ID A0A2K8PLF2_STRLA Unreviewed; 748 AA.
AC A0A2K8PLF2;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=recD1 {ECO:0000313|EMBL:ATZ26613.1};
GN Synonyms=recD2 {ECO:0000256|HAMAP-Rule:MF_01488}, recD2_1
GN {ECO:0000313|EMBL:QUQ56441.1};
GN ORFNames=SLAV_24050 {ECO:0000313|EMBL:ATZ26613.1}, SLLC_22175
GN {ECO:0000313|EMBL:QUQ56441.1};
OS Streptomyces lavendulae subsp. lavendulae.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=58340 {ECO:0000313|EMBL:ATZ26613.1, ECO:0000313|Proteomes:UP000231791};
RN [1] {ECO:0000313|EMBL:ATZ26613.1, ECO:0000313|Proteomes:UP000231791}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCM 3239 {ECO:0000313|EMBL:ATZ26613.1,
RC ECO:0000313|Proteomes:UP000231791};
RA Busche T., Novakova R., Al'Dilaimi A., Homerova D., Feckova L.,
RA Rezuchova B., Mingyar E., Csolleiova D., Bekeova C., Winkler A.,
RA Sevcikova B., Kalinowski J., Kormanec J., Ruckert C.;
RT "Complete genome sequence of Streptomyces lavendulae subsp. lavendulae CCM
RT 3239 (formerly 'Streptomyces aureofaciens CCM 3239'), the producer of the
RT angucycline-type antibiotic auricin.";
RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:QUQ56441.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Del-LP {ECO:0000313|EMBL:QUQ56441.1};
RA Novakova R., Ruckert C., Knirschova R., Feckova L., Busche T.,
RA Csolleiova D., Homerova D., Rezuchova B., Javorova R., Sevcikova B.,
RA Kalinowski J., Kormanec J.;
RT "The linear plasmid pSA3239 is essential for the replication of the
RT Streptomyces lavendulae subsp. lavendulae CCM 3239 chromosome.";
RL Submitted (APR-2021) 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; CP024985; ATZ26613.1; -; Genomic_DNA.
DR EMBL; CP073778; QUQ56441.1; -; Genomic_DNA.
DR RefSeq; WP_030229518.1; NZ_JOEW01000011.1.
DR AlphaFoldDB; A0A2K8PLF2; -.
DR GeneID; 82166767; -.
DR KEGG; slx:SLAV_24050; -.
DR OrthoDB; 9763659at2; -.
DR Proteomes; UP000231791; Chromosome.
DR Proteomes; UP000676025; 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: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; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 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; IPR010994; RuvA_2-like.
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; PF14520; HHH_5; 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.
DR SUPFAM; SSF47781; RuvA domain 2-like; 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, ECO:0000313|EMBL:ATZ26613.1};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01488, ECO:0000313|EMBL:ATZ26613.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01488}; Reference proteome {ECO:0000313|Proteomes:UP000231791}.
FT DOMAIN 355..557
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT BINDING 366..370
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01488"
SQ SEQUENCE 748 AA; 80333 MW; 56A94F54DA565372 CRC64;
MTTNGAVQLA VVEGVLERIT YANEESGYTV ARVDTGRGAG DLLTVVGSLL GAQPGESLRM
EGRWGSHPQY GKQFSVENYS TLLPATIQGI RRYLGSGLIK GIGPKIADRI VEHFGTDTLD
VIEAEPKRLI EVPGLGPKRT KMIGAAWEEQ KAIKEVMVFL QGVGVSTSIA VRIYKKYGDA
SISVVRNQPY RLAADVWGIG FLTADRIAQA VGIPHDSPER VRAGLQYALS QSTDQGHCFL
PEERLIADGV KLLQVDTGLV IECLAELAAD PEGVVRESVP DPQGGPDPLT AVYLVPFHRA
ELSLVGQVRR LLNAEEDRMP GFRDVDWDKA LGWLAGRTGA SLAPEQRDAV RLALTRRVAV
LTGGPGCGKS FTVRSIVELA RAKKAKVVLA APTGRAAKRL SELTGAEAST VHRLLELKPG
GDAAYDRDRP LDADLVVVDE ASMLDLLLAN KLVKAVAPGA HLLLVGDVDQ LPSVGAGEVL
RDLLAEGGPV PAVRLTRIFR QAQQSGVVTN AHRINTGVPP ITDGLPDFFL FPEEDTEAAG
LLAVDVAARR IPARFGLDPR RDVQVLAPMH RGPAGAGNLN GLLQQAITPA RPNLPEKRFG
GRVFRVGDKV TQIRNNYEKG ANGVFNGTVG VVTALDLDEQ RLTVRTEEDE EVGYEFAELD
ELAHAYAVTI HRSQGSEYPA VVIPVTTGAW MMLQRNLLYT AVTRAKKLVV LVGSRKALGQ
AVRTVSAGRR YTAVAARLSG RIPVGNIT
//
