ID A0A0W0XW96_9GAMM Unreviewed; 729 AA.
AC A0A0W0XW96;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
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 Name=uvrD {ECO:0000313|EMBL:KTD48644.1};
GN ORFNames=Lrub_0995 {ECO:0000313|EMBL:KTD48644.1};
OS Legionella rubrilucens.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=458 {ECO:0000313|EMBL:KTD48644.1, ECO:0000313|Proteomes:UP000054608};
RN [1] {ECO:0000313|EMBL:KTD48644.1, ECO:0000313|Proteomes:UP000054608}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WA-270A-C2 {ECO:0000313|EMBL:KTD48644.1,
RC ECO:0000313|Proteomes:UP000054608};
RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA Pupko T., Shuman H.A., Segal G.;
RT "Genomic analysis of 38 Legionella species identifies large and diverse
RT effector repertoires.";
RL Submitted (NOV-2015) 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:KTD48644.1}.
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DR EMBL; LNYT01000007; KTD48644.1; -; Genomic_DNA.
DR RefSeq; WP_058531094.1; NZ_LNYT01000007.1.
DR AlphaFoldDB; A0A0W0XW96; -.
DR STRING; 458.Lrub_0995; -.
DR PATRIC; fig|458.5.peg.1031; -.
DR OrthoDB; 9806690at2; -.
DR Proteomes; UP000054608; 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 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; 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; 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};
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}; Reference proteome {ECO:0000313|Proteomes:UP000054608}.
FT DOMAIN 8..286
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 287..565
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 29..36
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 729 AA; 81614 MW; 9D400C0EEC6CDA26 CRC64;
MTVDALLKGL NDRQRQAVVA PLGNTLVLAG AGSGKTRVLV SRIAWLIQEH HFSPHSILAV
TFTNKAAGEM KARLSHLLPV SLAGFWVGTF HGLCHRILRR HHQDAHLPAE FHILDSEDQA
RVIKRVIAAL NLDDDQWPVK QAQAFINGKK DEGLRPQHIH AQSFGPTRTL IQIYQAYEQA
CQTAGVVDFA ELLLRTHELL RDNPDILQHY QHRFGAILVD EFQDTNTIQY AWIRLLAGQG
ASVMAVGDDD QSIYGWRGAK VGNIQQFPRD FNNTLVVRLE QNYRSTATIL DAANALISNN
QSRMGKELWT DGSAGEKIIV YAAFNELDEA RFISERIQMA IHDGRSADEI AILYRSNAQS
RVIEEALLRA GIAYRIYGGV RFFERAEIKD TLAYLRLLAN PDDDTAFERV VNFPTRGIGE
KTLDELRQLA RNRQGSLWQA AGELLAQGAL PQRAASALEK FTHLIRGLQT KTQYLELDEQ
ISEVINGSGL YAHFSKIKGD KSESRLDNLQ ELINAAKQFR YEQDVDEEFP LLVAFLAHAS
LEAGEMQAAE HERYVHLMTL HAAKGLEFPM VFLAGMEEGV FPGKQSIEEP DRLEEERRLC
YVGMTRAMEK LLLSYAEVRR QYGREEYHRP SRFLRELPAE LLDEVRVKAH YQSAPSASPR
SSSVAAVAAS DAGLKLGQNV SHAKFGQGVV VSVEGSGAHT RVQIKFADHG VKWLVLAYAN
LTIAENCSF
//
