ADDA_STRPG
ID ADDA_STRPG Reviewed; 1210 AA.
AC A2RFA8;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 97.
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=SpyM51212;
OS Streptococcus pyogenes serotype M5 (strain Manfredo).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=160491;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Manfredo;
RX PubMed=17012393; DOI=10.1128/jb.01227-06;
RA Holden M.T.G., Scott A., Cherevach I., Chillingworth T., Churcher C.,
RA Cronin A., Dowd L., Feltwell T., Hamlin N., Holroyd S., Jagels K.,
RA Moule S., Mungall K., Quail M.A., Price C., Rabbinowitsch E., Sharp S.,
RA Skelton J., Whitehead S., Barrell B.G., Kehoe M., Parkhill J.;
RT "Complete genome of acute rheumatic fever-associated serotype M5
RT Streptococcus pyogenes strain Manfredo.";
RL J. Bacteriol. 189:1473-1477(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; AM295007; CAM30537.1; -; Genomic_DNA.
DR AlphaFoldDB; A2RFA8; -.
DR SMR; A2RFA8; -.
DR KEGG; spf:SpyM51212; -.
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; 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..1210
FT /note="ATP-dependent helicase/nuclease subunit A"
FT /id="PRO_0000379349"
FT DOMAIN 27..483
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT DOMAIN 512..798
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 1210 AA; 138999 MW; B6D87466A09E4D68 CRC64;
MISFAPFLSP EAIKHLQENE RYSDQSQKRT AQQIEAIYTS GQNILVSASA GSGKTFVMVE
RILDKILRGV SIDRLFISTF TVKAATELRE RIENKLYSQI AQTTDFQMKV YLTEQLQSLC
QADIGTMDAF AQKVVSRYGY SIGISSQFRI MQDKAEQDVL KQEVFSKLFS EFMNQKEAPV
FRALVKNFSG NCKDTSAFRE LVYTCYSFSQ STENPKIWLQ ENFLSAAKTY QRLEDIPDHD
IELLLLAMQD TANQLRDVTD MEDYGQLTKA GSRSAKYTKH LTIIEKLSDW VRDFKCLYGK
AGLDRLIRDV TDLIPSGNDV TVSKVKYPVF KTLHQKLKQF RHLETILMYQ KDCFPLLEQL
QDFVLVFSEA YLAVKIQESA FEFSDIAHFA IKILEENTDI RQSYQQHYHE VMVDEYQDNN
HMQERLLTLL SNGHNRFMVG DIKQSIYRFR QADPQIFNQK FRDYQKKPEQ GKVILLKENF
RSQSEVLNVS NAVFSHLMDE SVGDVSYDEQ HQLIAGSHAQ TVPYLDRRAQ LLLYNSDKDD
GNAPSDSEGI SFSEVTIVAK EIIKLHNDKG VPFEDITLLV SSRTRNDIIS HTFNQYGIPI
VTDGGQQNYL KSVEVMVMLD TLRTINNPRN DYALVALLRS PMFAFDEDDL ARIALQKDNE
LDKDCLYDKI QRAVIGRGAH PELIHDTLLG KLNVFLKTLK SWRRYAKLGS LYDLIWKIFN
DRFYFDFVAS QAKAEQAQAN LYALALRANQ FEKSGYKGLY RFIKMIDKVL ETQNDLADVE
VAAPKQAVNL MTIHKSKGLQ FPYVFILNCD KRFSMTDIHK SFILNRQHGI GIKYLADIKG
LLGETTLNSV KVSMETLPYQ LNKQELRLAT LSEQMRLLYV AMTRAEKKVY FIGKASKSKS
QDITDPKKLG KLLPLALREQ LLTFQDWLLA IADIFSTEDL YFDVRFIEDS DLTQESVGRL
QTPQLLNPDD LKDNRQSETI ARALDMLEAV SQLNANYEAA IHLPTVRTPS QLKATYEPLL
EPIGVDIIEK SSRSLSDFTL PHFSKKAKVE ASHIGSALHQ LMQVLPLSKP INQQTLLDAL
RGIDSNEEVK TALDLKKIES FFCDTSLGQF FQTYQKHLYR EAPFAILKLD PISQEEYVLR
GIIDAYFLFD DHIVLVDYKT DKYKQPIELK KRYQQQLELY AEALTQTYKL PVTKRYLVLM
GGGKPEIVEV
