ID A0A0K9GW68_9BACI Unreviewed; 798 AA.
AC A0A0K9GW68;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=AC625_16355 {ECO:0000313|EMBL:KMY50900.1};
OS Peribacillus loiseleuriae.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Peribacillus.
OX NCBI_TaxID=1679170 {ECO:0000313|EMBL:KMY50900.1, ECO:0000313|Proteomes:UP000037146};
RN [1] {ECO:0000313|Proteomes:UP000037146}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FJAT-27997 {ECO:0000313|Proteomes:UP000037146};
RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA Shi H., Pan Z., Liu X.;
RT "Genome sequencing project for genomic taxonomy and phylogenomics of
RT Bacillus-like bacteria.";
RL Submitted (JUL-2015) 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:KMY50900.1}.
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DR EMBL; LFZW01000001; KMY50900.1; -; Genomic_DNA.
DR RefSeq; WP_049682249.1; NZ_LFZW01000001.1.
DR AlphaFoldDB; A0A0K9GW68; -.
DR STRING; 1679170.AC625_16355; -.
DR PATRIC; fig|1679170.3.peg.3719; -.
DR OrthoDB; 9803432at2; -.
DR Proteomes; UP000037146; 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: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; 1.
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:UP000037146}.
FT DOMAIN 158..249
FT /note="RecD helicase-like helix-hairpin-helix"
FT /evidence="ECO:0000259|Pfam:PF14490"
FT DOMAIN 594..665
FT /note="RecD-like DNA helicase SH3"
FT /evidence="ECO:0000259|Pfam:PF18335"
FT DOMAIN 682..730
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13538"
FT BINDING 369..373
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01488"
SQ SEQUENCE 798 AA; 90014 MW; FFD8ED1C6EBC4705 CRC64;
MGQQDALDLF SEEKKFMKGR HLVTIFHNES NLYSVVRIRL DETNLDYDEQ EAVVTGYFPK
IHEQETYIFY GTMKDHPRFG MQFHVEHFRK DMPQSKEGIV AYLSSDLFKG IGKRTAESIV
DKLGENAISK ILANPSILDT VPKLSSEKAK SFYDSLIEHQ GLEQVMIGLN QYGFGPQLSM
KIYQMYQHDT LSILQKNPYQ LVEDVEGIGF GRADELGFQL GISGGHPDRI KAACLYTLDA
QCLQDGHVYM EAEDLLETVK RMLEENKRDA IEFTAISSEI VKLEDEGKIK VEERRIYPPS
LYFSEKGIVT NIKRILSQTE YEDQFPESEF LLALGELEER LGVDYAPAQK EAIQTALQSP
MLILTGGPGT GKTTVIKGIV ELYAELHGVS MEIGDYKKET EPFPFVLAAP TGRAAKRMAE
STGLPAVTIH RLLGWNGSEG FSHDEENPIE GRIVIIDEMS MVDTWLAHQL LKALPEHVQL
VLVGDEDQLP SVGPGQVLKD LLASQSVPMV GLEQIYRQAD GSSIIELAHE IKRGRLPESF
SHQQSDRSFI RCGTGQIAQV VEKVVANARK KGFTSRDIQV LAPMYRGPAG IDNLNKMLQE
VFNGNAEEKK RELKFGDVVY RSGDKVLQLV NQPEEGVYNG DMGEIVSVLF AKENTDNVDK
LVISFDGIEV MYNRQDLNQI THAYCCSIHK SQGSEFPIVI LPVVKSYYRM LRRNLLYTAI
TRSKNFLILC GEEDAFRQGI ERNNEMKRKT TLMQKLQAAD LGESELETET EVAIDPFEIL
MKVDPMIGME HVTPYDFM
//
