ADDA_STRT1
ID ADDA_STRT1 Reviewed; 1217 AA.
AC Q5LY80;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 103.
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=str1716;
OS Streptococcus thermophilus (strain CNRZ 1066).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=299768;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CNRZ 1066;
RX PubMed=15543133; DOI=10.1038/nbt1034;
RA Bolotin A., Quinquis B., Renault P., Sorokin A., Ehrlich S.D.,
RA Kulakauskas S., Lapidus A., Goltsman E., Mazur M., Pusch G.D., Fonstein M.,
RA Overbeek R., Kyprides N., Purnelle B., Prozzi D., Ngui K., Masuy D.,
RA Hancy F., Burteau S., Boutry M., Delcour J., Goffeau A., Hols P.;
RT "Complete sequence and comparative genome analysis of the dairy bacterium
RT Streptococcus thermophilus.";
RL Nat. Biotechnol. 22:1554-1558(2004).
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; CP000024; AAV63236.1; -; Genomic_DNA.
DR RefSeq; WP_011227531.1; NC_006449.1.
DR AlphaFoldDB; Q5LY80; -.
DR SMR; Q5LY80; -.
DR KEGG; stc:str1716; -.
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; 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..1217
FT /note="ATP-dependent helicase/nuclease subunit A"
FT /id="PRO_0000379356"
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; 138351 MW; F133F4E0E43988A9 CRC64;
MLTKAFLSPA EIEERIAQEA ASDKDRKLTP EQIEAIYSNG TNILVSASAG SGKTFVMVER
ILDMIGRGVG IDQLFISTFT VKAAGELKER LEKRLTKHLG QAETDEERAF LSDQIAKIGT
ADIGTMDAFT QKLVNQYGYL LGVSPTFRIM TDLAEQTLMK NEVYADLFND YMQGKDAQLF
QKLVRNFTGH SKTSKAFRDL VYDIYSFSQA TADPEKWLCQ NLLKGQIEAK PEQAKNELLD
GLKDGLLADF LAFLRDHLGI AQREFAKAKY LNNVSDAIIL LEGSLINDQT DMEDLLKQLL
TLSGGTGLTN MTRPKDEELK AYKEAYNKTK NEFVAQLREV DTQLTVLEVL TKHNDDILPM
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 HPEVVMQGLE AKLTLFTETL ADWRDYSKCH SIYDLIWKIY
NDRFYYDYVG GLPRAEQRQA NLYALALRAN AYEKTGFKGL SRFIGMIDKI IASGNDLEEV
TDLVPKNAVS LMTIHKSKGL EFKYVFVLQM NRKFIGHSKD GLSGKYIINR EKGLGIKYLA
DLKDQINTNL PKLNVVLETL TFQDNRREER RASISEEMRL LYVAMTRAEK KLYLVGKGSK
ETLTQQYGTD VENNRLPVAL RDQIATYQDW IMALDTAFMR KDLKFTVRFV EDEELTPEAI
GQVEVKAAVD ADDLSNNRQT EEIERALTVL ESVEKLNHLY APAIDLPSVR TPSQLKTFYE
PIMDTEGVDI MDKKEGVQPL ETASTFELPD FGQKTKVTGA AVGSATHELM QRLTLSDTVT
LQDLTQALSR VSASDQVKAR VQLEKLLGFF DTELGKLILA NRDKLRREAP FAMLAEDPAS
KEDFVVRGII DGYLLLEDRI VLFDYKTDHF THPSELKTRY QGQMSLYAKA LSQAYQMEKV
DKYLILLGGK DLEVVEV
