ID U5Q9U2_9BACT Unreviewed; 948 AA.
AC U5Q9U2;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, 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};
GN Name=pcrA {ECO:0000313|EMBL:AGY54059.1};
GN ORFNames=BRDCF_p1432 {ECO:0000313|EMBL:AGY54059.1};
OS Bacteroidales bacterium CF.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales.
OX NCBI_TaxID=1400053 {ECO:0000313|EMBL:AGY54059.1, ECO:0000313|Proteomes:UP000017642};
RN [1] {ECO:0000313|EMBL:AGY54059.1, ECO:0000313|Proteomes:UP000017642}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF {ECO:0000313|EMBL:AGY54059.1};
RX PubMed=24356833;
RA Tang S., Edwards E.A.;
RT "Complete Genome Sequence of Bacteroidales Strain CF from a Chloroform-
RT Dechlorinating Enrichment Culture.";
RL Genome Announc. 1:e01066-13(2013).
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; CP006772; AGY54059.1; -; Genomic_DNA.
DR AlphaFoldDB; U5Q9U2; -.
DR STRING; 1400053.BRDCF_p1432; -.
DR KEGG; bacc:BRDCF_p1432; -.
DR HOGENOM; CLU_004585_7_0_10; -.
DR Proteomes; UP000017642; 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:UP000017642}.
FT DOMAIN 40..325
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 326..685
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT REGION 565..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 783..887
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..647
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 806..875
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 61..68
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 948 AA; 104792 MW; 463DB27D8059675E CRC64;
MSKPLLNRIW FDIIVKNFAA KIHNIYNFVP MKTDFSTIYE GLNSAQSQAV EQFDGPCLIV
AGAGSGKTRV LTCRIANILD HGHKAGSVLA LTFTNKASKE MKERIASLVG YDVARNLWMG
TFHSVFVKFL REDAELLGFP KSFTIYDTSD SRSAIRACVK ELSLDEKIYK PNEVLSRISM
AKNNLVTPAA YLSNATLAQN DAAAKKPRIG EIYALYHKKF KQAGAMDFDD ILVYTNILLR
DFPQVLEKLR SRFSYILVDE YQDTNYSQYL IVKKLASVHR NLCVVGDDAQ SIYSFRGARI
ENILNFRKDY PEAKEFRLEQ NYRSTQTIVK AANSLIARNS MQIKKECFSS AAEGEKISVM
NAYTDQEEAF MLASSVLARI YQDKASYGDF AVLYRTNAQS RAVEEALRKR SLPYKIYGGH
SFYERAEVKD MISYLRLLLN KKDDEAFRRI VNVPPRGIGD TTVSCLTAAA NSAGVSLWEA
MMEGQMSAMG IKQAAAGKLF QFAKMIAEIS AKVATYNVYD IAMEVLVKSG YMDYLRSDTS
VEGQARLDNV EELMNSIKAF VEEVEETGEI NNDPESAKPA LDSNSSNSSI SSNSSNSSAS
SASSASSASS ASSTSPASST SSTSPLTDDS DLDVQVPDGQ GSNSNPLVSL SNYIENIALL
SAIDENNAPE DSNKISLMTV HSAKGLEFPY VYVVGMEENL FPSGSMSGIK ETDLEEERRL
FYVALTRAKL NVTLSYAQSR FRWGSHVNYP TSRFLREIDP KYLDWPDMKS EMGGDDYNLV
SMSSLSNSGT SRSDNRFRDK SGSGNDDRTT SGNYERSSSG SYDRSAFGSY NRSGSGSHDR
SGSGTWNGSP GSQYRDRAGN PSNDKSSSGD ARNVFRPSTT FRKPADPDFK ADPISKLKVG
LKVEHDRFGF GTLLELEGDA LNAKAIVDFE QGGKKTLLLK FAKLRVVE
//
