ADDA_STRS2
ID ADDA_STRS2 Reviewed; 1227 AA.
AC A4W0M7;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 87.
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=SSU98_0758;
OS Streptococcus suis (strain 98HAH33).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=391296;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=98HAH33;
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; CP000408; ABP91916.1; -; Genomic_DNA.
DR AlphaFoldDB; A4W0M7; -.
DR SMR; A4W0M7; -.
DR KEGG; ssv:SSU98_0758; -.
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..1227
FT /note="ATP-dependent helicase/nuclease subunit A"
FT /id="PRO_0000379353"
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
