ID Q2FXV8_STAA8 Unreviewed; 825 AA.
AC Q2FXV8;
DT 21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 111.
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 OrderedLocusNames=SAOUHSC_01723 {ECO:0000313|EMBL:ABD30796.1};
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061 {ECO:0000313|EMBL:ABD30796.1, ECO:0000313|Proteomes:UP000008816};
RN [1] {ECO:0000313|Proteomes:UP000008816}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47 {ECO:0000313|Proteomes:UP000008816};
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington D.C
RL (2006).
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 ---------------------------------------------------------------------------
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; CP000253; ABD30796.1; -; Genomic_DNA.
DR RefSeq; WP_001283311.1; NZ_LS483365.1.
DR RefSeq; YP_500232.1; NC_007795.1.
DR AlphaFoldDB; Q2FXV8; -.
DR SMR; Q2FXV8; -.
DR STRING; 93061.SAOUHSC_01723; -.
DR PaxDb; 1280-SAXN108_1647; -.
DR GeneID; 3921073; -.
DR KEGG; sao:SAOUHSC_01723; -.
DR PATRIC; fig|93061.5.peg.1571; -.
DR eggNOG; COG0507; Bacteria.
DR HOGENOM; CLU_007524_0_1_9; -.
DR OrthoDB; 9803432at2; -.
DR Proteomes; UP000008816; Chromosome.
DR GO; GO:0009338; C:exodeoxyribonuclease V complex; IBA:GO_Central.
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 GO; GO:0017116; F:single-stranded DNA helicase activity; IBA:GO_Central.
DR GO; GO:0006310; P:DNA recombination; IBA:GO_Central.
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};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01488}; Reference proteome {ECO:0000313|Proteomes:UP000008816}.
FT DOMAIN 352..512
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 760..796
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 363..367
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01488"
SQ SEQUENCE 825 AA; 93049 MW; F58D6953A3A0F948 CRC64;
MSDPTLFDYS MIKGTVEAIL FQNSDNFYTV LKVDTIETNE DFDTMPTVVG FLPNIVEGDV
YTFKGQVVDH PRYGKQLKAE TFEKEMPQTK EAIISYLSSD LFKGVGKKTA QNIVNTLGDN
AINDILDDHS VLEKVSGLSK KKQKQIAEQI SANQESEKIM IRLHDLGFGP KLSMAIYQFY
LGDTLTILDR NPYQLIYDIK GIGFNKADQL ARNIGIAYND NERLKAALLY TLEEECIKQG
HTYLPINVVI DLTVDVLNYQ DEEVIEPEKL DEMLQYLNEE KRLIIDNEQV AIPSLYYSEI
KSVQNLFRIK THTNKLTEIE QSDLQMHIGE IEDANQVNYA ASQKEALQTA INSKVMLLTG
GPGTGKTTVI KGIVELYAEI HGLSLDYDDY VNDDYPVVLA APTGRASKRL QESTGLEAMT
IHRLIGWNQD TKPEDILENE INARLIIIDE MSMVDTWLFH QFLSAVPLDA QLIFVGDEDQ
LPSVGPGQVF KDLIESKAIP RVNLTEVYRQ QDGSSIIELA HRMKLGQKID ITQRFHDRSF
INCQANQIPT VVEKVVTSAV NKGYTMADIQ VLAPMYKGNA GIKRLNQVLQ DILNPKKKDT
REIEFGDVVF RKGDKVLQLV NRPNDNIFNG DIGVIVGIFW AKENALNKDV LVVDFEGNEI
TFTKQDMMEL THAYCTSIHK SQGSEFPIVI MPIVKQYFRM LQRPILYTGL TRAKTSLVLL
GDPEAFDIGL KTNGQARLTQ LCTLLKNYFN SEDEEMLENT ATNDTGASQT TIDDQVEAPM
SSNDSEEVMS DSTKTDTNVL TEATMFKIDP MINMGEITPY DFIER
//
