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Database: UniProt
Entry: ADDA_LACPL
LinkDB: ADDA_LACPL
Original site: ADDA_LACPL 
ID   ADDA_LACPL              Reviewed;        1249 AA.
AC   Q88U41; F9URH6;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 113.
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=5.6.2.4 {ECO:0000255|HAMAP-Rule:MF_01451};
DE   AltName: Full=ATP-dependent helicase/nuclease AddA {ECO:0000255|HAMAP-Rule:MF_01451};
DE   AltName: Full=DNA 3'-5' helicase AddA {ECO:0000255|HAMAP-Rule:MF_01451};
GN   Name=addA {ECO:0000255|HAMAP-Rule:MF_01451}; Synonyms=rexA;
GN   OrderedLocusNames=lp_2693;
OS   Lactiplantibacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)
OS   (Lactobacillus plantarum).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactiplantibacillus.
OX   NCBI_TaxID=220668;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX   PubMed=12566566; DOI=10.1073/pnas.0337704100;
RA   Kleerebezem M., Boekhorst J., van Kranenburg R., Molenaar D., Kuipers O.P.,
RA   Leer R., Tarchini R., Peters S.A., Sandbrink H.M., Fiers M.W.E.J.,
RA   Stiekema W., Klein Lankhorst R.M., Bron P.A., Hoffer S.M.,
RA   Nierop Groot M.N., Kerkhoven R., De Vries M., Ursing B., De Vos W.M.,
RA   Siezen R.J.;
RT   "Complete genome sequence of Lactobacillus plantarum WCFS1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:1990-1995(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX   PubMed=22156394; DOI=10.1128/jb.06275-11;
RA   Siezen R.J., Francke C., Renckens B., Boekhorst J., Wels M.,
RA   Kleerebezem M., van Hijum S.A.;
RT   "Complete resequencing and reannotation of the Lactobacillus plantarum
RT   WCFS1 genome.";
RL   J. Bacteriol. 194:195-196(2012).
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=Couples ATP hydrolysis with the unwinding of duplex DNA by
CC         translocating in the 3'-5' direction.; EC=5.6.2.4;
CC         Evidence={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=5.6.2.4;
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; AL935263; CCC79815.1; -; Genomic_DNA.
DR   RefSeq; WP_011101882.1; NC_004567.2.
DR   RefSeq; YP_004890329.1; NC_004567.2.
DR   AlphaFoldDB; Q88U41; -.
DR   SMR; Q88U41; -.
DR   STRING; 220668.lp_2693; -.
DR   EnsemblBacteria; CCC79815; CCC79815; lp_2693.
DR   KEGG; lpl:lp_2693; -.
DR   PATRIC; fig|220668.9.peg.2254; -.
DR   eggNOG; COG1074; Bacteria.
DR   HOGENOM; CLU_001114_3_1_9; -.
DR   OrthoDB; 9810135at2; -.
DR   PhylomeDB; Q88U41; -.
DR   Proteomes; UP000000432; 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:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:UniProtKB-UniRule.
DR   CDD; cd17932; DEXQc_UvrD; 1.
DR   Gene3D; 3.90.320.10; -; 1.
DR   Gene3D; 6.10.250.2380; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 4.
DR   HAMAP; MF_01451; AddA; 1.
DR   InterPro; IPR014152; AddA.
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   NCBIfam; TIGR02785; addA_Gpos; 1.
DR   PANTHER; PTHR11070:SF48; ATP-DEPENDENT HELICASE_NUCLEASE SUBUNIT A; 1.
DR   PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR   Pfam; PF12705; PDDEXK_1; 1.
DR   Pfam; PF00580; UvrD-helicase; 1.
DR   Pfam; PF13361; UvrD_C; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF52980; Restriction endonuclease-like; 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; Isomerase; Nuclease; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..1249
FT                   /note="ATP-dependent helicase/nuclease subunit A"
FT                   /id="PRO_0000379285"
FT   DOMAIN          5..482
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT   DOMAIN          521..811
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   1249 AA;  141029 MW;  0C270367B7E0ECF3 CRC64;
     MSEGTNYTPS QQAVIAQQGN NLLVSASAGS GKTTVLIERI MRKILAGTNI DQLLVVTFTN
     LAAKHMKQKL ESQINKRISQ LMTDNPAQTT ASPAIRQLRQ QLNLLGVANI STLDAFCLRV
     IQRYYYVIDL DPVFRLLTDN TEGLLIRDQV WDSVREQLYD EDGTLFDLLT ANFSNDRSDD
     GLSRLIFRLF DFAQSTPDPE GWLSKLPEPY QVDEEALTAS AFYQQQLLPL LINEVDGMQM
     KLRQAQKVAT DADLVPKTLE VLATAQKTLT TLREQLATAS WNELRTQVAT FKIGALKKTY
     KDEPEKTARA KTMGTFVDGV KKQMTTLSET YFAADEQQVL DIMVGAKSIV TELVDATKQF
     KTAFAAEKRR RHVLDFSDLE HLTLQILTSD NESSQAALAQ LRAQFEEVMV DEYQDINSLQ
     ESILQLLARD QPGNMFMVGD VKQSIYQFRL ADPLLFLHKY HDFGTNPEHG ERIVLAENFR
     SVANVDHLTN LIFSQLMDAP VGQIDYDEAA YLKYGPKDYP ADMPQTTNLL LYQTETDKST
     EDVSTDETNF SIDDPAVGSI TMVAQKILAL KAQDKPIYER ANGEYRPFRY SDVALLVPTR
     NHNLTIIDVF KRYHIPVVVN DAQNYFQTTE IRIMMALLSI IDNPYQDIPL VAVLRSPIVG
     LDENQLVYLR IQNKTSDYFQ AVQDFYHHYP TGPATEYGDQ VYAKIETFLT QLTEFRDLAR
     RNQIVTLIWQ IYERTGFLDY VGGMPAGKQR QANLHALYER AYTYEQGSFK GLFQFVRFIR
     RMQEKDQDLA AAVAETDAEA VNVMTIHGSK GLEYPVIFVM DMDKQFNQTD TRSSALLDRE
     AGIGITYLDP ETRVKYPTLP QVVTKQVVSK KMRAEEMRKL YVAMTRAQQQ LYLVGTIKDI
     DTATEKWRQA FASDGRVLSA QARIAATNQL DWVGMAVMRH PAMKAYWGDE WPNYELTDDP
     TKLAVELGDA TTVLAEQSEA VTDTQPDALE LVEQQVTIDV DQVTRDYLTT LLNFHYPHQA
     STTTTAYQSV SEVKRIFEDP DTPLMNANPT VSQRRSRPTS RFVTGSLELP QFLQTTQAPT
     SAEVGSATHL VLEQLDLTKP VNETTVQSTI DGLVANRVLT TNVAKLIAVD TIVAFYQSAL
     GSQILDNPAK VHREVPFSLL IPARQIFDVD EHETGKVLIH GIIDGYLETA DGLTLFDYKT
     DHVKRPEDLK TRYAGQVKLY AAALASMYPG KVTKQYLYSL PQQVFVPVN
//
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