ID   ADDA_STRTD              Reviewed;        1217 AA.
AC   Q03IZ8;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 98.
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=STER_1681;
OS   Streptococcus thermophilus (strain ATCC BAA-491 / LMD-9).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=322159;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-491 / LMD-9;
RX   PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA   Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V.,
RA   Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA   Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA   Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA   Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA   Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA   Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J.R., Hutkins R.,
RA   O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T.,
RA   Richardson P., Kozyavkin S., Weimer B.C., Mills D.A.;
RT   "Comparative genomics of the lactic acid bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006).
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; CP000419; ABJ66824.1; -; Genomic_DNA.
DR   RefSeq; WP_011681595.1; NC_008532.1.
DR   AlphaFoldDB; Q03IZ8; -.
DR   SMR; Q03IZ8; -.
DR   PRIDE; Q03IZ8; -.
DR   KEGG; ste:STER_1681; -.
DR   HOGENOM; CLU_001114_3_1_9; -.
DR   OMA; KQSIYRW; -.
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..1217
FT                   /note="ATP-dependent helicase/nuclease subunit A"
FT                   /id="PRO_0000379355"
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;  138310 MW;  6367C67980BF0CBF CRC64;
     MLTKAFLSPA EIEERIAQEA ASDKDRKLTP EQIEAIYSNG TNILVSASAG SGKTFVMVER
     ILDMIGRGVG IDQLFISTFT VKAAGELKER LEKRLTKHLG QAETDEERAF LSDQIAKIGT
     ADIGTMDAFT QKLVNQYGYL LGVSPTFRIM TDLAEQTLMK NEVYADLFND YMQGKDAQLF
     QKLVRNFTGH SKTSKAFRDL VYDIYSFSQA TADPEKWLRQ NLLKGQIEAK PEQAKNELLD
     SLKDGLLADF LAFLRDHLGI AQREFAKAKY LNNVSDAIIL LEGSLINDQT DMEDLLKQLL
     TLSGGTGLTN MTRPKDEELK AYKEAYNKTK NEFVAQLREV DTQLTVLEVL AKHNDDILPM
     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 HPEVVMQGLD AKLTLFTETL ADWRDYSKCH SIYDLIWKIY
     NDRFYYDYVG GLPRAEQRQA NLYALALRAN AYEKTGFKGL SRFIGMIDKI IASGNDLEEV
     TDLVPKNAVS LMTIHKSKGL EFKYVFVLQM NRKFIGHSKD GLSGKYIINR EKGLGIKYLA
     DLKDQINTNL PKLNVVLETL TFQENRREER RASISEEMRL LYVAMTRAEK KLYLVGKGSK
     ETLTQQYGTN VENNRLPVAI RDQIATYQDW IMALDTAFMR KDLKFTVRFV EAEELTPEAI
     GQVEVQAAVD ADDLSNNRQT EDIKRALTVL ESVEKLNQLY APAIDLPSVR TPSQLKTLYE
     PIMDTEGVDI MDKKEGVQPL ETASTFELPD FGQKTKVTGA AVGSATHELM QRLILSDKVT
     LQDLTQALSR VSADDQVKAR VQLEKLLGFF DTELGKLILA NRGKLRREAP FAMLAEDPAS
     KEDFVVRGII DGYLLLEDRI VLFDYKTDHF THPSELKTRY QGQMSLYAKA LSQAYQMEKV
     DKYLILLGGK DLEVVEV