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Database: UniProt
Entry: A5HZM6_CLOBH
LinkDB: A5HZM6_CLOBH
Original site: A5HZM6_CLOBH 
ID   A5HZM6_CLOBH            Unreviewed;       884 AA.
AC   A5HZM6;
DT   26-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2007, sequence version 1.
DT   27-MAR-2024, entry version 95.
DE   RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE            EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN   Name=pcrA {ECO:0000313|EMBL:CAL82235.1};
GN   OrderedLocusNames=CBO0683 {ECO:0000313|EMBL:CAL82235.1};
OS   Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=441771 {ECO:0000313|EMBL:CAL82235.1, ECO:0000313|Proteomes:UP000001986};
RN   [1] {ECO:0000313|EMBL:CAL82235.1, ECO:0000313|Proteomes:UP000001986}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hall / ATCC 3502 / NCTC 13319 / Type A [Sanger]
RC   {ECO:0000313|Proteomes:UP000001986};
RX   PubMed=17519437; DOI=10.1101/gr.6282807;
RA   Sebaihia M., Peck M.W., Minton N.P., Thomson N.R., Holden M.T.G.,
RA   Mitchell W.J., Carter A.T., Bentley S.D., Mason D.R., Crossman L.,
RA   Paul C.J., Ivens A., Wells-Bennik M.H.J., Davis I.J., Cerdeno-Tarraga A.M.,
RA   Churcher C., Quail M.A., Chillingworth T., Feltwell T., Fraser A.,
RA   Goodhead I., Hance Z., Jagels K., Larke N., Maddison M., Moule S.,
RA   Mungall K., Norbertczak H., Rabbinowitsch E., Sanders M., Simmonds M.,
RA   White B., Whithead S., Parkhill J.;
RT   "Genome sequence of a proteolytic (Group I) Clostridium botulinum strain
RT   Hall A and comparative analysis of the clostridial genomes.";
RL   Genome Res. 17:1082-1092(2007).
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=5.6.2.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00034618};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by
CC         translocating in the 3'-5' direction.; EC=5.6.2.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00034617};
CC   -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC       {ECO:0000256|ARBA:ARBA00009922}.
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DR   EMBL; AM412317; CAL82235.1; -; Genomic_DNA.
DR   RefSeq; YP_001253224.1; NC_009495.1.
DR   AlphaFoldDB; A5HZM6; -.
DR   GeneID; 5184938; -.
DR   KEGG; cbo:CBO0683; -.
DR   PATRIC; fig|413999.7.peg.679; -.
DR   HOGENOM; CLU_004585_5_5_9; -.
DR   Proteomes; UP000001986; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0033202; C:DNA helicase complex; IBA:GO_Central.
DR   GO; GO:0043138; F:3'-5' DNA helicase activity; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0000725; P:recombinational repair; IBA:GO_Central.
DR   CDD; cd17932; DEXQc_UvrD; 1.
DR   Gene3D; 1.10.10.160; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR013986; DExx_box_DNA_helicase_dom_sf.
DR   InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR   InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR014016; UvrD-like_ATP-bd.
DR   PANTHER; PTHR11070:SF2; ATP-DEPENDENT DNA HELICASE SRS2; 1.
DR   PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR   Pfam; PF00580; UvrD-helicase; 1.
DR   Pfam; PF13361; UvrD_C; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR   PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00560}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|PROSITE-
KW   ProRule:PRU00560};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU00560};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00560}; Reference proteome {ECO:0000313|Proteomes:UP000001986}.
FT   DOMAIN          7..293
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   DOMAIN          294..561
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51217"
FT   COILED          725..832
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         28..35
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ   SEQUENCE   884 AA;  103715 MW;  F3ED713CCAF39258 CRC64;
     MHLDVISGLN DAQREAVTTT EGYIRVIAGA GSGKTKALTS RYIYLVHELG ISTANILCAT
     FTNKAAREMK KRIRTMIGDN DTGLIGTFHG FCRRLLKEDI YTINYPDNFI VMDNEDMDLV
     LRIVYEDANI SSKQFTFSKA KDMISKRKNK DFKYISYIIE TDNNELKKKF LTSKNVEDRI
     FYGYLYQQKK NYNLDFNDLI IFTLHILETF PKVRKKWQQK LEYIMVDEFQ DVNIKQYRLV
     SILSEYHKNL FVVGDPDQTV YSWRGANVNL ILNFDKEFKG TKTIMMNQNY RSSSNIIKAS
     NSLISKNKQR IDKELIPIKH GNIPVVYKHS ENIYKEANWI INQIEQIIKG GNSYKNIAIL
     YRAHYVSRSI EEALLKNKIP YTLYSGVEFY QRKEIKDILS YLRMVVFEDD LSFIRIINEP
     KRNFGKKRME IIRKYAEDNN CSLYSSLKIN LEDKLIAKSK ADKFVDLIER YKKIYKEMRI
     TDLLMELLNN SGYEAMLRES GEDERLENLA ELKNSISDYE NSAGEDTTLE DYLQEISLFT
     NSDLKENKDT INMMTLHTAK GLEFPYVFIC EFNEGIFPSA RTNTKEKMEE ERRLAYVGYT
     RAKNALFLSD AEGVNYDGSY RFPSRFIFNT GKTYLNYLVE LKESLIDDAN EFISDSENSM
     NKSNNIKFKI GERIIHKLLG LGVIIGIDND NSSYMIKFDN AETFRNISFS TQLDKADTNN
     LDIIKSNERK AIDHLEAERL EAERKEQERL EAERLEAERK EQERLEAERL EAERKEQERL
     EAERLEAERK EQERLEAERL EAERKEQERL EAERLEAERK EQERLEAEQI EVSTMILKIK
     EEISELEEIV SKNKYKLFGK GAILKKEAKK RIQILYLKID EISN
//
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