ID U3TSM2_9ENTR Unreviewed; 726 AA.
AC U3TSM2;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
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=E05_20540 {ECO:0000313|EMBL:BAN96820.1};
OS Plautia stali symbiont.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae.
OX NCBI_TaxID=891974 {ECO:0000313|EMBL:BAN96820.1, ECO:0000313|Proteomes:UP000016901};
RN [1] {ECO:0000313|EMBL:BAN96820.1, ECO:0000313|Proteomes:UP000016901}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21470838; DOI=10.1016/j.micres.2011.03.001;
RA Kobayashi H., Kawasaki K., Takeishi K., Noda H.;
RT "Symbiont of the stink bug Plautia stali synthesizes rough-type
RT lipopolysaccharide.";
RL Microbiol. Res. 167:48-54(2011).
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}.
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DR EMBL; AP012551; BAN96820.1; -; Genomic_DNA.
DR AlphaFoldDB; U3TSM2; -.
DR KEGG; psts:E05_20540; -.
DR eggNOG; COG0210; Bacteria.
DR HOGENOM; CLU_004585_5_2_6; -.
DR Proteomes; UP000016901; Chromosome.
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:InterPro.
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; IPR013986; DExx_box_DNA_helicase_dom_sf.
DR InterPro; IPR005753; DNA_helicase_ATP-dep_UvrD.
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; TIGR01075; uvrD; 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};
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:UP000016901}.
FT DOMAIN 14..292
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 293..570
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 35..42
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 726 AA; 82290 MW; 84A8FE7992639B65 CRC64;
MLKTVLMDVS DLLNGLNDKQ REAVAAPRSN LLVLAGAGSG KTRVLVHRIA WLLSVENCSP
YSIMAVTFTN KAAAEMRHRI DQLIGTSQGG MWIGTFHGLA HRLLRAHHLD AGLPQDFQIL
DSEDQLRLLK RLIKAMNLDE KQWPARQGMW YINGKKDEGL RPKHIESYGN PVEQTWLRIY
QAYQEACDRA GLVDFAELLL RAHELWLNKP QILNHYRERF SNILVDEFQD TNNIQYAWIR
MLAGDSGRVI IVGDDDQSIY GWRGAQVENI QRFLQDFLGA ETIRLEQNYR STNNILKAAN
ALIANNNGRL GKELWTDGSD GEKISLYCAF NELDEARFAV NRIKTWHENG NALQDCAILY
RSNAQSRVLE EALLQGSIPY RIYGGMRFFE RQEIKDALAY LRLLANRNDD AAFERVVNTP
VRGVGDRTLD VVRQTAREQQ LTLWQATRAL LQSKALAGRA ASALQRFCEL VDALATETAE
LPLHVQTDRV IKDSGLWLMY EQEKGEKGQA RIENLEELVT ATRQFSYQDE DEDLMPLQAF
LSHAALEAGE GQADKWQDAV QLMTLHSAKG LEFSQVFIVG MEEGMFPSQM SLDEGGRLEE
ERRLAYVGVT RAMEKLTLTY AETRRLYGKE VYHRPSRFIG ELPEECVEEV RLRASVSRPV
SHQRMGTPVA KSDSGFALGQ RVRHAKFGEG TIINLEGSGE HSRLQVAFQG QGIKWLVAAY
VRLETV
//
