ID   ADDA_STRA5              Reviewed;        1207 AA.
AC   Q8E061;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 110.
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=SAG0874;
OS   Streptococcus agalactiae serotype V (strain ATCC BAA-611 / 2603 V/R).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=208435;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-611 / 2603 V/R;
RX   PubMed=12200547; DOI=10.1073/pnas.182380799;
RA   Tettelin H., Masignani V., Cieslewicz M.J., Eisen J.A., Peterson S.N.,
RA   Wessels M.R., Paulsen I.T., Nelson K.E., Margarit I., Read T.D.,
RA   Madoff L.C., Wolf A.M., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA   DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., Lewis M.R., Radune D.,
RA   Fedorova N.B., Scanlan D., Khouri H.M., Mulligan S., Carty H.A.,
RA   Cline R.T., Van Aken S.E., Gill J., Scarselli M., Mora M., Iacobini E.T.,
RA   Brettoni C., Galli G., Mariani M., Vegni F., Maione D., Rinaudo D.,
RA   Rappuoli R., Telford J.L., Kasper D.L., Grandi G., Fraser C.M.;
RT   "Complete genome sequence and comparative genomic analysis of an emerging
RT   human pathogen, serotype V Streptococcus agalactiae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:12391-12396(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; AE009948; AAM99760.1; -; Genomic_DNA.
DR   RefSeq; NP_687888.1; NC_004116.1.
DR   RefSeq; WP_000143232.1; NC_004116.1.
DR   AlphaFoldDB; Q8E061; -.
DR   SMR; Q8E061; -.
DR   STRING; 208435.SAG0874; -.
DR   EnsemblBacteria; AAM99760; AAM99760; SAG0874.
DR   KEGG; sag:SAG0874; -.
DR   PATRIC; fig|208435.3.peg.881; -.
DR   HOGENOM; CLU_001114_3_1_9; -.
DR   OMA; KQSIYRW; -.
DR   Proteomes; UP000000821; 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; Reference proteome.
FT   CHAIN           1..1207
FT                   /note="ATP-dependent helicase/nuclease subunit A"
FT                   /id="PRO_0000379328"
FT   DOMAIN          26..482
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT   DOMAIN          508..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;  139412 MW;  138664D929A2C4F9 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
     GLTNLARDIT NVIPSGNDVT VAGVKYPIFK QLHNRIVGLK HLEVIFKYQG ESLFLLELLQ
     SFVLDFSEQY LQEKIQENAF EFSDIAHFAI QILEENHDIR QLYQDKYHEV MVDEYQDNNH
     TQERMLELLS NGHNRFMVGD IKQSIYRFRQ ADPQIFNDKY KAYQDNPSQG KLIILKENFR
     SQSEVLDSTN SVFTHLMDEE VGDILYDESH QLKAGSPRQQ ERHPNNKTQV LLLDTDEDDI
     DDSDSQQYDI 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
     EILPAVKVSM ETLPYQLNKR ELRLATLSEQ MRLLYVAMTR AEKKLYLVGK ASQTKWADHY
     DLVSENNHLP LASRETFVTF QDWLLAVHET YKKQELFYDI NFVSLEELTD HHIGMVNPSL
     PFNPDNKVEN RQSEDIVRAI SVLESVEQIN QTYKAAIELP TVRTPSQVKK IYEPILDIEG
     VDVMETITKT SVDFKLPDFS TSKKQDPAAL GSAVHELMQR IEMSSHVKME DIQKALTEVN
     AETSVKAAIQ IEKINYFFQE TSLGKYIQEE VEHLHREAPF AMLKEDPESG EKFVVRGIID
     GYLLLENRII LFDYKTDKFV NPLELKERYQ GQMALYAEAL KKSYEIEKID KYLILLGGKQ
     LEVVKMD