ADDA_STRPM
ID ADDA_STRPM Reviewed; 1222 AA.
AC Q48UB8;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
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=M28_Spy0574;
OS Streptococcus pyogenes serotype M28 (strain MGAS6180).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=319701;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGAS6180;
RX PubMed=16088825; DOI=10.1086/430618;
RA Green N.M., Zhang S., Porcella S.F., Nagiec M.J., Barbian K.D., Beres S.B.,
RA Lefebvre R.B., Musser J.M.;
RT "Genome sequence of a serotype M28 strain of group A Streptococcus:
RT potential new insights into puerperal sepsis and bacterial disease
RT specificity.";
RL J. Infect. Dis. 192:760-770(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}.
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DR EMBL; CP000056; AAX71688.1; -; Genomic_DNA.
DR AlphaFoldDB; Q48UB8; -.
DR SMR; Q48UB8; -.
DR EnsemblBacteria; AAX71688; AAX71688; M28_Spy0574.
DR KEGG; spb:M28_Spy0574; -.
DR HOGENOM; CLU_001114_3_1_9; -.
DR OMA; KQSIYRW; -.
DR Proteomes; UP000009292; 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_0000379345"
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; 140318 MW; 40ADD32495E7C26C CRC64;
MLFNINEKGE PLVISFAPFL SPEAIKHLQE NERCSDQSQK RTAQQIEAIY TSGQNILVSA
SAGSGKTFVM VERILDKILR GVSIDRLFIS TFTVKAATEL RERIENKLYS QIAQTTDFQM
KVYLTEQLQS LGQADIGTMD 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 SAFEFSDITH FAIKILEENT DIRQSYQQHY
HEVMVDEYQD NNHMQERLLT LLSNGHNRFM VGDIKQSIYR FRQADPQIFN QKFRDYQKKP
EQGKVILLKE NFRSQSEVLN VSNAVFSHLM DESVGDVLYD EQHQLIAGSH AQTVPYLDRR
AQLLLYNSDK DDGNAPSDSE GISFSEVTIV AKEIIKLHND KGVPFEDITL LVSSRTRNDI
ISHTFNQYSI 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
PSQLKAAYEP LLEPIGVDII EKSSRSLSDF TLPHFSKKVK VEASHIGSAL HQLMQVLPLS
KPINQQTLLD ALREIDSNEE VKTALDLKKI ESFFCDTSLG QFFQTYQKHL YREAPFAILK
VDPISQEEYV LRGIIDAYFL FDDHIVLVDY KTDKYKQPIE LKKRYQQQLE LYAEALTQTY
KLPVTKRYLV LMGGGKPEIV EV
