ID A0A150LG35_9BACI Unreviewed; 802 AA.
AC A0A150LG35;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=B4135_3305 {ECO:0000313|EMBL:KYD11190.1};
OS Caldibacillus debilis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Caldibacillus.
OX NCBI_TaxID=301148 {ECO:0000313|EMBL:KYD11190.1, ECO:0000313|Proteomes:UP000075683};
RN [1] {ECO:0000313|EMBL:KYD11190.1, ECO:0000313|Proteomes:UP000075683}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B4135 {ECO:0000313|EMBL:KYD11190.1,
RC ECO:0000313|Proteomes:UP000075683};
RA Berendsen E.M., Wells-Bennik M.H., Krawcyk A.O., De Jong A., Holsappel S.,
RA Eijlander R.T., Kuipers O.P.;
RT "Draft Genome Sequences of Seven Thermophilic Sporeformers Isolated from
RT Foods.";
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:KYD11190.1}.
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DR EMBL; LQYT01000113; KYD11190.1; -; Genomic_DNA.
DR RefSeq; WP_061569686.1; NZ_LQYT01000113.1.
DR AlphaFoldDB; A0A150LG35; -.
DR STRING; 301148.B4135_3305; -.
DR PATRIC; fig|301148.3.peg.1271; -.
DR OrthoDB; 9803432at2; -.
DR Proteomes; UP000075683; 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}; Coiled coil {ECO:0000256|SAM:Coils};
KW 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}.
FT DOMAIN 357..518
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT COILED 251..285
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 368..372
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01488"
SQ SEQUENCE 802 AA; 90941 MW; 8017BDF0ACD77EC8 CRC64;
MTEQGTAPFA DGKKYIKGRL IVTIFHNEKN LYTVLRLRVE ETTEDFRDKE VVVTGYFPPI
HENETYVFYG RFVEHPKYGL QYQAEQFRRD IPTTKQGIVQ YLSSPLFKGI GKKTAEKIVE
HIGENAISKI LEQPSVLDSV PNLPAEKAKQ LYDALVLHQG LEKIMIALNE YGFGTNLALR
IYQAYKEQTL EIIEQNPYRL VEDVEGIGFN RADELGSRLG FQGNHPYRIK AGILYALETL
CLQEGHCFYE RESLKQAVKE LLEKSRDAEI DFDAIELEML KLEEEGKIIA EETRVYLPSI
YFSEKGLVNN IKRLLAQERN GGRFSEAEIL LALGEVEERL GIEYSPSQRE ALRTALHSPM
MILTGGPGTG KTTVIRGIIE LYGKLYGYSL NPADYRGDEP FPFLLAAPTG RAAKRMAEST
GLPAVTIHRL LGWNGTESFE HDEDHPVSGK LLIIDEMSMV DIWLAHHLFK ALPDDIQVVI
VGDEDQLPSV GPGQVLKDLL ASNLIPTVRL TEIYRQENGS SIIPLAHSIK NGVIPPDLTE
QKKDRSFIAC SYRQVSHVVR QVVEKALEKG YSKKDIQVLA PIYRGNAGID HFNLLLQDLL
NGNEDGKKRE LKFGDVTYRV GDKVLQLVNR PEDNVFNGDI GEVVAILYAK ENVEKEDVLI
VSFDGNEVAY TRQDLQQITL SYCVSIHKSQ GSEFPVVILP VLKGYYRMLR RNLLYTAVTR
SKRFLIICGE EEAFRIAVSR ADDHQRNTSL RERLLRACRE TEEEDPEAVR ESSLEEELMK
VDPMIGMENI TPYHFLESGE KE
//
