ID   ADDA_LEVBA              Reviewed;        1262 AA.
AC   Q03NA7;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 102.
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=LVIS_2267;
OS   Levilactobacillus brevis (strain ATCC 367 / BCRC 12310 / CIP 105137 / JCM
OS   1170 / LMG 11437 / NCIMB 947 / NCTC 947) (Lactobacillus brevis).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Levilactobacillus.
OX   NCBI_TaxID=387344;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 367 / BCRC 12310 / CIP 105137 / JCM 1170 / LMG 11437 / NCIMB
RC   947 / NCTC 947;
RX   PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA   Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V.,
RA   Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA   Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA   Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA   Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA   Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA   Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J.R., Hutkins R.,
RA   O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T.,
RA   Richardson P., Kozyavkin S., Weimer B.C., Mills D.A.;
RT   "Comparative genomics of the lactic acid bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(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; CP000416; ABJ65315.1; -; Genomic_DNA.
DR   RefSeq; WP_011668835.1; NC_008497.1.
DR   AlphaFoldDB; Q03NA7; -.
DR   SMR; Q03NA7; -.
DR   STRING; 387344.LVIS_2267; -.
DR   EnsemblBacteria; ABJ65315; ABJ65315; LVIS_2267.
DR   KEGG; lbr:LVIS_2267; -.
DR   PATRIC; fig|387344.15.peg.2171; -.
DR   eggNOG; COG1074; Bacteria.
DR   HOGENOM; CLU_001114_3_1_9; -.
DR   OMA; KQSIYRW; -.
DR   OrthoDB; 137860at2; -.
DR   Proteomes; UP000001652; 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..1262
FT                   /note="ATP-dependent helicase/nuclease subunit A"
FT                   /id="PRO_0000379276"
FT   DOMAIN          5..476
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT   DOMAIN          515..808
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   1262 AA;  141233 MW;  FCA4D5213BEF9F8F CRC64;
     MSTKFSFTPS QDQAIHQTGN NLLVSASAGS GKTRVLVQRV IERLKTGVGI DQILIVTFTK
     AAAAEMRERI QTALRQELAV SQGDSAQQQF YLRQLNQLPV ADISTLDAFC LRLLQRYYYV
     IDLDPVFRLL ADETENGLLR DEVWADLRED LYANDDSGLF ARLTENFSGD RNDQGLADLV
     QQTYTFANAT PNPTAWLAEL PQPYQLDSDQ LMTTSFYQQR LRPFFQSQLQ QLQADLTSAQ
     ALANQAGLDK QAAHVTAVLE NVAAVQQLVT GDSWNALRAA IQDFAWGRMP AVRKTNEDYP
     IYNELKTTYY DPARKQLDSL KKTYLIQDEQ QAMTTIRRSG ELVGELSRVV TAFRTAYRQE
     KQRRHVLDFA DVEHAALAIL TQDSDQSRQV AAQLRHQFAE IMVDEYQDTN GLQEAILTAI
     AEPAPQGNLF MVGDVKQSIY RFRQADPTLF MTKTDQYAAD AAAGELIVLA ENFRSMKNVD
     DFTNLIFKQL MDRELGEIDY TGAAQLKFGA SYYPDTVTST AELLVYLTED APESAGDADS
     EAMDATFQVD NKHQGEVLMV GQKIQQLIAD QTPIYDREAK QVRPMTYGDI TLLTPTRTNN
     LIITDELRRL GIPVVVNDAR NYFKTTEIQI MMALLQIIDN PYQDIPLAAV LRSPIVGLNE
     NELALLRINQ RTGDYYQAVL HFQRSFVPNQ ASDFQQAVYQ KVSHFLEQLQ EFRDIAQQDE
     LVTLIWRIYQ ETGFLDYVGG MPAGEQRQAN LHALYERAKS YEQSSFKGLF QFVRFVERLQ
     ERDDDLAGAP VQAADDAVSV MTIHGSKGLE FPVVFIMDAS RQFNKQDQQG NYVMSGKTGI
     GIDYLDPDSR VKAPSLQKLV TAQAISRASL AEEMRKLYVA LTRAESRVYI VGSHKTQEAA
     ISAWEQAYQS PNLVLNATLR EKNTLANYLD WIGMCLVRDP KFAAELRQGT TTFSGLAGDP
     ATFAVHFVTA HDLGPTQGVN ETAVDWLQAA SETAAKVTTP PVDTEQLHQI MDFRYPHQAA
     TATTAYQSVS EAKRLFEDPD NATIGEYQAS ATGQVGGHRF VTHDFARPDF LQTVREPLAT
     EIGSATHLVL QQLDVTVTPT LDRVQGVIDQ LVADQVLTAE VAQRIQPELI LRFFSSSVGQ
     QVLAAPDQLH REVPFSLLMP ARSLFQDFQE TDSQVLVHGI IDGYLTTPAG VILFDYKTDH
     VNAQNQAASI EKIVERYGGQ VNLYAAALKQ MTGQPIVGQY LYLLAIGELV AVPEQQVRRL
     SE