ID A0A159Z6F8_9RHOB Unreviewed; 881 AA.
AC A0A159Z6F8;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-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 ORFNames=AKL17_2840 {ECO:0000313|EMBL:AMY70078.1};
OS Frigidibacter mobilis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Frigidibacter.
OX NCBI_TaxID=1335048 {ECO:0000313|EMBL:AMY70078.1, ECO:0000313|Proteomes:UP000076128};
RN [1] {ECO:0000313|EMBL:AMY70078.1, ECO:0000313|Proteomes:UP000076128}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cai42 {ECO:0000313|Proteomes:UP000076128};
RA Geng S., Pan X., Wu X.;
RT "Complete genome sequence of Defluviimonas alba cai42t isolated from an
RT oilfield in Xinjiang.";
RL Submitted (SEP-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}.
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DR EMBL; CP012661; AMY70078.1; -; Genomic_DNA.
DR RefSeq; WP_066814182.1; NZ_CP012661.1.
DR AlphaFoldDB; A0A159Z6F8; -.
DR STRING; 1335048.AKL17_2840; -.
DR KEGG; daa:AKL17_2840; -.
DR PATRIC; fig|1335048.3.peg.2955; -.
DR OrthoDB; 9806690at2; -.
DR Proteomes; UP000076128; 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; 3.30.160.800; -; 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; 2.
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 39..319
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 320..676
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT REGION 384..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 60..67
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 881 AA; 96871 MW; 5F994DD7E81A0B58 CRC64;
MSRFDEDDAF EGAATAVSQS LSQRAMAGVA GARGTAYLDD LNPAQREAAE ALDGPLLMLA
GAGTGKTKTL MARIANLVVS GRARPNEILA VTFTNKAARE MRERLARQPF QVLEPLRWMG
TFHSISVKIL RRHAELAGLK SNFTILDTDD QIRLMKQVIN AANIDEKRWP ARQLAGIIDG
WKNRALTPSN VPSSEAAAFN NRGTELYAAY QDRLRSLNAA DFGDLLLYVV EIFKAYPDLL
TEYQQKFRYI LVDEYQDTNV AQYLWLRLLA QGHRNICCVG DDDQSIYGWR GAEVGNILRF
EKDFPGARVI RLEQNYRSTG HILAAASGII AKNAGRLGKT LWTAGGLGEK VRLIGRWDGE
EEARWIGEEA EALQRGSSVI ANRRSNARSK TSIQESERLA KGGRVSQNAA GDIHVSNLMR
EQSLTPAGAG NIPIPRGFGL DEMAILVRGS SQMRAFEDRF LTIGLPYRVV GGPRFYERAE
IRDAMAYFRL AVSPTDDLAF ERIVNTPKRG LGDKAQQVIQ MTARADETSL LEGARYAVAS
GKLGGKGAAE LRRFVENVDR WHKAIAAASP ATARNPADDD DELIELDEAS VPSAHDHAHV
RLAEEILEES GYIAMWQNDK TPEAAGRLEN LKELVKALEQ FENLQGFLEH VALISENSSE
EESEKITIMT LHAAKGLEFP VVFLPGWEDG LFPSQRSMDE SGQKGLEEER RLAYVGITRA
EELCTISFAG NRQVYGRWQS QMPSRFIDEL PEADVEVLTP PGLYGGGYGA AAGFGGNAGG
SSVEARATKA DVYNSPGWRR LQDRAGNRPV SQPRESRHTV IDLDAVSAFD VGDRVFHQKF
GYGHVQEIEG DKLAVAFDKA GTKKIVAGFV VAAADADDVP F
//
