ID   ADDA_STRP1              Reviewed;        1222 AA.
AC   Q9A0H3; Q48ZK5;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 2.
DT   03-AUG-2022, entry version 138.
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=SPy_0777, M5005_Spy0595;
OS   Streptococcus pyogenes serotype M1.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=301447;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700294 / SF370 / Serotype M1;
RX   PubMed=11296296; DOI=10.1073/pnas.071559398;
RA   Ferretti J.J., McShan W.M., Ajdic D.J., Savic D.J., Savic G., Lyon K.,
RA   Primeaux C., Sezate S., Suvorov A.N., Kenton S., Lai H.S., Lin S.P.,
RA   Qian Y., Jia H.G., Najar F.Z., Ren Q., Zhu H., Song L., White J., Yuan X.,
RA   Clifton S.W., Roe B.A., McLaughlin R.E.;
RT   "Complete genome sequence of an M1 strain of Streptococcus pyogenes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:4658-4663(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-947 / MGAS5005 / Serotype M1;
RX   PubMed=16088826; DOI=10.1086/432514;
RA   Sumby P., Porcella S.F., Madrigal A.G., Barbian K.D., Virtaneva K.,
RA   Ricklefs S.M., Sturdevant D.E., Graham M.R., Vuopio-Varkila J., Hoe N.P.,
RA   Musser J.M.;
RT   "Evolutionary origin and emergence of a highly successful clone of serotype
RT   M1 group A Streptococcus involved multiple horizontal gene transfer
RT   events.";
RL   J. Infect. Dis. 192:771-782(2005).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK33717.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE004092; AAK33717.1; ALT_INIT; Genomic_DNA.
DR   EMBL; CP000017; AAZ51213.1; -; Genomic_DNA.
DR   RefSeq; NP_268996.1; NC_002737.2.
DR   AlphaFoldDB; Q9A0H3; -.
DR   SMR; Q9A0H3; -.
DR   STRING; 1314.HKU360_00606; -.
DR   PaxDb; Q9A0H3; -.
DR   EnsemblBacteria; AAK33717; AAK33717; SPy_0777.
DR   KEGG; spy:SPy_0777; -.
DR   KEGG; spz:M5005_Spy0595; -.
DR   PATRIC; fig|160490.10.peg.663; -.
DR   HOGENOM; CLU_001114_3_1_9; -.
DR   OMA; KQSIYRW; -.
DR   Proteomes; UP000000750; 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..1222
FT                   /note="ATP-dependent helicase/nuclease subunit A"
FT                   /id="PRO_0000379340"
FT   DOMAIN          27..483
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT   DOMAIN          512..798
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT   BINDING         48..55
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT   CONFLICT        613
FT                   /note="A -> V (in Ref. 2; AAZ51213)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1222 AA;  140337 MW;  BCD024642672AB91 CRC64;
     MLFNINEKGE PLVISFAPFL SPEAIKHLQE NERCRDQSQK RTAQQIEAIY TSGQNILVSA
     SAGSGKTFVM VERILDKILR GVSIDRLFIS TFTVKAATEL RERIENKLYS QIAQTTDFQM
     KVYLTEQLQS LCQADIGTMD AFAQKVVSRY GYSIGISSQF RIMQDKAEQD VLKQEVFSKL
     FNEFMNQKEA PVFRALVKNF SGNCKDTSAF RELVYTCYSF SQSTENPKIW LQENFLSAAK
     TYQRLEDIPD HDIELLLLAM QDTANQLRDV TDMEDYGQLT KAGSRSAKYT KHLTIIEKLS
     DWVRDFKCLY GKAGLDRLIR DVTGLIPSGN DVTVSKVKYP VFKTLHQKLK QFRHLETILM
     YQKDCFSLLE QLQDFVLAFS EAYLAVKIQE SAFEFSDIAH FAIKILEENT DIRQSYQQHY
     HEVMVDEYQD NNHMQERLLT LLSNGHNRFM VGDIKQSIYR FRQADPQIFN QKFRDYQKKP
     EQGKVILLKE NFRSQSEVLN VSNAVFSHLM DESVGDVLYD EQHQLIAGSH AQTVPYLDRR
     AQLLLYNSDK DDGNAPSDSE GISFSEVTIV AKEIIKLHND KGVPFEDITL LVSSRTRNDI
     ISHTFNQYGI PIATDGGQQN YLKSVEVMVM LDTLRTINNP RNDYALVALL RSPMFAFDED
     DLARIALQKD NELDKDCLYD KIQRAVIGRG AHPELIHDTL LGKLNVFLKT LKSWRRYAKL
     GSLYDLIWKI FNDRFYFDFV ASQAKAEQAQ ANLYALALRA NQFEKSGYKG LYRFIKMIDK
     VLETQNDLAD VEVATPKQAV NLMTIHKSKG LQFPYVFILN CDKRFSMTDI HKSFILNRQH
     GIGIKYLADI KGLLGETTLN SVKVSMETLP YQLNKQELRL ATLSEEMRLL YVAMTRAEKK
     VYFIGKASKS KSQEITDPKK LGKLLPLALR EQLLTFQDWL LAIADIFSTE DLYFDVRFIE
     DSDLTQESVG RLQTPQLLNP DDLKDNRQSE TIARALDMLE AVSQLNANYE AAIHLPTVRT
     PSQLKATYEP LLEPIGVDII EKSSRSLSDF TLPHFSKKAK VEASHIGSAL HQLMQVLPLS
     KPINQQTLLD ALRGIDSNEE VKTALDLKKI ESFFCDTSLG QFFQTYQKHL YREAPFAILK
     LDPISQEEYV LRGIIDAYFL FDDHIVLVDY KTDKYKQPIE LKKRYQQQLE LYAEALTQTY
     KLPVTKRYLV LMGGGKPEIV EV