ID A0A249SSJ0_9BACT Unreviewed; 777 AA.
AC A0A249SSJ0;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-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};
GN ORFNames=CK934_06355 {ECO:0000313|EMBL:ASZ10625.1};
OS Chitinophaga sp. MD30.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Chitinophaga.
OX NCBI_TaxID=2033437 {ECO:0000313|EMBL:ASZ10625.1, ECO:0000313|Proteomes:UP000217148};
RN [1] {ECO:0000313|EMBL:ASZ10625.1, ECO:0000313|Proteomes:UP000217148}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD30 {ECO:0000313|EMBL:ASZ10625.1,
RC ECO:0000313|Proteomes:UP000217148};
RA Wan X., Darris M., Hou S., Donachie S.P.;
RT "Draft genome sequence of a novel Chitinophaga sp., MD30, isolated from a
RT biofilm in an air conditioner condensate pipe.";
RL Submitted (AUG-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}.
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DR EMBL; CP023254; ASZ10625.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A249SSJ0; -.
DR OrthoDB; 9810135at2; -.
DR Proteomes; UP000217148; 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 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}; Reference proteome {ECO:0000313|Proteomes:UP000217148}.
FT DOMAIN 7..292
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 293..574
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT REGION 686..723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 694..708
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 28..35
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 777 AA; 88463 MW; 6ACF98B462B33C8A CRC64;
MKANYLDELN ERQREAVAHI NGPLMIVAGA GSGKTKVLTT RIAHLMRNGV DAFNILSLTF
TNKAAREMKE RVERILGGSE ARNLYIGTFH SVFARLLRAE AHRLGYPNDF TIYDSDDAKS
VLKTIINEQN LDDKHYKPNF VYNRISAAKN SLMSPEEYQH DYYVQQEDMR ANRPMIGKLY
DMYAKRCFKN GAMDFDDLLY KMYVLLKNFP EVLHKYQHKF KYIMIDEYQD TNPAQYEIIK
LLGAVHENIC VVGDDAQSIY SFRGATIENI LQFEKDYEDV RVVKLEQNYR STKSILNVAN
EVIQHNKGQI EKNLWTDNAD GEKIKLIRTM TDNDEGKFVA DTIAEQKLRN HYDNKDFVIL
YRTNAQSRSF EENLRRKAIP YRILGGMSFY QRKEIKDFVA YLRVTMNTQD EESIKRIINY
PVRGIGKTTI EKTVVLSNEH NITFWEVLNR AKEFGFKGGT LEAIDGFVTM IQSFQANLTK
HNAYDVAVQV GKSTNIVKEL FNDKTTEGLA RYENIQELLN SIKEFTETPT EDGELLDKSL
GSYLQQITLL TDADQGKDEN SDVVKLMTIH AAKGLEFPVV FTVGLEETLF PSQMSVNTRE
ELEEERRLFY VAITRAKSRL WLTYANSRYR FGNLVQNEAS RFLEEMPEQY IDRSYAGGGA
IRNSFGGGGG QWGSGNNMFD RMQKKTPVTQ APATGPKPAG PRPSAPAGNH VPSPGFTPDD
PATMEVGMEV EHQKFGFGTI QGLEGAPNNR IATVVFPKGG GEKKIMLNYA KLMIVKK
//
