ID   ADDA_LATSS              Reviewed;         890 AA.
AC   Q38X69;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=ATP-dependent helicase/nuclease subunit A;
DE            EC=3.1.-.-;
DE            EC=3.6.4.12;
DE   AltName: Full=ATP-dependent helicase/nuclease AddA;
GN   Name=addA; Synonyms=rexAN; OrderedLocusNames=LCA_0910;
OS   Latilactobacillus sakei subsp. sakei (strain 23K) (Lactobacillus sakei
OS   subsp. sakei).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Latilactobacillus.
OX   NCBI_TaxID=314315;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=23K;
RX   PubMed=16273110; DOI=10.1038/nbt1160;
RA   Chaillou S., Champomier-Verges M.-C., Cornet M., Crutz-Le Coq A.-M.,
RA   Dudez A.-M., Martin V., Beaufils S., Darbon-Rongere E., Bossy R., Loux V.,
RA   Zagorec M.;
RT   "The complete genome sequence of the meat-borne lactic acid bacterium
RT   Lactobacillus sakei 23K.";
RL   Nat. Biotechnol. 23:1527-1533(2005).
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 (By similarity). {ECO:0000250}.
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- SUBUNIT: Heterodimer of AddA and AddB/RexB. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the helicase family. AddA subfamily.
CC       {ECO:0000305}.
CC   -!- CAUTION: The C-terminus of this sequence has an annotated frameshift;
CC       it can be made to better match orthologs upon shifting at position 874.
CC       {ECO:0000305}.
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DR   EMBL; CR936503; CAI55212.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q38X69; -.
DR   SMR; Q38X69; -.
DR   STRING; 314315.LCA_0910; -.
DR   EnsemblBacteria; CAI55212; CAI55212; LCA_0910.
DR   KEGG; lsa:LCA_0910; -.
DR   eggNOG; COG1074; Bacteria.
DR   HOGENOM; CLU_001114_3_1_9; -.
DR   OMA; QSFIVQA; -.
DR   Proteomes; UP000002707; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0006302; P:double-strand break repair; IEA:InterPro.
DR   Gene3D; 3.40.50.300; -; 4.
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; IPR014016; UvrD-like_ATP-bd.
DR   PANTHER; PTHR11070; PTHR11070; 1.
DR   PANTHER; PTHR11070:SF48; PTHR11070:SF48; 1.
DR   Pfam; PF00580; UvrD-helicase; 1.
DR   Pfam; PF13361; UvrD_C; 1.
DR   SUPFAM; SSF52540; SSF52540; 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..890
FT                   /note="ATP-dependent helicase/nuclease subunit A"
FT                   /id="PRO_0000379288"
FT   DOMAIN          7..482
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00560"
FT   DOMAIN          510..804
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00617"
FT   BINDING         28..35
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00560"
SQ   SEQUENCE   890 AA;  102008 MW;  7096BAAB2452F82E CRC64;
     MAILSNPQFT PSQQAAVDHD GHDILVSASA GSGKTSVLVA RVIQKILKGT DVDTLLVVTF
     TEAAATEMRQ RIQAALRDAS EKATEPAVKQ RLRQQLSLVP TAQISTLHAF CLKVIKQFYY
     VIDRDPVFRL LSDTAERLLL ADQVWQRVRE AFYNHEYVKE NEQDTLFYEL AQNFSNDRND
     DGLTDIVFEL LDFANANSNP VKWLNKLPKS YAVDEAGLTA SDYFQEKILP ILQQTITECL
     EALQEAEQLS KTSENLMIYA PQIATTQAAL TQINADAKTL NWQAWRQQLT DAQLGPAKRT
     KKLEPDEQIN KDRLKADLDD VKKKIQTLLD TYFVFDEATT ANIQRQAGQL VQKLVSVTLT
     FREAFQAEKE RRHLLDFSDL EQLCLTILSV EDSPARAFYQ QKFSEVLVDE YQDTNPLQET
     IIQKVTSDHP RNLFMVGDVK QSIYAFRLAD PSLFKNKYNE FGVTEAERDS ERIILAENFR
     SRRNIDDFTN LIFKQLMDEN LGELDYDENA ALQYGARYYP DQHPTAPTEL LLYETKPEEA
     VANPQLDKSE GQVVAVAKRI QAMMTNGEQI WDKKLEKMRP IEYRDIVLLA PTRGNNLFIL
     DYFKRFGLPV VIKDAQNYFQ TTEVQIMLAL LQVIDNPNQD IPLVSVLRSP IVGLNENELA
     LIRINDKTDD YYQAVFNFID QYNEQKVGHL GQQVMQKLTH FMALLTSFRT IARQQPIVDL
     IWTIYQETGF LDYVGGMPAG RQRQANLHAL YERATAYEEN GFKGLFQFIQ FIERLQKQDK
     DLAQPTSLEN QDAISVMTIH GSKGLEFPVV FLIDTSRRFN QQDLQRSYVL DNHGGLGVVY
     LDSQKRLKVP TLPELAITAQ KRKKLRAEEM LKTIRCFDTC GTMVNHRWPL