ID A0A139NFQ4_9STRE Unreviewed; 805 AA.
AC A0A139NFQ4;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=STRDD10_00749 {ECO:0000313|EMBL:KXT74702.1};
OS Streptococcus sp. DD10.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1777878 {ECO:0000313|EMBL:KXT74702.1, ECO:0000313|Proteomes:UP000072050};
RN [1] {ECO:0000313|EMBL:KXT74702.1, ECO:0000313|Proteomes:UP000072050}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DD10 {ECO:0000313|EMBL:KXT74702.1,
RC ECO:0000313|Proteomes:UP000072050};
RA Denapaite D., Rieger M., Koendgen S., Brueckner R., Ochigava I.,
RA Kappeler P., Maetz-Rensing K., Leendertz F., Hakenbeck R.;
RT "Highly variable Streptococcus oralis are common among viridans
RT streptococci isolated from primates.";
RL Submitted (JAN-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}.
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:KXT74702.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LQRE01000068; KXT74702.1; -; Genomic_DNA.
DR RefSeq; WP_067193222.1; NZ_KQ969158.1.
DR AlphaFoldDB; A0A139NFQ4; -.
DR STRING; 1777878.STRDD10_00749; -.
DR PATRIC; fig|1777878.3.peg.825; -.
DR OrthoDB; 9803432at2; -.
DR Proteomes; UP000072050; Unassembled WGS sequence.
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; 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; 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, ECO:0000313|EMBL:KXT74702.1};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01488};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01488}; Reference proteome {ECO:0000313|Proteomes:UP000072050}.
FT DOMAIN 346..536
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT BINDING 357..361
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01488"
SQ SEQUENCE 805 AA; 90886 MW; 013749AB699F0CB9 CRC64;
MEFYFTGTIE RIIFENPSNF FRILLLEISA TNADDYDDLD IIVTGTIADV LEGENYTFWG
ELVQHPKYGK QLKIVRYEKE KPSSQGLVKY FSSEHFKGIG RKTAQKIIDL YGEEDTINQI
LAKPEKLQSI SGLSSTNREA FISTLRTNYG TELILSQLAE YGIPNRLAFQ IQDFYKEETL
EIIESNPYQL VEDIQGLGFK IADQIAESLG IEAIAPARYR AGLIHSLFSL SMERGDTYVE
ARDLLEYCIN LLETARPVEL APEAVAQELG LLIQDDRVQN VDTKIFDNSL FFAEEGIRTN
LIRILEKGQQ QMYPVKQILD LIAEVEDEFG ISYDTIQKEA ICNAINNKVF ILTGGPGTGK
TTVINGFIAV YAALHKLDLR KKSELPILLA APTGRAARRM NELTGLPSAT IHRHLGMTGD
DEVSNLSDYL DADLIIIDEF SMVDTWLANQ LLQNISSNSQ ILIVGDADQL PSVSPGQVLA
DLLHVSCLPQ VKLEKIYRQS EDSTIVMLAS QIRQGLLPAD FTAKKADRSY FETRSEHIPQ
MIERIAGAAI RSGIAAQDVQ VLAPMYRGQA GIDNINHLMQ ELINPAIKEQ LSFTFNETTY
REGDKVIHLV NDTESNVFNG DLGYITELTP AKYTDSKQDE LLLNFDGGEI RYPRNEWYKI
RLAYAMSIHK SQGSEFPVVI LPITSSSRRM LQRNLIYTAI TRAKSKLILL GEYQAFDFAT
QNTGTSRKTY LIERFEENKQ PQSTDFQNLS TEDVDKDVNH PVIAVDNTEN FVEKDVKNYL
LSKENWNQIN PMIGIEETDI AEFFK
//
