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Database: UniProt
Entry: Q81GH7_BACCR
LinkDB: Q81GH7_BACCR
Original site: Q81GH7_BACCR 
ID   Q81GH7_BACCR            Unreviewed;       688 AA.
AC   Q81GH7;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 121.
DE   RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE            EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN   OrderedLocusNames=BC_1223 {ECO:0000313|EMBL:AAP08208.1};
OS   Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS   15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=226900 {ECO:0000313|EMBL:AAP08208.1, ECO:0000313|Proteomes:UP000001417};
RN   [1] {ECO:0000313|EMBL:AAP08208.1, ECO:0000313|Proteomes:UP000001417}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB
RC   9373 / NCTC 2599 / NRRL B-3711 {ECO:0000313|Proteomes:UP000001417};
RX   PubMed=12721630; DOI=10.1038/nature01582;
RA   Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA   Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA   Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA   Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.;
RT   "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT   anthracis.";
RL   Nature 423:87-91(2003).
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; AE016877; AAP08208.1; -; Genomic_DNA.
DR   RefSeq; NP_831007.1; NC_004722.1.
DR   RefSeq; WP_000191201.1; NZ_CP034551.1.
DR   AlphaFoldDB; Q81GH7; -.
DR   KEGG; bce:BC1223; -.
DR   PATRIC; fig|226900.8.peg.1193; -.
DR   HOGENOM; CLU_004585_6_1_9; -.
DR   OrthoDB; 9810135at2; -.
DR   Proteomes; UP000001417; 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:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000725; P:recombinational repair; IBA:GO_Central.
DR   CDD; cd17932; DEXQc_UvrD; 1.
DR   CDD; cd18807; SF1_C_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}; Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00560}; Reference proteome {ECO:0000313|Proteomes:UP000001417}.
FT   DOMAIN          49..323
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   DOMAIN          324..601
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51217"
FT   COILED          620..654
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         70..77
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ   SEQUENCE   688 AA;  79700 MW;  50547BC30993B2A6 CRC64;
     MTQEKFSQKS LTHADIPRAT YHIPKTSTHL IMEEDVDAAY FRALEQQNVF LNEKQLEAVR
     TTEGPVLTLA GAGSGKTSVL TTRVGYLVNV KQVHPRNILL LTFTQKAAEE IRSRVAKLPG
     MNHAASSYVV AGTFHSVFLK LLRSQGYNQQ ILANEKHKQI MIKKILKELR LKDDYDAETM
     LAMISLEKNK LNRPKDVKAK TPVEQEFKEV YERFEEVKQR YNYIDFDDIL LETYYMLENN
     APLLTQLQQR FHYIEVDEFQ DTSYAQYEIV KLLATPRNNL FIAGDDDQAI YGWRGASHQI
     ILSFPKEFDN TTIIALNTNY RSNPFIVGLG NEVIKLNQER FDKELYSVRE EGVQPFYARP
     ATTLDEANQI LQLIQEKVDS GERNYKDFCL LYRTHSVSRS LLDQLTIHKI PFIKHGASQS
     FYEHSLIKPV LDHLRLVIEP FRLESLSNIL PTMYIGRDDC ISFIEREQWK YGEGRFPSLL
     HFLLLNPSLK PFQVKKVNER IDFIKFIKEL EPKKALKEII HGKGKYLEYL QSNDRSSFTM
     HKDIQEEMLE ELMESATRFT DIPAYLQFID EAIQGQKEME ALKTMPQKDA VSLMSIHNAK
     GLEFPCVFLL GASDGILPHT SSLKDANDRI TETSEALEEE RRLLYVAITR AKEELYISSP
     QFFRGKKLDI SRFLYTVRKD LPEKTSTK
//
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