ID G8P7B8_LACLC Unreviewed; 833 AA.
AC G8P7B8;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 55.
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=llh_3750 {ECO:0000313|EMBL:AEU39926.1};
OS Lactococcus cremoris subsp. cremoris A76.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus; Lactococcus cremoris subsp. cremoris.
OX NCBI_TaxID=1104322 {ECO:0000313|EMBL:AEU39926.1, ECO:0000313|Proteomes:UP000007114};
RN [1] {ECO:0000313|EMBL:AEU39926.1, ECO:0000313|Proteomes:UP000007114}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A76 {ECO:0000313|EMBL:AEU39926.1,
RC ECO:0000313|Proteomes:UP000007114};
RA Bolotin A., Quinquis B., Ehrlich S.D., Sorokin A.;
RT "Complete Genome Sequence of Lactococcus lactis subsp. cremoris A76.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
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; CP003132; AEU39926.1; -; Genomic_DNA.
DR RefSeq; WP_014572232.1; NC_017492.1.
DR AlphaFoldDB; G8P7B8; -.
DR KEGG; llr:llh_3750; -.
DR PATRIC; fig|1104322.3.peg.752; -.
DR HOGENOM; CLU_007524_0_1_9; -.
DR Proteomes; UP000007114; Chromosome.
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:RHEA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
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; IPR006345; DNA_helicase_RecD-like.
DR InterPro; IPR003583; Hlx-hairpin-Hlx_DNA-bd_motif.
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; PF13245; AAA_19; 1.
DR Pfam; PF14490; HHH_4; 1.
DR Pfam; PF18335; SH3_13; 1.
DR Pfam; PF13538; UvrD_C_2; 1.
DR SMART; SM00278; HhH1; 2.
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, ECO:0000313|EMBL:AEU39926.1};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01488};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01488}.
FT DOMAIN 96..112
FT /note="Helix-hairpin-helix DNA-binding motif class 1"
FT /evidence="ECO:0000259|SMART:SM00278"
FT DOMAIN 188..207
FT /note="Helix-hairpin-helix DNA-binding motif class 1"
FT /evidence="ECO:0000259|SMART:SM00278"
FT BINDING 355..359
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01488"
SQ SEQUENCE 833 AA; 92783 MW; 5150162ABB980F2C CRC64;
MTDKTYVTGS IEAIFFSNPS NFYKVLLIEI DETNAEYDDF EIVVNGAIGD VVEGDSYTFY
GQLTQHPKYG EQLQVSQYEK AVPTSGAGLV KYFSSDKFPG IGKKTAEKIV ETFPENTVDS
ILEAPEKLDG LLTLARKNSF IKRLRENHGM EKMLTKLAEY GLPSKLTFQI YELYKEETIE
KIEENPYQLV EEVKGVGFKT ADKIASELGI EADSPNRFRA ALMHEVNTHS QATGDTYIEA
KNLLELTIDL LEEARNIEVN PAEVAAEING LIVDGKVQQE GTKIFENSLF FAEDGIRKSL
TALTNRLGKD FADEKLLTVL EEVEKDLEIT YDELQKQAII GAMNQQFFIL TGGPGTGKTT
IINGFIETYA RLYQLDLDPD HYNDDVFPIL LAAPTGRASR RMNELTGLPA ATIHRHLGLG
QDEAEDALGN ELSGSLLIVD EFSMVDTWLA NKLFQAIPGS MKVLLVGDAD QLPSVGPGQI
FADLLKIPEI PSVKLDKIFR QGDDSTITDL AHHIKDGQLP ADFTVKKTDR SYFEVSANFV
PQTVEQIASA WQKRGNNPFE LQILAPMYKG AAGINAMNIL LQNLFNPLND RLEFVLGDMK
FREGDKVLHL VNDAEANVFN GDLGQIVELI AAKYTDSKQD EIVMDFDGQE LTYPRSEWYK
ITLAYAMSIH KSQGSEFSTV IVPMVSSYSR MLERNLLYTA ITRAKQSLIL LGEERAFAQA
VAREGANRKT FLVERFKDDK PAAENLSVDS LTKKVTDKKE ISNKEKNSGS VADLNLENFS
VRKKTAPKVE EISLFDEETE SLGNGILTEA LILSGNFDPL IGLTEQDFAI FNK
//
