ID I3Z1I3_BELBD Unreviewed; 781 AA.
AC I3Z1I3;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN OrderedLocusNames=Belba_0442 {ECO:0000313|EMBL:AFL83101.1};
OS Belliella baltica (strain DSM 15883 / CIP 108006 / LMG 21964 / BA134).
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC Belliella.
OX NCBI_TaxID=866536 {ECO:0000313|EMBL:AFL83101.1, ECO:0000313|Proteomes:UP000006050};
RN [1] {ECO:0000313|Proteomes:UP000006050}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15883 / CIP 108006 / LMG 21964 / BA134
RC {ECO:0000313|Proteomes:UP000006050};
RA Lucas S., Copeland A., Lapidus A., Goodwin L., Pitluck S., Peters L.,
RA Mikhailova N., Davenport K., Kyrpides N., Mavromatis K., Pagani I.,
RA Ivanova N., Ovchinnikova G., Zeytun A., Detter J.C., Han C., Land M.,
RA Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D.,
RA Tindall B., Pomrenke H., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Belliella baltica DSM 15883.";
RL Submitted (JUN-2012) 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; CP003281; AFL83101.1; -; Genomic_DNA.
DR AlphaFoldDB; I3Z1I3; -.
DR STRING; 866536.Belba_0442; -.
DR KEGG; bbd:Belba_0442; -.
DR PATRIC; fig|866536.3.peg.458; -.
DR eggNOG; COG0210; Bacteria.
DR HOGENOM; CLU_004585_5_2_10; -.
DR Proteomes; UP000006050; 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; 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:UP000006050}.
FT DOMAIN 35..320
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 321..596
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT REGION 693..722
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 705..722
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 56..63
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 781 AA; 89609 MW; 163E331B4E273A1F CRC64;
MSIRQVRIHP RSIKAKKSIN FEACRTDRLR MDYLKGLNPP QKEAVEHTDG PVMIIAGAGS
GKTRVLTYRI AHLIHAKGVD PFNILSLTFT NKAAAEMKNR IERLIGLEAR NTWMGTFHST
FAKILRVEAE KLGYPSNFTI YDTDDSKSLI RSIVKEMKLD DKVYKPNTVL SRISGAKNRL
ISWEAYLNDP YIKADDESAM KPRMGEIYKT YQKRLFKSSA MDFDDLLFNT NILFRDHLDV
LNKYQQRFKY VMVDEFQDTN LSQYLITKKL AAVHQNICVV GDDAQSIYAF RGADIQNILN
FEKDYPDLFI VKLEQNYRST KNIVQAANSI IAKNKAQLQK NVWTQNDEGD MIELIKASSD
NEEGRVVATT IFEEKNNKKL NNSDFAILYR TNSQSRSMEE ALRKMNINYK IVGGLSFYQR
KEIKDLMAYM RFVVNRDDEE AFKRIINYPK RGIGDTTVEK MLVAAYEHDI PLWEVMTNAT
SFLSGRASNA VEDFTTMIKS FSIEVERKDA FEAATSISKQ SGLLRDLYED KTIEGLNRYE
NVQELLNAIK EYVDNPENED KSLGAFLQEI ALLTDNDRDK DTTDSVTLMT IHSSKGLEFK
QVFVVGMEED LFPSQMMMQS REDLEEERRL FYVASTRAMD KLYLTYALTR YRYGRLLNCE
PSRFLEEVDP ACIRVNKRMT AAPSGALRNE GSEGRNGFIG IKKNPSMRPQ TTAKVHTPSP
DFKPSNTNNL AESMLVEHPK FGFGKVLKIE IEGINKKATI QFENFGEKTL LLSFAKLRII
D
//
