ADDA_STRPD
ID ADDA_STRPD Reviewed; 1222 AA.
AC Q1JHM1;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 1.
DT 03-AUG-2022, entry version 100.
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=MGAS10270_Spy0650;
OS Streptococcus pyogenes serotype M2 (strain MGAS10270).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=370552;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGAS10270;
RX PubMed=16636287; DOI=10.1073/pnas.0510279103;
RA Beres S.B., Richter E.W., Nagiec M.J., Sumby P., Porcella S.F., DeLeo F.R.,
RA Musser J.M.;
RT "Molecular genetic anatomy of inter- and intraserotype variation in the
RT human bacterial pathogen group A Streptococcus.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7059-7064(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; CP000260; ABF33715.1; -; Genomic_DNA.
DR AlphaFoldDB; Q1JHM1; -.
DR SMR; Q1JHM1; -.
DR EnsemblBacteria; ABF33715; ABF33715; MGAS10270_Spy0650.
DR KEGG; sph:MGAS10270_Spy0650; -.
DR HOGENOM; CLU_001114_3_1_9; -.
DR OMA; KQSIYRW; -.
DR Proteomes; UP000002436; 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.
FT CHAIN 1..1222
FT /note="ATP-dependent helicase/nuclease subunit A"
FT /id="PRO_0000379344"
FT DOMAIN 39..495
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT DOMAIN 524..810
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT BINDING 60..67
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
SQ SEQUENCE 1222 AA; 140217 MW; 608495B19FBFC62B CRC64;
MLFNINEKGE PLVISFAPFL SPEAIKHLQE NERCSDQSQK 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
YQKDCFPLLE QLQDFVLAFS EAYLAVKIQE SAFEFSDIAH FAIKILEENT DIRQSYQQHY
HEVMVDEYQD NNHMQERLLT LLSNGHNRFM VGDIKQSIYR FRQADPQIFN QKFRDYQKKP
EQGKVILLKE NFRSQSEVLN VSNAVFSHLM DESVGDALYD EQHQLIAGSH AQTVPYLDRR
AQLLLYNSDK DDGNAPSDSE GISFSEVTIV AKEIIKLHND KGVPFEDITL LVSSRTRNDI
ISHTFNQYGI PIVTDGGQQN YLKSVEVMVM LDTLRTINNP RNDYALVALL RSPMFAFDED
DLARIALQKD NELDKDCLYD KIQRAVIGRG AHPELIHDTL LGKLNIFLKT LKSWRRYAKL
GSLYDLIWKI FNDRFYFDFV ASQAKAEQAQ ANLYALALRA NQFEKSGYKG LYRFIKMIDK
VLETQNDLAD VEVAAPKQAV NLMTIHKSKG LQFPYVFILN CDKRFSMTDI HKSFILNRQH
GIGIKYLADI KGLLGETTLN SVKVSMETLP YQLNKQELRL ATLSEQMRLL YVAMTRAEKK
VYFIGKASKS KSQDITDPKK LGKLLPLALR EQLLTFQDWL LAIADIFSTE DLYFDVRFIE
DSDLTQESVG RLQTPQLLNP DDLKDNRQSE TIARALDMLE AVSQLNANYE AAIHLPTVRT
PSQLKATYEP LLEPIGVDII EKSSRSLSDF TLPHFSKKAK VEVSHIGSAL HQLMQVLPLS
KPINQQTLLD ALRGIASNEE VKTALDLKKI ESFFCDTSLG QFFQTYQKHL YREAPFAILK
LDPISQEEYV LRGIIDAYFL FDDHIVLVDY KTDKYKQPIE LKKRYQQQLE LYAEALTQTY
KLPVTKRYLV LMGGGNPEIV EV
