ID   ADDA_STRA1              Reviewed;        1207 AA.
AC   Q3K1I4;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 96.
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=SAK_0997;
OS   Streptococcus agalactiae serotype Ia (strain ATCC 27591 / A909 / CDC
OS   SS700).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=205921;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27591 / A909 / CDC SS700;
RX   PubMed=16172379; DOI=10.1073/pnas.0506758102;
RA   Tettelin H., Masignani V., Cieslewicz M.J., Donati C., Medini D.,
RA   Ward N.L., Angiuoli S.V., Crabtree J., Jones A.L., Durkin A.S., DeBoy R.T.,
RA   Davidsen T.M., Mora M., Scarselli M., Margarit y Ros I., Peterson J.D.,
RA   Hauser C.R., Sundaram J.P., Nelson W.C., Madupu R., Brinkac L.M.,
RA   Dodson R.J., Rosovitz M.J., Sullivan S.A., Daugherty S.C., Haft D.H.,
RA   Selengut J., Gwinn M.L., Zhou L., Zafar N., Khouri H., Radune D.,
RA   Dimitrov G., Watkins K., O'Connor K.J., Smith S., Utterback T.R., White O.,
RA   Rubens C.E., Grandi G., Madoff L.C., Kasper D.L., Telford J.L.,
RA   Wessels M.R., Rappuoli R., Fraser C.M.;
RT   "Genome analysis of multiple pathogenic isolates of Streptococcus
RT   agalactiae: implications for the microbial 'pan-genome'.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:13950-13955(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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000114; ABA45488.1; -; Genomic_DNA.
DR   RefSeq; WP_000143231.1; NC_007432.1.
DR   AlphaFoldDB; Q3K1I4; -.
DR   SMR; Q3K1I4; -.
DR   KEGG; sak:SAK_0997; -.
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; 1.
DR   PANTHER; PTHR11070:SF48; PTHR11070:SF48; 1.
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_0000379326"
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;  139446 MW;  8F7247D5DFC85196 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 FYEPILDIEG
     VDVMETITKT SVDFKLPDFS TSKKQDPAAL GSAVHELMQR IEMSSHVKME DIQKALTEVN
     AETSVKAAIQ IEKINYFFQE TSLGKYIQEE VEHLHREAPF AMLKEDPESG EKFVVRGIID
     GYLLLENRII LFDYKTDKFV NPLELKERYQ GQMALYAEAL KKSYEIEKID KYLILLGGKQ
     LEVVKMD