ID A0A1M6T3Y7_9FIRM Unreviewed; 740 AA.
AC A0A1M6T3Y7;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=ATP-dependent DNA helicase {ECO:0000256|RuleBase:RU364053};
DE EC=5.6.2.4 {ECO:0000256|RuleBase:RU364053};
GN ORFNames=SAMN02745243_03116 {ECO:0000313|EMBL:SHK51634.1};
OS Hespellia stercorisuis DSM 15480.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Hespellia.
OX NCBI_TaxID=1121950 {ECO:0000313|EMBL:SHK51634.1, ECO:0000313|Proteomes:UP000184301};
RN [1] {ECO:0000313|EMBL:SHK51634.1, ECO:0000313|Proteomes:UP000184301}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15480 {ECO:0000313|EMBL:SHK51634.1,
RC ECO:0000313|Proteomes:UP000184301};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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 ECO:0000256|RuleBase:RU364053};
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, ECO:0000256|RuleBase:RU364053}.
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DR EMBL; FQZY01000055; SHK51634.1; -; Genomic_DNA.
DR RefSeq; WP_073112117.1; NZ_FQZY01000055.1.
DR AlphaFoldDB; A0A1M6T3Y7; -.
DR STRING; 1121950.SAMN02745243_03116; -.
DR OrthoDB; 9810135at2; -.
DR Proteomes; UP000184301; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IEA:InterPro.
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; IPR005751; ATP-dep_DNA_helicase_PcrA.
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 NCBIfam; TIGR01073; pcrA; 1.
DR PANTHER; PTHR11070:SF2; ATP-DEPENDENT DNA HELICASE SRS2; 1.
DR PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR Pfam; PF21196; PcrA_UvrD_tudor; 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}; DNA-binding {ECO:0000256|RuleBase:RU364053};
KW Helicase {ECO:0000256|PROSITE-ProRule:PRU00560,
KW ECO:0000256|RuleBase:RU364053};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00560,
KW ECO:0000256|RuleBase:RU364053};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00560}; Reference proteome {ECO:0000313|Proteomes:UP000184301}.
FT DOMAIN 5..285
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 286..562
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 26..33
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 740 AA; 83945 MW; 427A8AE9BD83A755 CRC64;
MDKYGTLNAQ QQEAVFHVDG PLLILAGAGS GKTRVLTHRI AYLIEEKGVN PWNILAITFT
NKAAGEMRER VDQLVGFGSE SIWVSTFHST CVRILRRHID LLGYDNNFTI YDGDDQKTLM
KDVCKLINID TKVYKERNLL AAISSAKDEM ISPDEYEVNA AGDFSKLKIA KVYREYEKQL
RANNALDFDD LLVKTVQLLQ TQPDVLDYYQ ERFRYIMVDE YQDTNTVQFR LISTLAGKYK
NLCVVGDDDQ SIYKFRGANI KNILNFEKEF DHARVIKLEQ NYRSTSTILD AANAVIRNNY
GRKDKTLWTD NGEGDKIRLR QFDSAYDEAE YIVGDIKSHV DNGLGSYNDH AILYRTNAQS
RIFEEKFVVA NIPYRIVGGV NFYARREIKD LLAYLKTIDN GKDDLAVRRI INVPKRGIGL
TTINRVQESA AEREIGFYEA LGGLDLIPGV GRGAAKLESF VALIEYFKSR AAVCGVSDLM
QEIIEKTGYV ENLEAEDTEE AKARIENIDE LVSKIVSYEE SCEDEQPTLS GFLEEVALVA
DIDSLDESTD YVVLMTLHSA KGLEFPHVYL SGMEDGIFPS YMTITADDPD EIEEERRLCY
VGITRAREEL TLTCARRRMV RGETQYNKMS RFLKEIPAHL MTTGNLIEEE PEVPAQKAYF
QAKQSFHAKA FSASKQPRQF TVVQGKGLNF DVGDRVRHKK FGEGLVTGIA EGGRDYEVTV
EFDHVGVKKM FASFAKLERI
//