ADDA_STRPZ
ID ADDA_STRPZ Reviewed; 1222 AA.
AC B5XKR4;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 79.
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=Spy49_0604;
OS Streptococcus pyogenes serotype M49 (strain NZ131).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=471876;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NZ131;
RX PubMed=18820018; DOI=10.1128/jb.00672-08;
RA McShan W.M., Ferretti J.J., Karasawa T., Suvorov A.N., Lin S., Qin B.,
RA Jia H., Kenton S., Najar F., Wu H., Scott J., Roe B.A., Savic D.J.;
RT "Genome sequence of a nephritogenic and highly transformable M49 strain of
RT Streptococcus pyogenes.";
RL J. Bacteriol. 190:7773-7785(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; CP000829; ACI60926.1; -; Genomic_DNA.
DR AlphaFoldDB; B5XKR4; -.
DR SMR; B5XKR4; -.
DR EnsemblBacteria; ACI60926; ACI60926; Spy49_0604.
DR KEGG; soz:Spy49_0604; -.
DR HOGENOM; CLU_001114_3_1_9; -.
DR OMA; KQSIYRW; -.
DR Proteomes; UP000001039; 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_0000379348"
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; 140275 MW; 4C6C28756AA91001 CRC64;
MLFNINEKGE PLVISFAPFL SPEAIKHLQE NERCSDQSQK RTAQQIEAIY TSGQNILVSA
SAGSGKTFVM VERILDKILR GVSIDRLFIS TFTVKAATEL RERIENKLYS QIAQTTDFQM
KVYLTEQLQS LCQADIGTMD AFAQKVVSRY GYSIGISSQF RIMQDKAEQD VLKQEVFSKL
FSEFMNQKEA 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 QKFRDYQKKT
EQGKVILLKE NFRSQSEVLN VSNAVFSHLM DESVGDVLYD EQHQLIAGSH AQTVPYLDRR
AQLLLYNSDK DDGNAPSDSE GISFSEVTIV AKEIIKLHND KGVPFEDITL LVSSRTRNDI
ISHTFNQYGI PIVTDGGQQN YLKSVEVMVM LDTLRTINNP RNDYALVALL RSPMFAFDED
DLARIALQKD NELDKDCLYD KIQRAVIGRG AYPELIHDTL LGKLNVFLKT LKSWRRYAKL
GSLYDLILEN FHERFYFDFV 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
