ID Q898W6_CLOTE Unreviewed; 743 AA.
AC Q898W6;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 137.
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=CTC_00322 {ECO:0000313|EMBL:AAO34963.1};
OS Clostridium tetani (strain Massachusetts / E88).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=212717 {ECO:0000313|EMBL:AAO34963.1, ECO:0000313|Proteomes:UP000001412};
RN [1] {ECO:0000313|EMBL:AAO34963.1, ECO:0000313|Proteomes:UP000001412}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Massachusetts / E88 {ECO:0000313|Proteomes:UP000001412};
RX PubMed=12552129; DOI=10.1073/pnas.0335853100;
RA Brueggemann H., Baumer S., Fricke W.F., Wiezer A., Liesegang H., Decker I.,
RA Herzberg C., Martinez-Arias R., Merkl R., Henne A., Gottschalk G.;
RT "The genome sequence of Clostridium tetani, the causative agent of tetanus
RT disease.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(2003).
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; AE015927; AAO34963.1; -; Genomic_DNA.
DR RefSeq; WP_011098634.1; NC_004557.1.
DR AlphaFoldDB; Q898W6; -.
DR STRING; 212717.CTC_00322; -.
DR GeneID; 24254047; -.
DR KEGG; ctc:CTC_00322; -.
DR HOGENOM; CLU_007524_0_1_9; -.
DR OrthoDB; 9803432at2; -.
DR Proteomes; UP000001412; 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; 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 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};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01488, ECO:0000313|EMBL:AAO34963.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01488}; Reference proteome {ECO:0000313|Proteomes:UP000001412}.
FT DOMAIN 333..449
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 743 AA; 84694 MW; DD9A1714497CD058 CRC64;
MEEIQGTVDS IIFRNDENGY VVSRIKEDAK AITTIVGCIP YISEGQNLKL QGGWVIHPQF
GRQFKVESCE EIIPDTKKGI ERYLASGVIS GIGPVTAKKI VKEFGLETFD ILENDIERLK
EIDGIGDKKI NIIQEAYKDQ KEVRNIMMFF QEYGISINHC LKIYKKFKGE SIKIVKENPY
VLTENIAGIG FKTADKIARN LGVDVDSPFR IQSGVNYAVN QFSALGNTCM PIDKLIKEGK
EILNVKEEDI KENILQNAFQ GKLRVEIVDG KEYVFSIPYY YCELGVTKNI LKLSLYNHKD
LDMTVEEEIK KFEENNNIEF SPSQREAIMG AFLNGVEIIT GGPGTGKTTI INCISEIYEN
YGYTVCMGAP TGRAAKRMTE ATGRDAKTIH RLLEMGVGEE EVFSKTEETP LECDVVIIDE
ASMIDIMLMN NLLKAISIGT RLIIVGDVDQ LPSVGPGNVL RDLIESNCVK IVRLKDIFRQ
SETSAITVNA HKINNGQMPV LNEREKDFFF LKGDSNEDIL DVLLALVHKR LPNFNKDWDK
LKHIQILSPM RKGLLGVENL NKNLQMVLNP PSKDKKERKF KEYIFRVGDK IMQTKNNYNI
KWKKIDKYNR EEGLGIFNGD IGYIEDIDEE NNNMTIIFDE EKRVIYEDIF LDEIDLAYAI
TIHKSQGSEF PAVIIPTFMG PPMLMNRNLL YTGITRAKEL VVVVGELKAL KFMVDNNRSF
ERYSLLKWRI QNILENFYEN DEQ
//
