ID   ADDA_STRS7              Reviewed;        1214 AA.
AC   C0MGY6;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 86.
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=SZO_11320;
OS   Streptococcus equi subsp. zooepidemicus (strain H70).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=553483;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H70;
RX   PubMed=19325880; DOI=10.1371/journal.ppat.1000346;
RA   Holden M.T.G., Heather Z., Paillot R., Steward K.F., Webb K., Ainslie F.,
RA   Jourdan T., Bason N.C., Holroyd N.E., Mungall K., Quail M.A., Sanders M.,
RA   Simmonds M., Willey D., Brooks K., Aanensen D.M., Spratt B.G., Jolley K.A.,
RA   Maiden M.C.J., Kehoe M., Chanter N., Bentley S.D., Robinson C.,
RA   Maskell D.J., Parkhill J., Waller A.S.;
RT   "Genomic evidence for the evolution of Streptococcus equi: host
RT   restriction, increased virulence, and genetic exchange with human
RT   pathogens.";
RL   PLoS Pathog. 5:E1000346-E1000346(2009).
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; FM204884; CAW99551.1; -; Genomic_DNA.
DR   AlphaFoldDB; C0MGY6; -.
DR   SMR; C0MGY6; -.
DR   PRIDE; C0MGY6; -.
DR   EnsemblBacteria; CAW99551; CAW99551; SZO_11320.
DR   KEGG; seq:SZO_11320; -.
DR   eggNOG; COG1074; Bacteria.
DR   HOGENOM; CLU_001114_3_1_9; -.
DR   OMA; KQSIYRW; -.
DR   Proteomes; UP000001368; 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..1214
FT                   /note="ATP-dependent helicase/nuclease subunit A"
FT                   /id="PRO_0000379329"
FT   DOMAIN          27..483
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT   DOMAIN          512..800
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT   BINDING         48..55
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
SQ   SEQUENCE   1214 AA;  138272 MW;  B014E85539BFFC8C CRC64;
     MRIDEGFLTP EAIARLQQEE ALSDKTHKRT AQQIEAIYSS GQNILVSASA GSGKTFVMVE
     RILDKILRGI PVDRLFISTF TVKAATELIE RIEKKLHTAI AETQDYQLKA YLNDQLQALS
     QADIGTMDAF AQKLVHQHGY VLGISPHFRI IQDKAEQDIL KREVFRQVFE DYMSQTDNKA
     FIQLVQNFSG RRKDSSAFRE IVDSIYAFSQ STANPSSWLA EVFLRGSKTY TSFADIPDQA
     VDTLLACMQD TADQLRDLTD MEGYAQTTKA GKLTAKYTKH LKMIDSLYEW ALHFDSLYGK
     ARLGQLAQEL TALLPSGADI TVAGHKYPIF KSLQEQLVGF RHLETILAYQ QESLPLLEVL
     QAFVISFSEA YLAAKMQENA FEFSDIAHFA IEILQQAPDI RQAYQGHYHE VMVDEYQDNN
     HMQERLLELL SNGHNRFMVG DIKQSIYRFR QADPQIFNQK FKDYQSNPEH GKLILLKENF
     RSQSEVLNVT NAVFSRLMDE SLGEITYDDK HQLVAGSEAQ KQLHPENRAQ LLLYNTDQAQ
     EGTEEASTND GISAGEVTLV AKEIIRLYNE EKVAFEDITL LVSSRTRNDT IFQVFNQYGI
     PLVADGGQEN YLKSVEVMVM LDTLRSINNP LNDYALVALM RSPMFSFDED QLARISLQSS
     SQDQPQAFYD KLSNSLRGQG EHPGLIGQEL MTKLVDFDRT LSDWRQFAKL HSLYELIWKV
     FNDRFYFDFV ASQPKAEQAQ ANLYALAIRA DQFEQSGYKG LSRFIGMIDK VLETQNDLAD
     VEVERPKHAV NLMTIHKSKG LEFHYVFILN CDKRFAMADL QAPIILNRDE GIGIKYVANV
     KELLRDEKLA SLKVTMETLP YQLNKQQLRL ATLSEQMRLL YVAMTRAEKK VYLVGKASKE
     KIQAKTADNS SEGRLALASR ERLLSFQDWL LAITATFSKE DLFIDVRFVD DSDLTAEAVG
     QLRSSGLLQA DDLKDNRQTE DIARALDMLD KVSKLNASYQ AAIELPTVRT PSQLKTLYEP
     LMDTDGVDII DQPYHRPKSF DLPDFSKKKA VEPSQIGSSL HELMQRIPMS DQVTAGDIEQ
     ALQFVSADAE VKARIDIKKV TSFFATTELG QLLQEHHQCL HREAPFAMLK KDSLSQEQYV
     VRGIIDGYLL FEDRIVLFDY KTDHYQHSAE LKQRYQQQMD LYAEALSQSY GIARIEKYLV
     LMGGSQLEVV RLDE