ID A0A249DH48_LACRH Unreviewed; 821 AA.
AC A0A249DH48;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=BGK71_06025 {ECO:0000313|EMBL:ASX18475.1};
OS Lacticaseibacillus rhamnosus (Lactobacillus rhamnosus).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lacticaseibacillus.
OX NCBI_TaxID=47715 {ECO:0000313|EMBL:ASX18475.1, ECO:0000313|Proteomes:UP000215843};
RN [1] {ECO:0000313|EMBL:ASX18475.1, ECO:0000313|Proteomes:UP000215843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LR5 {ECO:0000313|EMBL:ASX18475.1,
RC ECO:0000313|Proteomes:UP000215843};
RA Nam Y.-D., Kang J., Chung W.-H.;
RT "Complete genome sequence of Lactobacillus rhamnosus LR5.";
RL Submitted (AUG-2016) 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; CP017063; ASX18475.1; -; Genomic_DNA.
DR RefSeq; WP_049171193.1; NZ_VRTQ01000001.1.
DR AlphaFoldDB; A0A249DH48; -.
DR GeneID; 69831794; -.
DR Proteomes; UP000215843; 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 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; 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 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:ASX18475.1};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01488};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01488}.
FT DOMAIN 149..239
FT /note="RecD helicase-like helix-hairpin-helix"
FT /evidence="ECO:0000259|Pfam:PF14490"
FT DOMAIN 581..652
FT /note="RecD-like DNA helicase SH3"
FT /evidence="ECO:0000259|Pfam:PF18335"
FT DOMAIN 669..717
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13538"
FT REGION 753..776
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 359..363
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01488"
SQ SEQUENCE 821 AA; 90183 MW; 69C8E0790833D34F CRC64;
MDRHEDSVTG RVKSIFFQNP TNFFKILLID ITATTITWTE PDIVVTGTFG DIKEDETYTF
TGHVVDHPKY GQQFQADNYH VDRPTNKTGL INYLSSDKFP GIGPKTAEKI IDKLGVDAID
RILDDPESLK GLGISAAKQK MLVTNLKTNQ GMERVIIGLN DYGFTSNMAG RIYQQYQNDA
LEVIKQNPYQ LINDIDGIGF TRADQIAAKL AIAPDSQLRL GGAVMDTLQR LTDGEGDTFV
DLKTLVTQTL DLLERARQVA VNPEAVGQAI VTLAKDNALV AEGKRIFPKR LYDSEWQIAR
QLKGLADAGR AAKQPALAEI KQTLAAVQEE TGIAYDEVQK KAIITALQSP IFLLTGGPGT
GKTTVTDGIV RTYAQLHDLS LDRHEYTPDD PFPIMLAAPT GRAAKRISET TQLPASTIHR
LLGLGVDTQE FAPNDLPDGL LIIDEMSMVD TYLFRTLLTA LHPGMQIVLV GDKDQLPSVG
PGQVFADLLR SQALPHAALT HIHRQDADSS IIPLAHAVNA GRLPDDFTRP QVDRSFLPCS
PSQVPEVVGQ VVQRAAVKQF SIADIQVLAP MYRGTAGIDR LNPLLQDILN PKRSARTKTV
HFGETEYRIG DKILQLVNDP NQNVFNGEIG QIVGITFAKE AASKTDELTI DFDGNEITYK
RSDFSKITLA YATSIHKAQG SEFPMVILPL TMQSRRMLRR NLLYTAITRA KSFLILVGEL
AAFETAVGEI AVNRHTGLVQ RLQQAFGMTV SQPDVEKPTP ATEVSQNTGQ IDTNLSDLDN
GISTDESNNY QLTPTLVASQ RIDPMIGMNG VTPQMFMTKE K
//
