ID A0A0X7BC52_9FLAO Unreviewed; 777 AA.
AC A0A0X7BC52;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-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};
GN Name=pcrA_2 {ECO:0000313|EMBL:KVV14722.1};
GN ORFNames=AP058_01775 {ECO:0000313|EMBL:KVV14722.1};
OS Flavobacterium sp. TAB 87.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1729581 {ECO:0000313|EMBL:KVV14722.1, ECO:0000313|Proteomes:UP000059935};
RN [1] {ECO:0000313|EMBL:KVV14722.1, ECO:0000313|Proteomes:UP000059935}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TAB87 {ECO:0000313|EMBL:KVV14722.1,
RC ECO:0000313|Proteomes:UP000059935};
RA Gilbert D.G.;
RL Submitted (OCT-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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KVV14722.1}.
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DR EMBL; LLWK01000036; KVV14722.1; -; Genomic_DNA.
DR RefSeq; WP_066309273.1; NZ_LLWK01000036.1.
DR AlphaFoldDB; A0A0X7BC52; -.
DR STRING; 1729581.AP058_01775; -.
DR PATRIC; fig|1729581.3.peg.1837; -.
DR OrthoDB; 9810135at2; -.
DR Proteomes; UP000059935; Unassembled WGS sequence.
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; 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; 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:UP000059935}.
FT DOMAIN 6..291
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 292..573
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 27..34
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 777 AA; 88512 MW; 7A09DE7F319014DB CRC64;
MQKYIDQLNE AQREPVLQKD GPMIIIAGAG SGKTRVLTIR IAYLMSLGVD AFSILSLTFT
NKAAREMKQR ISSIVGAAEA KNLWMGTFHS VFARILRSEA DLLGYPSNFT IYDSQDSARL
LSSIIKEMQL DRDVYKPKQV LSKISSYKNS LITVKAYFNN PELQEADAMA KKPRMGEIYQ
EYVNRCFKAG AMDFDDLLLK TNELLNLFPE VLAKYQNRFR YILVDEYQDT NHSQYLIVRA
LSDKFQNICV VGDDAQSIYA FRGANINNIL NFQKDYEGVK MFRLEQNYRS TKNIVEAANT
IIEKNKTKLD KIVWTANDFG PKIKVHRSLT DAEEGRFVAS TIFEQKMQNQ LPNGAFAILY
RTNAQSRAME DALRKRDIPY RIYGGLSFYQ RKEIKDVLCY LRLVINPKDE EALIRVINYP
ARGIGDTTVE KLTIAANHYK RSIWEVMQNI DKIDLKLNSG TKNKLNDFVT MIQSFQVINE
NQDAFYITDH VAKKTGLVQE LKKDATPEGM AKIQNIEELL NGIKDFTEGQ KEIDGARGAL
AEFMEDVALA TDLDKDTSDE DRVALMTIHL AKGLEFPQVF VVGMEEDLFP SAMSMSTRSE
LEEERRLFYV ALTRAEYQAY LTYAQWRYRW GKLTDSEPSR FIEEIDGQYL EYLTPSESNY
RFKPMIDKDI FGDVDKSKFR SMKPVGGTPP KTFSDSDPKS EINIRKLKPV SSGAASANPN
LFDSKLLSGN IVMHERFGKG EIINIEGVGA DKKAEIKFEV GGIKKLLLRF AKLDVIG
//
