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Database: UniProt
Entry: A0A160IIN1_9BACI
LinkDB: A0A160IIN1_9BACI
Original site: A0A160IIN1_9BACI 
ID   A0A160IIN1_9BACI        Unreviewed;       728 AA.
AC   A0A160IIN1;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE            EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN   ORFNames=ABE65_003040 {ECO:0000313|EMBL:ANC75843.1};
OS   Fictibacillus phosphorivorans.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Fictibacillus.
OX   NCBI_TaxID=1221500 {ECO:0000313|EMBL:ANC75843.1, ECO:0000313|Proteomes:UP000076623};
RN   [1] {ECO:0000313|EMBL:ANC75843.1, ECO:0000313|Proteomes:UP000076623}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G25-29 {ECO:0000313|EMBL:ANC75843.1,
RC   ECO:0000313|Proteomes:UP000076623};
RA   Zheng Z.;
RT   "Complete genome sequence of Fictibacillus phosphorivorans G25-29, a strain
RT   toxic to nematodes.";
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
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; CP015378; ANC75843.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A160IIN1; -.
DR   STRING; 1221500.ABE65_003040; -.
DR   KEGG; fpn:ABE65_003040; -.
DR   Proteomes; UP000076623; Chromosome.
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:0003678; F:DNA helicase activity; IEA:InterPro.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
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}; Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00560}.
FT   DOMAIN          14..307
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   DOMAIN          308..570
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51217"
FT   COILED          524..554
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         35..42
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ   SEQUENCE   728 AA;  84234 MW;  B98C92A2F5A89ACA CRC64;
     MGDFFTKMKN DLGITLNEVQ KKAVMKTEGP LLLLASPGSG KTTTIIMRIG YLIMEKGIQP
     SRIKAVTFSK ASANDMKERF TRFYPELPAV DFSTIHSFAF EVVRDHYRKL GLPFTIIEGE
     SDSGEKEGSA GNFQHNKKMM LRHLFKSLVG ENITEDQMDE LTTYISYIKN KMIPIERWSE
     VSCDVPQAEE IFKQYEELKR SDQHHVLLDF DDMLTIGNDV LENHAHVLRY YQNRYDYFLT
     DESQDTSLVQ HSIIEKMVST HRNLCVVADD DQSIYSWRGA EPSYLLKFKE KYSDASILFM
     EQNYRSSEDI VTVANSFIKR NKNRYEKNMF TQNPSHQPVE VKQLVNFKEQ SKYLVSELSD
     AIHLKEIAIL YRNNSSSIGL MNDFDRSGIP FYMKDADNRF FSHWVVQDIL NFMRMAFTDK
     RPDILEKIHL KFNGYITKQQ MQALKQLNHN DSVFDNLLNH VKLQEYQVKL LKASKETFKE
     MKEMKPLQAI RVIRDRLGYD KAIEKISKSL GFRMDYLVGI LNTLEEIATD LESLEEFAKR
     LKHLEVVLKT AKKKKGHDAI TLSTFHSAKG LEFNKVFMID VVDGIIPSSE DRSDHLLLEE
     AARLFYVGMT RAKKQLTLVT YPYRDGKKVE ESVFVSDVKN ILDPTRIMKS EPVKKNVKKI
     NGVPYNPYSI KKKEELYVGL AVTHRVFGTG EITEISGEFI TFKFQSKEKK LSISACLEMG
     LLEPLIHT
//
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