ID   ADDA_STRT2              Reviewed;        1217 AA.
AC   Q5M2T7;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 107.
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}; Synonyms=rexA;
GN   OrderedLocusNames=stu1716;
OS   Streptococcus thermophilus (strain ATCC BAA-250 / LMG 18311).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=264199;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-250 / LMG 18311;
RX   PubMed=15543133; DOI=10.1038/nbt1034;
RA   Bolotin A., Quinquis B., Renault P., Sorokin A., Ehrlich S.D.,
RA   Kulakauskas S., Lapidus A., Goltsman E., Mazur M., Pusch G.D., Fonstein M.,
RA   Overbeek R., Kyprides N., Purnelle B., Prozzi D., Ngui K., Masuy D.,
RA   Hancy F., Burteau S., Boutry M., Delcour J., Goffeau A., Hols P.;
RT   "Complete sequence and comparative genome analysis of the dairy bacterium
RT   Streptococcus thermophilus.";
RL   Nat. Biotechnol. 22:1554-1558(2004).
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; CP000023; AAV61315.1; -; Genomic_DNA.
DR   RefSeq; WP_011226520.1; NC_006448.1.
DR   AlphaFoldDB; Q5M2T7; -.
DR   SMR; Q5M2T7; -.
DR   STRING; 264199.stu1716; -.
DR   DNASU; 3165569; -.
DR   EnsemblBacteria; AAV61315; AAV61315; stu1716.
DR   KEGG; stl:stu1716; -.
DR   PATRIC; fig|264199.4.peg.1688; -.
DR   eggNOG; COG1074; Bacteria.
DR   HOGENOM; CLU_001114_3_1_9; -.
DR   OMA; KQSIYRW; -.
DR   Proteomes; UP000001170; 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; 2.
DR   PANTHER; PTHR11070:SF48; PTHR11070:SF48; 2.
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..1217
FT                   /note="ATP-dependent helicase/nuclease subunit A"
FT                   /id="PRO_0000379354"
FT   DOMAIN          26..487
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT   DOMAIN          515..799
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT   BINDING         47..54
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
SQ   SEQUENCE   1217 AA;  138365 MW;  83ACE0ABF088AE11 CRC64;
     MLTKAFLSPA EIEERIAQEA ASDKDRKLTP EQIEAIYSNG TNILVSASAG SGKTFVMVER
     ILDMIGRGVG IDQLFISTFT VKAAGELKER LEKRLTKHLG QAETDEERAF LSDQIAKIGT
     ADIGTMDAFT QKLVNQYGYL LGVSPTFRIM TDLAEQTLMK NEVYADLFND YMQGKDAQLF
     QKLVRNFTGH SKTSKAFRDL VYDIYSFSQA TADPEKWLCQ NLLKGQIEAK PEQAKNELLD
     GLKDGLLADF LAFLRDHLGI AQREFAKAKY LNNVSDAIIL LEGSLINDQT DMEDLLKQLL
     TLSGGTGLTN MTRPKDEELK AYKEAYNKTK NEFVAQLREV DTQLTVLEVL TKHNDDILPM
     LELLQSFVLD FSDQYLQAKI QENTFEFSDI AHFAIRILEE NPEVAVSYRD RYHEVMVDEY
     QDNSHTQERM LELLSNGHNR FMVGDIKQSI YRFRQADPQI FNDKFQLFLE NPDAGKLILL
     KENFRSQSEV LDATNGVFSH LMDQEIGDIL YDKTHMLVAG SQKQKEPHPE NETEVLIYNS
     DESSTSEDEE GPDQAISSGE ISLVIKEIIK LHEQGVRFED ITLLAPNRNT YLDLMVSFEE
     HGIPLVPDEY KSSYLESLEV MIMLDTLRAI NNPLNDYALV ALLRSPMFNF NEDDLTRIAV
     QADKGQFYDK LLAAHTKSGL HPEVVMQGLE AKLTLFTETL ADWRDYSKCH SIYDLIWKIY
     NDRFYYDYVG GLPRAEQRQA NLYALALRAN AYEKTGFKGL SRFIGMIDKI IASGNDLEEV
     TDLVPKNAVS LMTIHKSKGL EFKYVFVLQM NRKFIGHSKD GLSGKYIINR EKGLGIKYLA
     DLKDQINTNL PKLNVVLETL TFQENRREER RASISEEMRL LYVAMTRAEK KLYLVGKGSK
     ETLTQQYGTD VENNRLPVAL RDQIATYQDW IMALDTAFMR KDLKFTVRFV EDEELTPEAI
     GQVEVKAAVD ADDLSNNRQT EEIERALTVL ESVEKLNHLY APAIDLPSVR TPSQLKTFYE
     PIMDTEGVDI MDKKEGVQPL ETASTFELPD FGQKTKVTGA AVGSATHELM QRLTLSDTVT
     LQDLTQALSR VSASDQVKAR VQLEKLLGFF DTELGKLILA NRDKLRREAP FAMLAEDPAS
     KEDFVVRGII DGYLLLEDRI VLFDYKTDHF THPSELKTRY QGQMSLYAKA LSQAYQMEKV
     DKYLILLGGK DLEVVEV