REVQVSKSSF AIQDAEGNIM
     AQVEQFPLTL AYATTIHKSQ GATLDDLWCD LSQLWEPGQA YVALSRLRSA KGLHLIGWNP
     RSIIVDPKVL HFYKQFEGL