ADDA_STRGC
ID ADDA_STRGC Reviewed; 1216 AA.
AC A8AY33;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 94.
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=SGO_1413;
OS Streptococcus gordonii (strain Challis / ATCC 35105 / BCRC 15272 / CH1 /
OS DL1 / V288).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=467705;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Challis / ATCC 35105 / BCRC 15272 / CH1 / DL1 / V288;
RX PubMed=17720781; DOI=10.1128/jb.01023-07;
RA Vickerman M.M., Iobst S., Jesionowski A.M., Gill S.R.;
RT "Genome-wide transcriptional changes in Streptococcus gordonii in response
RT to competence signaling peptide.";
RL J. Bacteriol. 189:7799-7807(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; CP000725; ABV09291.1; -; Genomic_DNA.
DR RefSeq; WP_012130498.1; NC_009785.1.
DR AlphaFoldDB; A8AY33; -.
DR SMR; A8AY33; -.
DR STRING; 467705.SGO_1413; -.
DR PRIDE; A8AY33; -.
DR EnsemblBacteria; ABV09291; ABV09291; SGO_1413.
DR KEGG; sgo:SGO_1413; -.
DR eggNOG; COG1074; Bacteria.
DR HOGENOM; CLU_001114_3_1_9; -.
DR OMA; KQSIYRW; -.
DR Proteomes; UP000001131; 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; 1.10.10.160; -; 1.
DR Gene3D; 3.40.50.300; -; 4.
DR Gene3D; 3.90.320.10; -; 1.
DR HAMAP; MF_01451; AddA; 1.
DR InterPro; IPR013986; DExx_box_DNA_helicase_dom_sf.
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; Reference proteome.
FT CHAIN 1..1216
FT /note="ATP-dependent helicase/nuclease subunit A"
FT /id="PRO_0000379331"
FT DOMAIN 26..488
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT DOMAIN 514..801
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 1216 AA; 140370 MW; 3201CBC670F1478F CRC64;
MRKKSFLSPE EISQLQHFEA TSSKEQKRTA EQIEAIYSSG QNILVSASAG SGKTFVMVQR
IIDQILRGVS IQELFISTFT VKAAGELKER LEKELSKVLK ESQDEELKQH LAKQLAAIAT
ADIGTMDSFT QKLLNKYGYL LGLAPNFRIL QSASEQTMLQ NEVFQQLFEQ YYTGEQKEIF
EKLVKNFTGK KKNISGFRQQ VYAIYQFLQS TSNPQRWLQD FFLKGYEETD FSRERDKILQ
QVKGALFDLE DYFRFHLDNE GREFAGAKYQ ENVLLALDKL GSLQELSSEQ DYFRVLKDVV
LLSRASGGRA LTITTRKEEL KELADTFNQG RKERIEHLRG LESSIYQFEF LEKYQDDSLP
LLDLLRDFMS DFTQTYLERK KTENAFEFGD ISHFAIQILE DFPQVRSFYQ ERYHEVMVDE
YQDTNHTQER MLELLSNGYN RFMVGDIKQS IYRFRQADPQ IFNDKFRLYQ ADPSQGKLIV
LKENFRSHVE VLEATNDVFK RLMDEQVGEI NYDETHYLVA GNPTKASPDP KNRAEFLLYD
STVASEELSE ESISAGEVSL VIKEIIRLHE EEAVAFKDIT LLTASRTRND IILAEFAKHN
IPLVPDGGED NYLQSVEVMV MLDTLRTINN PLNDYALTAL LKSAMFDFGE DELARIALQK
SQEKSQENLY EKLENALTNQ GLHPDLILPD HKKKLELFQK TLLSWRTFAK THSLYDLIWK
IYQDRFYYEY VGALPNGAQR QANLYALSLR ANDYEKSSFK GLSRFISMID KILENQHDLA
SVPYAAPQDA VHLMTVHKSK GLEFKYVFLL NMDKAFNRQD TSSSIILSRK NGIGIKYIAD
VEVEYPEKVK PRSIRLSMDT LPYQQNLEEI KLASLSEQMR LLYVAMTRAE TKLYLVGKGS
QEKLEKRSWG QAEQGLLSAS IRSQTTSFQD WLYAIQTVFS EDQLAFDLRF VRDEDLTADK
IGQIHHSNPF DADDLTDNRQ SEDIGRALDI LESVDRLNSQ YRSAIELPSV RTPSQIKKFY
EPIMDTEGMD IIDERVAFRP QPNFDLPDFS RKAKVTGAQV GSAVHELMQR IPIDQKPDMA
VLKLSLKQVQ AEESVKKQID LNKIASFFET RLGEILLANS DKLHREAPFA MFKRDEISGQ
DFVLRGILDG YLLFEDRIIL FDYKTDKYKE ASELIARYHS QLDLYAQALS RSYGISQIEK
YLILLGGEQL QVVQVD
