ADDA_LIGS1
ID ADDA_LIGS1 Reviewed; 1248 AA.
AC Q1WRS0;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, 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=LSL_1607;
OS Ligilactobacillus salivarius (strain UCC118) (Lactobacillus salivarius).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Ligilactobacillus.
OX NCBI_TaxID=362948;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCC118;
RX PubMed=16617113; DOI=10.1073/pnas.0511060103;
RA Claesson M.J., Li Y., Leahy S., Canchaya C., van Pijkeren J.P.,
RA Cerdeno-Tarraga A.M., Parkhill J., Flynn S., O'Sullivan G.C., Collins J.K.,
RA Higgins D., Shanahan F., Fitzgerald G.F., van Sinderen D., O'Toole P.W.;
RT "Multireplicon genome architecture of Lactobacillus salivarius.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:6718-6723(2006).
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; CP000233; ABE00409.1; -; Genomic_DNA.
DR RefSeq; WP_011476466.1; NC_007929.1.
DR RefSeq; YP_536492.1; NC_007929.1.
DR AlphaFoldDB; Q1WRS0; -.
DR SMR; Q1WRS0; -.
DR STRING; 362948.LSL_1607; -.
DR PRIDE; Q1WRS0; -.
DR EnsemblBacteria; ABE00409; ABE00409; LSL_1607.
DR KEGG; lsl:LSL_1607; -.
DR PATRIC; fig|362948.14.peg.1702; -.
DR HOGENOM; CLU_001114_3_1_9; -.
DR OMA; KQSIYRW; -.
DR Proteomes; UP000006559; 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..1248
FT /note="ATP-dependent helicase/nuclease subunit A"
FT /id="PRO_0000379289"
FT DOMAIN 5..475
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT DOMAIN 508..804
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT BINDING 26..33
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
SQ SEQUENCE 1248 AA; 143487 MW; D9C1CA04AA93595D CRC64;
MANGFKFTPA QQKAIEDTGK NILVAASAGS GKTRVLVERV INKIKQGVSI DELLVVTFTE
AAAKEMKERI QIALRKELST ADSEEEKRRY LTQLSKLNVA NISTLHAFCL QIIKQYYYVI
NLDPMFRMLT EDTEVALLQE NVWDDLREKW YSKKSPEFEN LVVNFSSDRN DDGLSELVMK
TYQFANANPN PDEWLNNLVS EYDLGDQPLM ESNFYQNKIK PNVLDQIQLA KDNLKQGMDE
ANKLGLEKLY QTFEQDCATI DELQDFVVGC KEWNNLKTTL QNFKFKRAKS DRGLDDDQKK
QKERINKTLR DGSKKIIEDL SVKYFALPED EIKELTQKSK QIVETLSEVV KEFGAEFSKE
KRRRHVLDFS DLEHLTLQIL NTDTPDGRRV KERLKNKFKE IMVDEYQDTN QLQETILTTI
AHKNPGNMFM VGDVKQSIYG FRLADPGLFL KKYQSFATDD NDDERIILAE NFRSMENVTA
FTNLIFSQLM DEKVGEMAYD EDARLVYGAK YYPEETPIKA EVLVYESEDS SQESDDEPVN
EDFSIDNKAQ GQIVMTAKRI KELVENGEKI YDKKQGTIRP IEYRDIAILA PTRKNNLILT
EEFKRLGVPI FVPDAQNYFQ TTELKIMMSF LQIIDNPYQD IPLVAVLRSP IVGLKENELA
YLRINDKTGD YFQAVESFYD NFEVEKASAF AQSLYEKIAI FLKQLTEFRN MAQQNELASL
IWKIYEETGF LDYVGGMPGG LQRQANLHAL YERAAEYEEM SFKGLFQFVR FINKMQTKNK
DLSEATTQVS DDAVTVMTIH GSKGLEFPVV FLLDATHKFN VGDLNKPYLL NADDGIGISY
LDPDTRVKTD TLMKVIAGKQ ALKKLAAEQM RLLYVALTRA EQQLFIVGSY KDKNEALSKW
KKATQSESLV LNAGIRASVR NFMDWIGMCL TRSEIFKEVD DTVDAKEPEY IGELPVKFEV
KFYSNQDLRG ENITLDENSE SWLKQQLKKI EEQEPLEIND KQYRIIDKIL QSKYPNESLA
KTTAYQAVSD LKRAFDDPDN NMMQSLEIDW QDQVPQGINR YVQNELSLPK FMTTKVKVSP
AQVGIATHLL LQKLPLDDEV TLEELMQLLA QLVEDKLITS EVAKEINLNQ IKVFYTSDLG
RKVLKNKDKV KRELPFAMII PAGRLFSNVD NDVEQPILVH GIIDGLIELD DEVIIFDYKT
DHHTSEDKLI ENYRGQLNLY AMAVESMLNK KVSQKIIYSL DLGKSIVL
