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ADDA_STRSY
ID   ADDA_STRSY              Reviewed;        1227 AA.
AC   A4VUD2;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 89.
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=SSU05_0755;
OS   Streptococcus suis (strain 05ZYH33).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=391295;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=05ZYH33;
RX   PubMed=17375201; DOI=10.1371/journal.pone.0000315;
RA   Chen C., Tang J., Dong W., Wang C., Feng Y., Wang J., Zheng F., Pan X.,
RA   Liu D., Li M., Song Y., Zhu X., Sun H., Feng T., Guo Z., Ju A., Ge J.,
RA   Dong Y., Sun W., Jiang Y., Wang J., Yan J., Yang H., Wang X., Gao G.F.,
RA   Yang R., Wang J., Yu J.;
RT   "A glimpse of streptococcal toxic shock syndrome from comparative genomics
RT   of S. suis 2 Chinese isolates.";
RL   PLoS ONE 2:E315-E315(2007).
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; CP000407; ABP89721.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4VUD2; -.
DR   SMR; A4VUD2; -.
DR   STRING; 391295.SSU05_0755; -.
DR   EnsemblBacteria; ABP89721; ABP89721; SSU05_0755.
DR   KEGG; ssu:SSU05_0755; -.
DR   eggNOG; COG1074; Bacteria.
DR   HOGENOM; CLU_001114_3_1_9; -.
DR   OMA; KQSIYRW; -.
DR   Proteomes; UP000000243; 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; 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; Reference proteome.
FT   CHAIN           1..1227
FT                   /note="ATP-dependent helicase/nuclease subunit A"
FT                   /id="PRO_0000379352"
FT   DOMAIN          37..503
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT   DOMAIN          532..816
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT   BINDING         58..65
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
SQ   SEQUENCE   1227 AA;  140943 MW;  C4CC5EB68E59F034 CRC64;
     MDGTNERRSG LMAFEQFLSA EEIKAVQLAE AHSDKQQKRT AEQIEAIYTH GQNVLVSASA
     GSGKTFVMVQ RILDKLKRGI GIDQLFISTF TVKAAGELKE RIEKKLNETI AETTDMELRR
     HLSAQLADLT KADIGTMDSF TQKLVTTYGY SLGISPQFRI LQDETEKASL KKEVFDQLFA
     DYLEEDENGA FRKLVRNFSG NRKDNSGFRQ VVYQVHDFSQ STSSPTKWLK EQAVQADLYS
     QERIEQMLEQ GFKEKVLDKL YQAADFFRYH VEWGRNDFGS AKYFANVEEV LDLLTGLDSL
     DQKDLMERVE RILLINNQSR GKGLTNANRP KDEHLIAFKE EYNAGKSQII SELRDLGQEV
     YELTLLKDYQ VQALPLLILL RDFVLDFSQA YLDVKIKEAA FEFGDIGHFA IRILEENADI
     RQFFQEKYHE VMVDEYQDNN HSQERMLDLL SNGHNRFMVG DIKQSIYRFR QADPMIFQEK
     FELYQANPQS GKLILLKENF RSQIEVLEAT NAIFTRLMDR QVGEIKYDDT HSLVAGSPGQ
     KIAQPKNEME YLIYDQQDSA NSSTDAEEET PLTAGEIEVV AKEIIRLHNE EGADFKDITL
     LVQKRTHNDL IMSIFEKHGI PIVADGGAAS YLQSLEVMIM LDTLRVINNP LNDYALVALL
     KSPMFRFDED ELTRISLQAG TGFFYQKMEI AQQASGQHPE LMSEKLKKKI TDFLSILENW
     RAYAKLHSIY DMIWKMFNEK FYYDYVGALP NGSKRQANLY ALGLRANQFE KTGYKGLSRF
     IAMIDRALAN DKDLADVQEF LPQNAVQLMT IHKSKGLEFK YVFLMNIDKR FNLEDHYQSV
     IISRKNGLGI QYLADMKDKV NSPLPQVRVL MNTLPYQNNL QELKIANLSE QMRLLYVALT
     RAEKKLYLVG KGNADKLAEK YDGKKENGVL AQSTRESMAT FQDWILAIDE AFSGEDLHFK
     KVFVTDEDLT EEKIGKLTLK SKLEDASLKD IRQSEDIAQA LDQLSSVQEL NERYKAAIEL
     PSLRTPSQIK KLYEPILEQE GMEVMEKYQP KRTFNLPDFS KKPKITGAQV GSAVHELMQR
     LDLSWLVTED TVRAALEAVH AEQAIKDKIN VQMILDFFDT DLGREILANT DKLHREAPFA
     SLQTDSVSQE NFVLRGIIDG YLLYDDHIVL FDYKTDKYDQ PIQLSQRYQA QMQLYAEALK
     KAYKIDRVDC HLILLGGERI EVVEVNI
 
 
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