ID   ADDA_ALKMQ              Reviewed;        1197 AA.
AC   A6TVN2;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=ATP-dependent helicase/nuclease subunit A {ECO:0000255|HAMAP-Rule:MF_01451};
DE            EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_01451};
DE            EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_01451};
DE   AltName: Full=ATP-dependent helicase/nuclease AddA {ECO:0000255|HAMAP-Rule:MF_01451};
GN   Name=addA {ECO:0000255|HAMAP-Rule:MF_01451}; OrderedLocusNames=Amet_4169;
OS   Alkaliphilus metalliredigens (strain QYMF).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Alkaliphilus.
OX   NCBI_TaxID=293826;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=QYMF;
RX   PubMed=27811105; DOI=10.1128/genomea.01226-16;
RA   Hwang C., Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina Del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F.,
RA   Land M.L., Hauser L., Kyrpides N., Mikhailova N., Ye Q., Zhou J.,
RA   Richardson P., Fields M.W.;
RT   "Complete genome sequence of Alkaliphilus metalliredigens strain QYMF, an
RT   alkaliphilic and metal-reducing bacterium isolated from borax-contaminated
RT   leachate ponds.";
RL   Genome Announc. 4:0-0(2016).
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:0000255|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=3.6.4.12;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01451};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01451};
CC   -!- SUBUNIT: Heterodimer of AddA and AddB/RexB. {ECO:0000255|HAMAP-
CC       Rule:MF_01451}.
CC   -!- SIMILARITY: Belongs to the helicase family. AddA subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01451}.
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DR   EMBL; CP000724; ABR50250.1; -; Genomic_DNA.
DR   RefSeq; WP_012065198.1; NC_009633.1.
DR   AlphaFoldDB; A6TVN2; -.
DR   SMR; A6TVN2; -.
DR   STRING; 293826.Amet_4169; -.
DR   EnsemblBacteria; ABR50250; ABR50250; Amet_4169.
DR   KEGG; amt:Amet_4169; -.
DR   eggNOG; COG1074; Bacteria.
DR   HOGENOM; CLU_001114_3_1_9; -.
DR   OMA; KQSIYRW; -.
DR   OrthoDB; 137860at2; -.
DR   Proteomes; UP000001572; Chromosome.
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:0000724; P:double-strand break repair via homologous recombination; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.300; -; 4.
DR   Gene3D; 3.90.320.10; -; 1.
DR   HAMAP; MF_01451; AddA; 1.
DR   InterPro; IPR014152; DNA_helicase_suAddA.
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   PANTHER; PTHR11070; PTHR11070; 1.
DR   PANTHER; PTHR11070:SF48; PTHR11070:SF48; 1.
DR   Pfam; PF12705; PDDEXK_1; 1.
DR   Pfam; PF00580; UvrD-helicase; 1.
DR   Pfam; PF13361; UvrD_C; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF52980; SSF52980; 1.
DR   TIGRFAMs; TIGR02785; addA_Gpos; 1.
DR   PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR   PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE   3: Inferred from homology;
KW   ATP-binding; DNA damage; DNA repair; DNA-binding; Exonuclease; Helicase;
KW   Hydrolase; Nuclease; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..1197
FT                   /note="ATP-dependent helicase/nuclease subunit A"
FT                   /id="PRO_0000379227"
FT   DOMAIN          2..458
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT   DOMAIN          485..774
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT   BINDING         23..30
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
SQ   SEQUENCE   1197 AA;  137876 MW;  96F2A495DF5054D9 CRC64;
     MKNWTTEQQA AIDARGSNLL ISAAAGSGKT AVLVERIIQI ILKDKIDIDR LLIVTFTNAA
     AGEMRERIAG AIMEEMERKT EQEAHLRRQI NLLNRASITT IHSFCIDVVR RHFHIIDVDP
     GFRIGDITET SIMRLEALEE LFEEEYQGAH ETFFRLVEAF GGTKEDRPLQ DLVLKVYGFI
     QSQPYPEVWL KEKVGDFSLS IEDFDESLWI KTIKSRIEIQ LKGAMDLLNN ALSIAQEPGG
     PEVYEEAILS DLGQISELYD SLTLPITSFY EHLNHINHAR LKPSKESDPV LKEESKNLRD
     KAKGIIKDIK DNIFTVSPEA YVEDLNKLHP LMDYLYQLVT GFTSRYAQKK ADRGIVDFND
     LEHYGLEILA NELVAQEYQQ RFEYIFVDEY QDSNIVQETL IQSIKRKDNL FMVGDVKQSI
     YRFRLADPSL FIEKYETFGE KEGDINRRID LAKNFRSRGE VLAGVNYLFK YIMSKELGEI
     GYDHRAALYQ GASFESIKEP SIEVNLIEKN MEIDEDIEEE LQELADIEVE ARIIAKRIKD
     LLNEEIYDEK NEVYRRLEFK DIVVLLRTTK NWAQSFLEAF IREGIPAYAD ANTGYFEAIE
     VGMFLNLLKV IDNKRQDIPL ISVMRSPIGE FTTAELIDIR INDKNGTYYD AIEKYIEKNE
     DALKDKLVSF IEKLNKWGNE ARYIKIDQFI WKLLMDTGFY YYVGAMPGGL QRQANLRILF
     DRASQFEKTS IKGLFNFIKF IEKLQGSKGD MGAAKILGEN DNVVRIMSIH KSKGLEFPVV
     IAAGMGKNFN LRDTSADVLL HKDLGLGPKF VDSNLRTYRD SIAKLAMKDQ IKIESLSEEM
     RILYVAFTRP KDKLIIVGSL RKIDRLVTNW NQADNIYSLM NAKSYLDWIG AALIKHPHGE
     VLRELGDFEF NELKYKAEDS KWTVNILGRQ AVVLEEHEKR LKEEEYKEKL THFNREDFSP
     HRHTEHKEEI DNRLNWQYPY PQATVIPSKL SVSDIKKANM GEMDSIVHQI PTLVKTPKFM
     EGKKALTAAE RGTIIHFVLQ HLALNQVGSE EEISQQIDLM VARELITEEE AQVVNVGKIV
     NYFKSEIGKR MLGAEKVYRE SPFIIEKSAK DVIHGLSENL EEKLLVQGVI DCYFEEMDGL
     VLVDYKNDIV LNGDTASIMT RYDVQLMMYA EALERITGKQ VKETYLYLFD VDQGVKR