ID F4LWV3_TEPAE Unreviewed; 733 AA.
AC F4LWV3; L0S2F7;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 68.
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 OrderedLocusNames=TEPIRE1_1821 {ECO:0000313|EMBL:CCP26619.1};
OS Tepidanaerobacter acetatoxydans (strain DSM 21804 / JCM 16047 / Re1).
OC Bacteria; Bacillota; Clostridia; Thermosediminibacterales;
OC Tepidanaerobacteraceae; Tepidanaerobacter.
OX NCBI_TaxID=1209989 {ECO:0000313|EMBL:CCP26619.1, ECO:0000313|Proteomes:UP000010802};
RN [1] {ECO:0000313|Proteomes:UP000010802}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Re1 {ECO:0000313|Proteomes:UP000010802};
RX PubMed=23469343; DOI=10.1128/genomeA.00213-12;
RA Manzoor S., Bongcam-Rudloff E., Schnurer A., Muller B.;
RT "First genome sequence of a syntrophic acetate-oxidizing bacterium,
RT Tepidanaerobacter acetatoxydans strain Re1.";
RL Genome Announc. 1:E00213-E00213(2013).
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; HF563609; CCP26619.1; -; Genomic_DNA.
DR RefSeq; WP_013778747.1; NC_019954.2.
DR AlphaFoldDB; F4LWV3; -.
DR STRING; 1209989.TepRe1_1689; -.
DR KEGG; tae:TepiRe1_1821; -.
DR KEGG; tep:TepRe1_1689; -.
DR PATRIC; fig|1209989.3.peg.2098; -.
DR eggNOG; COG0272; Bacteria.
DR eggNOG; COG0507; Bacteria.
DR HOGENOM; CLU_007524_0_3_9; -.
DR OrthoDB; 9803432at2; -.
DR Proteomes; UP000010802; 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 GO; GO:0006281; P:DNA repair; IEA:InterPro.
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; IPR003583; Hlx-hairpin-Hlx_DNA-bd_motif.
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; PF13245; AAA_19; 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 SMART; SM00278; HhH1; 3.
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:CCP26619.1};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01488, ECO:0000313|EMBL:CCP26619.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01488}; Reference proteome {ECO:0000313|Proteomes:UP000010802}.
FT DOMAIN 83..104
FT /note="Helix-hairpin-helix DNA-binding motif class 1"
FT /evidence="ECO:0000259|SMART:SM00278"
FT DOMAIN 118..137
FT /note="Helix-hairpin-helix DNA-binding motif class 1"
FT /evidence="ECO:0000259|SMART:SM00278"
FT DOMAIN 182..201
FT /note="Helix-hairpin-helix DNA-binding motif class 1"
FT /evidence="ECO:0000259|SMART:SM00278"
FT DOMAIN 333..451
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT BINDING 344..348
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01488"
SQ SEQUENCE 733 AA; 83237 MW; E4C26B35F5B9D129 CRC64;
MIELEGVVER ITYYNEENGF TVAKITVKDN DDLITAIGYF HCLEVGEVLK LRGNWTIHKD
YGHQFKVEFY ETIMPATVRG IENYLASGVI RGIGPTMAKK IVKEFGEKTL EVLSNSPEKL
LSVPGIGEKK LKMITESYSQ QQETRDIMLF LQEYGIGPNV AVKIYKNYKE KSIQILKQNP
YRLADEVYGI GFKTADYIAQ KMGMERDSME RLCAGLKYAV VKAADEGHVF MPLEELLYKA
SELLSVEKEP LNQAFLALEE KKDIVVERAW GREDVYLAAF YYSEKAVARR LFLLAAMIDE
PLEITDETIN EIEKCCNIRL AKRQREAIEK AAQHGVLVIT GGPGTGKTTT IQSLLEFFKK
QELKVALAAP TGRAAKRMVE TTGVEAKTIH RLLEYNAYEQ GGMAFGKNQD DPLDEDVIIV
DEMSMVDIIL MHHLLSAVRP GARLILVGDK DQLPSVGPGS VLREIIESDK IPVVVLDEIF
RQAQESMIIV NAHRINKGYF PYINVKDKDF FFEQVLLPED ILETILEMTK NRLPNYGDFD
PLEDIQVITP MKKGLVGVAN LNDKLQFLLN PPSRRKKEYH YRACVFREGD KVMQIKNNYD
KEVFNGDLGR IVRIDDEDVV IVSFADAWQE REVAYQGQEI EELSLAYALS VHKSQGSEFP
VVIMPITTSH YVMLQRNLLY TAVTRAKKLI VLVGTKQALT IAIQNNRSLR RYGHLSDRII
DEFSQAIFRD GSI
//
