ID A0A2V3W1J8_9BACI Unreviewed; 1239 AA.
AC A0A2V3W1J8;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=DFR56_106123 {ECO:0000313|EMBL:PXW87054.1};
OS Pseudogracilibacillus auburnensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC Pseudogracilibacillus.
OX NCBI_TaxID=1494959 {ECO:0000313|EMBL:PXW87054.1, ECO:0000313|Proteomes:UP000247978};
RN [1] {ECO:0000313|EMBL:PXW87054.1, ECO:0000313|Proteomes:UP000247978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 28556 {ECO:0000313|EMBL:PXW87054.1,
RC ECO:0000313|Proteomes:UP000247978};
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 (MAY-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:PXW87054.1}.
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DR EMBL; QJJQ01000006; PXW87054.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V3W1J8; -.
DR OrthoDB; 9810135at2; -.
DR Proteomes; UP000247978; 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 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}; Coiled coil {ECO:0000256|SAM:Coils};
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:UP000247978}.
FT DOMAIN 2..475
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 512..800
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT COILED 963..990
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 23..30
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1239 AA; 144530 MW; 4C94CC05A317FA04 CRC64;
MVTWTKEQRE AIERKGSNIL VAAAAGSGKT AVLVERIIQK LMDVEDPLNI DEILVATFTN
AAAEEMRNRI GVALEDAIAK DPTSYHLKKQ LSLLQRASIS TLHSFCTTVV RQYAYLLDID
PSFRIADEME IDLIKQEVID EMFEDAYGAE EEELDRFFTV VDMFSSDRSD VEVEKLVLTL
YTFAMQHPWP EQWLNGVAES YHIEENCSED ELSWLTILKE EVKDQLYSFR SEILRAMDIA
RESDGPYHYL DALEADMNVI DHAIEHAHLW EDLQQSIVSS KLKSLSRKRV ECNEDKKEKV
QKIRSRFREQ WNKMKKNWFS RNIAAHLEDM RLLFPAIKRV TELVIEFKER FSAVKREKAI
VDFLDLEHFC LAILIEPTST LEQIIPSDIA YYYKNQFKEV LVDEYQDINI VQETILSVVS
DDTKRGNMFM VGDVKQSIYR FRHAEPTLFI EKYKRFREDE SHGKRIDLAR NFRSREEILT
GANYIFKQIF DESLGEIEYD TAAELIYGNT SYDNVPIENP ETELLIIDRD TEEKEEQTEG
ESVEDLEATQ LEVRLYAEKI KEWIGTKDKA PMQVIDKATN KKRNIQYRDI VILQRSLTGA
PTIVDELKKQ GIPVYAELRT GYFVAIEIQV MINMLKIIDN PYQDIPLASV LRSPIVGLNE
EQLTQIRLTK RYESFYVALK RYAKDNQDGS ILVQHFLDQH KKFRQLAKEG ALSELIWQIY
RDTGYYDFVG GIPGGRQRQA NLRALYDRAR GYESTSFRGL FRFLRFIERM QEQNKDLGEA
RALSEQEDVV RIMTIHKSKG LEFPVVIIGG MNKEFNFSDI RAKYILDKDQ GFATKFIDPV
KRITYPTLYY VSLQQESLRK LLAEEMRVLY VAMTRAKEKL VMIGNVASFE KKQEKWLQIT
DHLDWILPKQ LRKEAKTYLD WVGPALIRHH QSSLLLGEEE LAVDMPDEIR KDPSQWKLDI
VSATKLTNIN AQVEETKEKL KNTIIHWENA LHANPVFEKE VEERLSFQYT FQEATEARAK
QSVTEIKRRQ ELADVYSDQQ LTLPFRAPLR QRPSFMQVEK TLTAAEIGTA MHTVMQHLPI
SRPLSKEDIK EYVSIFVGEE KITEKEAEVI DLDAIEHFYS TDLAKRMFRS ENVEREVPFT
YTLEASEVYP NWSSETNEKV LLQGVIDCII YTDKGAIILD YKTDKITDEM ITDELITKLK
ARYKIQINLY KQALEDILQQ KVSESYLYFF SRDLLIKCE
//
