ADDA_STRA3
ID ADDA_STRA3 Reviewed; 1207 AA.
AC Q8E5T9;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 111.
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}; OrderedLocusNames=gbs0891;
OS Streptococcus agalactiae serotype III (strain NEM316).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=211110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEM316;
RX PubMed=12354221; DOI=10.1046/j.1365-2958.2002.03126.x;
RA Glaser P., Rusniok C., Buchrieser C., Chevalier F., Frangeul L., Msadek T.,
RA Zouine M., Couve E., Lalioui L., Poyart C., Trieu-Cuot P., Kunst F.;
RT "Genome sequence of Streptococcus agalactiae, a pathogen causing invasive
RT neonatal disease.";
RL Mol. Microbiol. 45:1499-1513(2002).
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; AL766847; CAD46535.1; -; Genomic_DNA.
DR RefSeq; WP_000143226.1; NC_004368.1.
DR AlphaFoldDB; Q8E5T9; -.
DR SMR; Q8E5T9; -.
DR STRING; 211110.gbs0891; -.
DR EnsemblBacteria; CAD46535; CAD46535; CAD46535.
DR KEGG; san:gbs0891; -.
DR eggNOG; COG1074; Bacteria.
DR HOGENOM; CLU_001114_3_1_9; -.
DR OMA; KQSIYRW; -.
DR Proteomes; UP000000823; 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..1207
FT /note="ATP-dependent helicase/nuclease subunit A"
FT /id="PRO_0000379327"
FT DOMAIN 26..482
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT DOMAIN 510..794
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 1207 AA; 139387 MW; 7CC9A91D88356907 CRC64;
MTFKPFLNPE DIAVIQTEEK NSDKKQKRTP EQIEAIYTFG NNVLVSASAG SGKTFVMVER
ILDKLLRGVP IDSLFISTFT VKAAGELKER LEKKINESLK SAESDDLKQF LTQQLVGIQT
ADIGTMDAFT QKIVNQYGYT LGISPIFRIL QDKNEQDVIK NEVYADLFSD YMTGKNAASF
IKLVKNFSGN RKDSKAFREM VYKVYAFSQS TDNPKRWMQT VFLKGAQTYT DFEAIPDQEV
SSLLNVMQTT ANQLRDLTDQ EDYKQLTAKG VPTANYKKHL KIIENLVHWS QDFNLLYGKK
GLANLARDIT NVIPSGNDVT VAGVKYPIFK QLHNRIVGLK HLEVIFKYQG ESLFLLELLQ
SFVLDFSEQY LQEKIQENAF EFSDIAHFAI QILEENHDIR QLYQDKYHEV MVDEYQDNNH
TQERMLELLS NGHNRFMVGD IKQSIYRFRQ ADPQIFNDKY KAYQDNPSQG KLIILKENFR
SQSEVLDSTN SVFTHLMDEE VGDILYDESH QLKAGSPRQQ ERHPNNKTQV LLLDTDEDDI
NDSDSQQYDI SPAEAKLVAK EIIRLHKEEN VPFQDITLLV SSRTRNDGIL QTFDRYGIPL
VTDGGEQNYL KSVEVMVMLD TLRSIDNPLN DYALVALLRS PMFGFNEDDL TRIAIQDVKM
AFYHKVKLSY HKEGHHSDLI TPELSSKIDH FMKTFQTWRD FAKWHSLYDL IWKIYNDRFY
YDYVGALPKA EQRQANLYAL ALRANQFEKT GFKGLSRFIR MIDKVLENEN DLADVEVALP
QNAVNLMTIH KSKGLEFKYV FILNIDKKFS MVDITSPLIL SRNQGIGIKY VADMRHELEE
ELLPAVKVSM ETLPYQLNKR ELRLATLSEQ MRLLYVAMTR AEKKLYLVGK ASQTKWADHY
DLVSENNHLP LASRETFVTF QDWLLAVHET YKKQELFYDI NFVSLEELTD HHIGMVNPSL
PFNPDNKAEN RQSEDIVRAI SVLESVEQIN QTYKAAIELP TVRTPSQVKK FYEPILDIEG
VDVMETITKT SVDFKLPDFS TSKKQDPAAL GSAVHELMQR IEMSSHVKME DIQKALTEVN
AETSVKAAIQ IEKINYFFQE TSLGKYIQEE VEHLHREAPF AMLKEDPESG EKFVVRGIID
GYLLLENRII LFDYKTDKFV NPLELKERYQ GQMALYAEAL KKSYEIEKID KYLILLGGKQ
LEVVKMD
