ID A0A127JWP2_9BURK Unreviewed; 797 AA.
AC A0A127JWP2;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=UC35_18270 {ECO:0000313|EMBL:AMO24426.1};
OS Ramlibacter tataouinensis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Ramlibacter.
OX NCBI_TaxID=94132 {ECO:0000313|EMBL:AMO24426.1, ECO:0000313|Proteomes:UP000070433};
RN [1] {ECO:0000313|EMBL:AMO24426.1, ECO:0000313|Proteomes:UP000070433}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5-10 {ECO:0000313|EMBL:AMO24426.1,
RC ECO:0000313|Proteomes:UP000070433};
RX PubMed=24425747; DOI=10.1099/ijs.0.058396-0;
RA Lee H.J., Lee S.H., Lee S.S., Lee J.S., Kim Y., Kim S.C., Jeon C.O.;
RT "Ramlibacter solisilvae sp. nov., isolated from forest soil, and emended
RT description of the genus Ramlibacter.";
RL Int. J. Syst. Evol. Microbiol. 64:1317-1322(2014).
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; CP010951; AMO24426.1; -; Genomic_DNA.
DR RefSeq; WP_061502198.1; NZ_CP010951.1.
DR AlphaFoldDB; A0A127JWP2; -.
DR PATRIC; fig|94132.3.peg.3734; -.
DR OrthoDB; 5905204at2; -.
DR Proteomes; UP000070433; Chromosome.
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; 3.
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:UP000070433}.
FT DOMAIN 13..290
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 291..613
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT REGION 543..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 34..41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 797 AA; 88864 MW; E30BCB21F622111D CRC64;
MFPEVESSSP LLANLNPEQL AAVTLPNEHA LILAGAGSGK TRVLTTRIAW LLSTGQVSPG
GVMAVTFTNK AAKEMMTRLQ AMLPVNVRGM WIGTFHGLCN RFLRAHWRLA NLPQSFQILD
TQDQLSAVKR VIKQFNVDEE RFPAKEMQWF ISGCKEDGLR PSMVELRGED VRKKVEIYQL
YEDQCQREGV VDFGELMLRS YEIMRDDDPL HEHYRRRFRH ILIDEFQDTN RLQYAWIKMF
AGEHNSVFAV GDDDQSIYAF RGARVGNMAD FVSEFQVRHQ IKLEQNYRSH SNILDSANEL
IRHNQRRLGK NLRTTQGPGE PVRVYEAPTD LAEAQWIVEE LRHLVRGEGP REGFPRNEIA
VLYRSNAQSR VIETALFNAG VPYRVYGGLR FFERAEIKHA LAYLRLLENP HDDTSFLRVV
NFPPRGIGAR SIEQLQDAAR ARGCSLHDAA GATTGRAGAN LAAFIGRIVA LRERTRDLTL
RETIELMLGE SGLIEHYKTE REGADRIENL EELVNAAESF VTQEGFGRDA IALPVDELAP
GALTQSPVSQ GLDPSLPEAN QPAPDYVAPD ADTGETLSPL AAFLTHAALE SGDNQAQAGQ
DAVQLMTVHS AKGLEFDCVF ISGLEEGLFP SERSMADHDG LEEERRLMYV AITRARKRLY
LSHSQTRLLH GQTRYNVRTR FFDELPEGAL KWLTPKDPGF GRSAFGYGSG YPTTRQYGGG
GGGAYSGERF ASPPVPQQKA APSHGLKAGM KVFHTKFGEG TIASLEGQGD DARAQVNFPR
HGVKWLALAV AKLTPVD
//
