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Database: UniProt
Entry: G0M0Y6_LACPE
LinkDB: G0M0Y6_LACPE
Original site: G0M0Y6_LACPE 
ID   G0M0Y6_LACPE            Unreviewed;       869 AA.
AC   G0M0Y6;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=ATP-dependent RecD-like DNA helicase {ECO:0000256|HAMAP-Rule:MF_01488};
DE            EC=3.6.4.12 {ECO:0000256|HAMAP-Rule:MF_01488};
GN   Name=recD2 {ECO:0000256|HAMAP-Rule:MF_01488};
GN   ORFNames=LPENT_03047 {ECO:0000313|EMBL:CCC18351.1};
OS   Lactiplantibacillus pentosus IG1.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactiplantibacillus.
OX   NCBI_TaxID=1042160 {ECO:0000313|EMBL:CCC18351.1};
RN   [1] {ECO:0000313|EMBL:CCC18351.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=IG1 {ECO:0000313|EMBL:CCC18351.1};
RA   Maldonado-Barragan A., Caballero-Guerrero B., Lucena-Padros H.,
RA   Ruiz-Barba J.L.;
RT   "Genome Sequence of Lactobacillus pentosus IG1, a Strain Isolated from
RT   Spanish-Style Green Olive Fermentations.";
RL   J. Bacteriol. 193:5605-5605(2011).
CC   -!- FUNCTION: DNA-dependent ATPase and ATP-dependent 5'-3' DNA helicase.
CC       Has no activity on blunt DNA or DNA with 3'-overhangs, requires at
CC       least 10 bases of 5'-ssDNA for helicase activity. {ECO:0000256|HAMAP-
CC       Rule:MF_01488}.
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=3.6.4.12;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01488};
CC   -!- SIMILARITY: Belongs to the RecD family. RecD-like subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01488}.
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DR   EMBL; FR874854; CCC18351.1; -; Genomic_DNA.
DR   AlphaFoldDB; G0M0Y6; -.
DR   GO; GO:0043139; F:5'-3' DNA helicase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   CDD; cd17933; DEXSc_RecD-like; 1.
DR   CDD; cd18809; SF1_C_RecD; 1.
DR   Gene3D; 1.10.10.2220; -; 1.
DR   Gene3D; 2.30.30.940; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   HAMAP; MF_01488; RecD_like; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR006345; DNA_helicase_RecD-like.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR029493; RecD-like_HHH.
DR   InterPro; IPR041451; RecD-like_SH13.
DR   InterPro; IPR027785; UvrD-like_helicase_C.
DR   NCBIfam; TIGR01448; recD_rel; 1.
DR   PANTHER; PTHR43788; DNA2/NAM7 HELICASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR43788:SF6; RECBCD ENZYME SUBUNIT RECD; 1.
DR   Pfam; PF13604; AAA_30; 1.
DR   Pfam; PF14490; HHH_4; 1.
DR   Pfam; PF18335; SH3_13; 1.
DR   Pfam; PF13538; UvrD_C_2; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_01488}; DNA-binding {ECO:0000256|HAMAP-Rule:MF_01488};
KW   Helicase {ECO:0000256|HAMAP-Rule:MF_01488};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01488, ECO:0000313|EMBL:CCC18351.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_01488}.
FT   DOMAIN          361..518
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          766..841
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        792..841
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         372..376
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01488"
SQ   SEQUENCE   869 AA;  95198 MW;  D5657414636A03AB CRC64;
     MTDEQANLFS DDVGRNPVSH FVVGKVAATF FSSSDSFYKV LLVKVTEQNI DWSEDEIVVT
     GNFADIQEET TYRFTGRTVT HPKYGVQFQA DNYQNETPTT RSGLIAYLSG NDFPGLGKRT
     AERIVDTLGE DAIDKILADP KVLKPIGLRA GVQATLVDTL TVNNGLEQTI IGLNAYGFGS
     RLAAAIYARY QGDTLARIQE NPYCLVEDIK GVGFKKADQI AAQLNIDPQA DERLKAALLT
     EIDELCVANG DTYTTAKPLL NQTLQLLENA RHVRIDPDKL ADQLVVLAKE NKIVGDENRI
     YLRGLYEAEW RVAEQLKRLL DEEDEHPLTD KAVESAIQHV SRASNITYDA SQTAALKAAI
     TSHVFLLTGG PGTGKTTIIR GLVALYAELH DVVLDVNQYK DEPFPISLAA PTGRAAKRMA
     ETTGLPASTI HRLLGLTGRE DGPEEPSKEL QGGILIIDEM SMVDTVLFQQ LLTSIPSEMQ
     VIFVGDKDQL PSVGAGQVFH DLLQFSELPQ IELTTIYRQG NDSSIIPLAH AIKDGQLPAD
     FTVNQPDRSF ISCNAYQVNH IIEQVVGKAK AKGFSADDVQ ILAPMYRGTA GIDQLNTTVQ
     NIFNPLKSAR QKHLTYNGQD FRVGDKVLHL VNSPEDNVFN GDIGRIVGID LAGDPHNESK
     KDQITIAFDQ NEVTYQRSDW NRLTLAYSMS IHKSQGSQFK MVILPMVPQF SRMLQRNLLY
     TAVTRAEQML ILLGDIQSFE RSVTNESVNR QTTLTKRLRQ VWGIETSDEA DEPEASAEPA
     TDVEAAAGDS ETTTEGEPTQ AKSENDDDVT SAQSVETAAD DGESGASTAA QPTQGPTVLT
     PTLVLSRQID PMIGMAGIKP TDFMPQATN
//
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