ID A0A370GWD1_9BACI Unreviewed; 1251 AA.
AC A0A370GWD1;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=ATP-dependent helicase/nuclease subunit A {ECO:0000256|HAMAP-Rule:MF_01451};
DE EC=3.1.-.- {ECO:0000256|HAMAP-Rule:MF_01451};
DE EC=5.6.2.4 {ECO:0000256|HAMAP-Rule:MF_01451};
DE AltName: Full=ATP-dependent helicase/nuclease AddA {ECO:0000256|HAMAP-Rule:MF_01451};
DE AltName: Full=DNA 3'-5' helicase AddA {ECO:0000256|HAMAP-Rule:MF_01451};
GN Name=addA {ECO:0000256|HAMAP-Rule:MF_01451};
GN ORFNames=DFR59_101484 {ECO:0000313|EMBL:RDI47819.1};
OS Falsibacillus pallidus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Falsibacillus.
OX NCBI_TaxID=493781 {ECO:0000313|EMBL:RDI47819.1, ECO:0000313|Proteomes:UP000255326};
RN [1] {ECO:0000313|EMBL:RDI47819.1, ECO:0000313|Proteomes:UP000255326}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25281 {ECO:0000313|EMBL:RDI47819.1,
RC ECO:0000313|Proteomes:UP000255326};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: The heterodimer acts as both an ATP-dependent DNA helicase
CC and an ATP-dependent, dual-direction single-stranded exonuclease.
CC Recognizes the chi site generating a DNA molecule suitable for the
CC initiation of homologous recombination. The AddA nuclease domain is
CC required for chi fragment generation; this subunit has the helicase and
CC 3' -> 5' nuclease activities. {ECO:0000256|HAMAP-Rule:MF_01451}.
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=5.6.2.4;
CC Evidence={ECO:0000256|ARBA:ARBA00034618, ECO:0000256|HAMAP-
CC Rule:MF_01451};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by
CC translocating in the 3'-5' direction.; EC=5.6.2.4;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01451};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01451};
CC -!- SUBUNIT: Heterodimer of AddA and AddB/RexB. {ECO:0000256|HAMAP-
CC Rule:MF_01451}.
CC -!- SIMILARITY: Belongs to the helicase family. AddA subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01451}.
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:RDI47819.1}.
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DR EMBL; QQAY01000001; RDI47819.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A370GWD1; -.
DR OrthoDB; 9810135at2; -.
DR Proteomes; UP000255326; Unassembled WGS sequence.
DR GO; GO:0008408; F:3'-5' exonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003690; F:double-stranded DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:UniProtKB-UniRule.
DR CDD; cd17932; DEXQc_UvrD; 1.
DR CDD; cd18807; SF1_C_UvrD; 1.
DR Gene3D; 1.10.274.50; -; 1.
DR Gene3D; 3.90.320.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 4.
DR HAMAP; MF_01451; AddA; 1.
DR InterPro; IPR014152; AddA.
DR InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011604; PDDEXK-like_dom_sf.
DR InterPro; IPR038726; PDDEXK_AddAB-type.
DR InterPro; IPR011335; Restrct_endonuc-II-like.
DR InterPro; IPR014016; UvrD-like_ATP-bd.
DR NCBIfam; TIGR02785; addA_Gpos; 1.
DR PANTHER; PTHR11070:SF48; ATP-DEPENDENT HELICASE_NUCLEASE SUBUNIT A; 1.
DR PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR Pfam; PF12705; PDDEXK_1; 1.
DR Pfam; PF00580; UvrD-helicase; 1.
DR Pfam; PF13361; UvrD_C; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF52980; Restriction endonuclease-like; 1.
DR PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01451};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW Rule:MF_01451};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW Rule:MF_01451};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_01451};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|HAMAP-
KW Rule:MF_01451};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|HAMAP-Rule:MF_01451};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01451};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01451};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_01451};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01451}; Reference proteome {ECO:0000313|Proteomes:UP000255326}.
FT DOMAIN 13..484
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 523..814
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 34..41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1251 AA; 143232 MW; ACE19DF9C17AAC79 CRC64;
MKRSVIPVKP ETVTWTDDQW KAIHAKNQDI LVAAAAGSGK TAVLVERIIG KIISEEEPFD
VDRLLVVTFT NASAAEMRHR IGEALEKAIS QNPSSVHLRK QLSLLNRASI STLHSFCLEV
IRKYYYLIDI DPGFRIADGT EGELLRDEVL DDLFEEEYGK EGNEPFYLLV DTFTNDRSDA
ALQDMVRKLY DFSRSHPFPD QWLDELVSMY DVNDGGPIEE LPFYDAILWD LLLQFEGAKS
LLQEAYELTK LPGGPAPRAE NYLDDMALVD RLITAGKTSW NELYLAMNTM EFNRAKACRG
DDFNKDLVKS ADDLRKKAKT ILEKQRNELF SRKPETFLND MQKMKGVISS LVELVKTFGE
KFKDVKEEKG LVDFSDLEHY CLEILMDSDD PNTPSEAAKS YRSQFKEVLV DEYQDTNMVQ
ETILQLVSAE RDNGNLFMVG DVKQSIYRFR LAEPNLFLNK YNAFDSEGEG SGLKIDLAMN
FRSRNEVLAG TNYLFKQIMG MKVGEIEYDE NAELKLGASY PQDETYPIEL HLIDLEDESG
SAADELEDQA SPEEDLVDLE KSQLEARWMA AKIKELIDSR KQIYDPKRKA YRPIQYKDIV
LLLRSMPWAP VIMEEFKEAG IPIYANLATG YFDATEITIM LSLLKVIDNP YQDIPLASVL
RSPIVGLSEK ELAAIRSSSS SGAFYDAVKA ASRKNHSGQA EGLNEKLQSF LSDLSAWRTL
ARQGALSQLI WQLYRDTKFY DFSGGLPGGK QRQANLRALY DRARQYESTS FRGLFRFLRF
IDRMRERGDD LGTARALSEG EDVVRLMTIH SSKGLEFPVV FMAGVSRNFN MMDLNASYLL
DKDLGFASKY MDPEKRITYP SLPQIAFKRK KKLETIAEEM RVLYVALTRA KEKLYLVASP
KNLEKSIQKW AGALSHQDWL LKDYDRASAK SYLDWIGPSM ARHSDLREFL EGSSPHPLLS
EEIASHESRW HIEVHHKSEL HNIFPEPESE NDGWIEAVQK GQPLKSSDSS GDKIDEVLSW
KYPYQEAAKR RSKQSVSELK RMLETRDAES DTSFLQKFQK PVMKRPKFMQ EQKLSPAERG
TAMHMVMQHI PFGERIDVHL LNTLLEAMVE KELLSIEQKE AITIGEILSF FETDLGRKMA
ESSNVHREIP FSIAVPANEI YTDWNSPDES VLVQGIIDCV IEEPDGLVLI DYKTDNITDR
FKGKFEDAKP VLENRYRVQL EFYEEALRKI WKKPIKQKFL FFFDGAHILE L
//
