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Database: UniProt
Entry: A0A0S2VZH6_9FIRM
LinkDB: A0A0S2VZH6_9FIRM
Original site: A0A0S2VZH6_9FIRM 
ID   A0A0S2VZH6_9FIRM        Unreviewed;       756 AA.
AC   A0A0S2VZH6;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=ATP-dependent RecD-like DNA helicase {ECO:0000256|HAMAP-Rule:MF_01488};
DE            EC=3.6.4.12 {ECO:0000256|HAMAP-Rule:MF_01488};
GN   Name=recD2 {ECO:0000256|HAMAP-Rule:MF_01488};
GN   ORFNames=IB211_00119c {ECO:0000313|EMBL:ALP92515.1};
OS   Intestinimonas butyriciproducens.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Intestinimonas.
OX   NCBI_TaxID=1297617 {ECO:0000313|EMBL:ALP92515.1, ECO:0000313|Proteomes:UP000064844};
RN   [1] {ECO:0000313|EMBL:ALP92515.1, ECO:0000313|Proteomes:UP000064844}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF211 {ECO:0000313|EMBL:ALP92515.1,
RC   ECO:0000313|Proteomes:UP000064844};
RX   PubMed=26620920; DOI=10.1038/ncomms10062;
RA   Bui T.P., Ritari J., Boeren S., de Waard P., Plugge C.M., de Vos W.M.;
RT   "Production of butyrate from lysine and the Amadori product fructoselysine
RT   by a human gut commensal.";
RL   Nat. Commun. 6:10062-10062(2015).
RN   [2] {ECO:0000313|Proteomes:UP000064844}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF211 {ECO:0000313|Proteomes:UP000064844};
RA   de Vos W.M., Bui N.T.P., Plugge C.M., Ritari J.;
RT   "A butyrogenic pathway from the amino acid lysine in a human gut
RT   commensal.";
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: DNA-dependent ATPase and ATP-dependent 5'-3' DNA helicase.
CC       Has no activity on blunt DNA or DNA with 3'-overhangs, requires at
CC       least 10 bases of 5'-ssDNA for helicase activity. {ECO:0000256|HAMAP-
CC       Rule:MF_01488}.
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|HAMAP-Rule:MF_01488};
CC   -!- SIMILARITY: Belongs to the RecD family. RecD-like subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01488}.
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DR   EMBL; CP011307; ALP92515.1; -; Genomic_DNA.
DR   RefSeq; WP_058116773.1; NZ_CP011307.1.
DR   AlphaFoldDB; A0A0S2VZH6; -.
DR   STRING; 1297617.IB211_00119c; -.
DR   KEGG; ibu:IB211_00119c; -.
DR   PATRIC; fig|1297617.4.peg.118; -.
DR   Proteomes; UP000064844; Chromosome.
DR   GO; GO:0043139; F:5'-3' DNA helicase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   CDD; cd17933; DEXSc_RecD-like; 1.
DR   CDD; cd18809; SF1_C_RecD; 1.
DR   Gene3D; 1.10.10.2220; -; 1.
DR   Gene3D; 2.30.30.940; -; 1.
DR   Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   HAMAP; MF_01488; RecD_like; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR006345; DNA_helicase_RecD-like.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR029493; RecD-like_HHH.
DR   InterPro; IPR041451; RecD-like_SH13.
DR   InterPro; IPR010994; RuvA_2-like.
DR   InterPro; IPR027785; UvrD-like_helicase_C.
DR   NCBIfam; TIGR01448; recD_rel; 1.
DR   PANTHER; PTHR43788; DNA2/NAM7 HELICASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR43788:SF6; RECBCD ENZYME SUBUNIT RECD; 1.
DR   Pfam; PF13604; AAA_30; 1.
DR   Pfam; PF14490; HHH_4; 1.
DR   Pfam; PF14520; HHH_5; 1.
DR   Pfam; PF18335; SH3_13; 1.
DR   Pfam; PF13538; UvrD_C_2; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF47781; RuvA domain 2-like; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_01488}; DNA-binding {ECO:0000256|HAMAP-Rule:MF_01488};
KW   Helicase {ECO:0000256|HAMAP-Rule:MF_01488, ECO:0000313|EMBL:ALP92515.1};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01488};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_01488}; Reference proteome {ECO:0000313|Proteomes:UP000064844}.
FT   DOMAIN          350..494
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   BINDING         361..365
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01488"
SQ   SEQUENCE   756 AA;  84121 MW;  6CC1DF56A309F68F CRC64;
     MIHRGTYDGT IYHNPVNKFC IISVKTADKE VPQEARSTHR YKDHLIRFVA TGYELPRTDA
     VELELDGEWT KGKYGVQLQV EQWREIVPKT KSGVEGYLAS GLIKGIGPAT AAQIVSRFGV
     ETLDILQNHP ERLLEIKGIT EGKLEDIKSS YAESRMLQDL MTLLSPFKIT PKTALKIYQH
     FGPASVDILK KSPFELCQIS GFGFLRVDGI IQKNGGDLHD PMRVKGALFC ALGDSKSGKG
     HLYLPADALK KAALRLLNAK IPVAGLRLHE PEVAEMLQTM ILNGDMVSVK DNIYLPRVFA
     QEDSVAREIA KRLIERPAPE LIGQALEQVK REIGLALSPK QEAAVYAAFR HNLSIITGSP
     GTGKTTVLKT ILEVYRRLQP SGAVSLMAPT GRASRRMAES TGFDKARTLH SGLGLSSEEE
     DSHGRAQEPL SADLIIVDEF SMVDMWLADK FFSRIKEGAR IVLVGDPDQL PSVGAGNVFR
     ELIGCGLIPV TVLDQIFRQS GDSLIAYNAR YINEGSTKLN YGPDFVFLAS DSQSQTAERI
     IARYCQEISE RGIDRVQILS PFRSEGAASA DLLNEAIREV VNPFRSSEEE VKVGTRVFRV
     NDRIMQTKNT DKVSNGDLGF IRYIKDGENG KRIGMDFGVG REIEYSMEDM ANLDLAYATT
     VHKSMGSEYE TVIMPILKAH NIILYRNLLY TGITRARKRV VMIGQKQALY MAINRNEISK
     RNTLLGERIR LYYKAYAKRF GVPLPEALKN ELKHAG
//
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