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ADDA_LACH4
ID   ADDA_LACH4              Reviewed;        1204 AA.
AC   A8YVK0;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 84.
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=lhv_1273;
OS   Lactobacillus helveticus (strain DPC 4571).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=405566;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DPC 4571;
RX   PubMed=17993529; DOI=10.1128/jb.01295-07;
RA   Callanan M., Kaleta P., O'Callaghan J., O'Sullivan O., Jordan K.,
RA   McAuliffe O., Sangrador-Vegas A., Slattery L., Fitzgerald G.F.,
RA   Beresford T., Ross R.P.;
RT   "Genome sequence of Lactobacillus helveticus: an organism distinguished by
RT   selective gene loss and IS element expansion.";
RL   J. Bacteriol. 190:727-735(2008).
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; CP000517; ABX27287.1; -; Genomic_DNA.
DR   RefSeq; WP_012211953.1; NC_010080.1.
DR   AlphaFoldDB; A8YVK0; -.
DR   SMR; A8YVK0; -.
DR   STRING; 405566.lhv_1273; -.
DR   PRIDE; A8YVK0; -.
DR   EnsemblBacteria; ABX27287; ABX27287; lhv_1273.
DR   KEGG; lhe:lhv_1273; -.
DR   eggNOG; COG1074; Bacteria.
DR   HOGENOM; CLU_001114_3_1_9; -.
DR   OMA; KQSIYRW; -.
DR   Proteomes; UP000000790; 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.
FT   CHAIN           1..1204
FT                   /note="ATP-dependent helicase/nuclease subunit A"
FT                   /id="PRO_0000379283"
FT   DOMAIN          2..472
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT   DOMAIN          500..783
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   1204 AA;  139431 MW;  1C17EB96CC6335DB CRC64;
     MPQFTKEQEK AINDRGHDIL VSASAGSGKT TVLVERVLKE ILAGTQVDEL LVVTFTKAAA
     EEMKTRIKAA LTKEMAKPGV DYRYLREQLN QIDTANISTI DAFCLDVIHR FYYSIELDPS
     FTILTDDTQA TLLKERALRE IEGEMLTSKD KAFRHFYDNF AGDRDADSPR DLLLDLYNFA
     MAKPEYKKWL AQLPQIYEIE DSVIGSKIWQ KQIKPYIATK FSKLQEKIAS YLTQAIMETK
     ELAKVKESFT LFAQNLNNFV QAVKEDDDYD KQRELLRSCV FTINFRKSKK WDEDLLEFYN
     EIQSLKDEAK SQVFDTFTSF YAVTEKEQIK IMQESQKIVT AISTAEIKLI ERFNQLKRNE
     NLLDYSDMEQ LAYQILSQDT SSSQMARDFY QNKFKEILID EYQDINALQE RIIQQIKSEK
     KNTLFMVGDV KQSIYGFRQA EPSLFLQKYH QFAEDENEHE ERILLSDNFR STEPVTQTVN
     AVFKSILSTD FGGIDYQKEG QLIFGAKYYP KSLPQASEVI VHEKKNNNEK SENEIDFSEI
     QMVLARIKQL EDEHVQIFDS NTGKMRDMEY SDIAILTRSR SDNLEIMQEF AKQDIPLFVT
     DAENYFQTFE LTVMMNYLKI IDNPDQDIPL VTVLRSPLFN FDEKELAKIR IKSKNSNFYS
     ALTSYVGTND VLSKKCKNFL NQLAELRSFA TTHRISELIW SIYERTNLLE IMTALPNGEQ
     RRVNLEALYE RATSYESAGF KGLYQFINFI DRMRRSQKDL AQPLLTKEAG NAVRLMTIHG
     SKGLEFPIVF YVGMQHHYQM RDLNGNYIIN SDSMGITLRE QNYRVDSLVK AMGNITKKQQ
     LLEEEARILY VALTRAKQKL ILVGDVPSFN KKVKEWSTEL NHAGQLPLIN KLSATSPLSF
     IGPSLRFDRH VAIKLNDITK SIDQSQKILF IDYQDEDTKF IKKDEDTDNQ NENTRKSALL
     TQTVNKLYQF NYPFRDASET TAYQAVSEIK KAFNDPIDAE LENSHLLTST NRYLQPIDTK
     PNFLYQTKFT GAEIGTATHL ILQYYDYTND SADNLDQEIA TLIEQKKLNP DIVSSLNKDQ
     IDWFVHGDFA KDFWKEPTNL KREVDFSSLL SARTLFKDFS DPDAKILVHG TIDGYFVAKN
     GIILFDYKTD HVNKTNIDKS IELIKEKYTG QLRLYEQALN EFSEKKVIGK YLILLDAKQV
     VEVK
 
 
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