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Database: UniProt
Entry: A0A371P5L5_9BACL
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ID   A0A371P5L5_9BACL        Unreviewed;       762 AA.
AC   A0A371P5L5;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE            EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN   ORFNames=DX130_22640 {ECO:0000313|EMBL:REK71244.1};
OS   Paenibacillus paeoniae.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=2292705 {ECO:0000313|EMBL:REK71244.1, ECO:0000313|Proteomes:UP000261905};
RN   [1] {ECO:0000313|EMBL:REK71244.1, ECO:0000313|Proteomes:UP000261905}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M4BSY-1 {ECO:0000313|EMBL:REK71244.1,
RC   ECO:0000313|Proteomes:UP000261905};
RA   Tuo L.;
RT   "Paenibacillus sp. M4BSY-1, whole genome shotgun sequence.";
RL   Submitted (AUG-2018) 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:REK71244.1}.
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DR   EMBL; QUBQ01000006; REK71244.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A371P5L5; -.
DR   OrthoDB; 9810135at2; -.
DR   Proteomes; UP000261905; 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   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
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}; Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00560}; Reference proteome {ECO:0000313|Proteomes:UP000261905}.
FT   DOMAIN          17..313
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   DOMAIN          314..576
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51217"
FT   REGION          662..688
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        664..688
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         38..45
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ   SEQUENCE   762 AA;  86901 MW;  50A6FB672D91FE7E CRC64;
     MGKLAPFLER KHKELGVQLN EVQRQAVEQA EGPLLLLASP GSGKTTTLIM RIGYLIEELG
     TDPARIKAVT FSRASARDMK DRFTRFFPGL QPVDFSTIHS LAFEIVRTHF YKTRTAYDII
     EGALEIEEED EAQGTVKPLP LHKRIILRNL FKDIVGENAT DDAMEELTTY ISYVKNKMLP
     PEQWASAKVD VPQADRILHE YEAFKRSGTP KLLIDFDDML TIANDVLEKD GAMLRKLQSR
     YDYVMTDESQ DTSMVQHAII EKLAMGHRNL CVVADDDQSI YSWRGAEPSY LLRFKDVYPD
     AVMLYMVQNY RSSPEIVQTA NTFIKRNKKR YEKEMFTHNA SHEPIAFKTL RDYREQAKYV
     VREIAKMEKL SEAAVLYRNN SSSIALMNDF DRAGIPFYMK DADNRFFSHW VIEDVLNFMR
     MSYTDKRADI LENIHLKFNG YISKHQMSVL KSIDNGESVF DNLLTIVQLH DYQIKPLQEA
     KETFREMNSM PPLPAIRVIR TRLGYEKALE KICERLGFRK EYLIGILNTL EDIAEGLETM
     ADFAARLKYL EKVLKGAKSR KGQNAVTFST FHSAKGLEFD HVYMVDLVEG IIPGSEDGKK
     EANGESSSME EAVRLFYVGM TRARKTLEMV TYGQRDGEQA TESSFMTAIK DIVDPERITA
     RTTAASERRS ASFSEGESTR ALKGMKSTSF TARREPIQAE LNPHAVKNPA EVTVGANVRH
     RVFGVGCVER ADNESIMIRF SENNVKTLAM AMCMERGLLE LV
//
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