ID A0A1W9L1M0_9GAMM Unreviewed; 638 AA.
AC A0A1W9L1M0;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
DE AltName: Full=DNA 3'-5' helicase II {ECO:0000256|ARBA:ARBA00034923};
GN ORFNames=BWK79_17135 {ECO:0000313|EMBL:OQW91333.1};
OS Beggiatoa sp. IS2.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Thiotrichaceae; Beggiatoa.
OX NCBI_TaxID=1934247 {ECO:0000313|EMBL:OQW91333.1, ECO:0000313|Proteomes:UP000192324};
RN [1] {ECO:0000313|EMBL:OQW91333.1, ECO:0000313|Proteomes:UP000192324}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IS2 {ECO:0000313|EMBL:OQW91333.1};
RA Sharrar A.M., Flood B.E., Bailey J.V., Jones D.S., Biddanda B.,
RA Ruberg S.A., Marcus D.N., Dick G.J.;
RT "Novel large sulfur bacteria in the metagenomes of groundwater-fed
RT chemosynthetic microbial mats in the Lake Huron basin.";
RL Submitted (JAN-2017) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OQW91333.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MTEL01000570; OQW91333.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W9L1M0; -.
DR Proteomes; UP000192324; Unassembled WGS sequence.
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 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};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|PROSITE-
KW ProRule:PRU00560};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU00560};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00560}.
FT DOMAIN 6..289
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 290..564
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 27..34
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 638 AA; 74177 MW; EEBD716437E92014 CRC64;
MTLDLSSLNE NQLAAVNWQD NVLLVLAGPG SGKTRVLTYR IARIIAETAD QHFAILALTF
TNKAAAEMRE RLTKLIPNVT ERVEVTTFHS FAASLLRQHG SHIGLRPDFT ILNQEEDQKA
ILQEVLSKRD MENYSSEKLL PLINKLLQYG VLVENAKSIL LKNKLGEEQA ELLTQVYSSY
CSQSIQNNCL DFGNLIIQAT TLLQNKPFIQ KFLHRIYYHV CVDEFQDTNR AQYHLLRQLV
NPERQNLFIV ADDDQIMYQW NGASPERLKN LQDDYQTTLI QLPENYRCPS EVIDLANRLI
SHNPRRHSDK LKIQAHRQVS ASDPIRIQEK FVTFEEEAKW IANDIAHRSD KAGCVVLARS
KSLLEIIVTE LEKLSIPAYL HKRKDEFEST PLVWLHAMLR LANTRHDKKQ LYRVCKAFYQ
LEGIKIEPET VESLAITQNN NDDYLRTWHI LVTERNELSE QAKQILTESV SKLMDRLDFD
SFIKKTFNWF DTLKSGDIQL QQETFIDYEE EKKTWQELQT EIEGQYGREQ VTLYLLLQEI
DLRSKKPSPP KNAIPCFTVH ASKGMEFKHV YLAGMVEEHF PSWQAIKKGD NSSEMEEERR
NCFVAITRTQ ETLTLTYSEK IFEWNKQPSR FLKEMGFS
//
