ID   ADDA_LIMF3              Reviewed;        1337 AA.
AC   B2GEY4;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   03-AUG-2022, entry version 84.
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=LAF_0037;
OS   Limosilactobacillus fermentum (strain NBRC 3956 / LMG 18251) (Lactobacillus
OS   fermentum).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Limosilactobacillus.
OX   NCBI_TaxID=334390;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 3956 / LMG 18251;
RX   PubMed=18487258; DOI=10.1093/dnares/dsn009;
RA   Morita H., Toh H., Fukuda S., Horikawa H., Oshima K., Suzuki T.,
RA   Murakami M., Hisamatsu S., Kato Y., Takizawa T., Fukuoka H., Yoshimura T.,
RA   Itoh K., O'Sullivan D.J., McKay L.L., Ohno H., Kikuchi J., Masaoka T.,
RA   Hattori M.;
RT   "Comparative genome analysis of Lactobacillus reuteri and Lactobacillus
RT   fermentum reveal a genomic island for reuterin and cobalamin production.";
RL   DNA Res. 15:151-161(2008).
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; AP008937; BAG26373.1; -; Genomic_DNA.
DR   RefSeq; WP_012390674.1; NC_010610.1.
DR   AlphaFoldDB; B2GEY4; -.
DR   SMR; B2GEY4; -.
DR   EnsemblBacteria; BAG26373; BAG26373; LAF_0037.
DR   GeneID; 61200775; -.
DR   KEGG; lfe:LAF_0037; -.
DR   PATRIC; fig|334390.5.peg.36; -.
DR   eggNOG; COG1074; Bacteria.
DR   HOGENOM; CLU_001114_3_1_9; -.
DR   OMA; KQSIYRW; -.
DR   OrthoDB; 137860at2; -.
DR   Proteomes; UP000001697; 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.
FT   CHAIN           1..1337
FT                   /note="ATP-dependent helicase/nuclease subunit A"
FT                   /id="PRO_0000379281"
FT   DOMAIN          3..484
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT   DOMAIN          522..867
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT   BINDING         24..31
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
SQ   SEQUENCE   1337 AA;  149911 MW;  CC8EB6227AC66139 CRC64;
     MVFTPSKEQE PAINDRQKDI LVSASAGSGK TAVLVERVIQ LMETGLSKDA KPSERPNIDD
     ILMVTFTTDA AKNMRDRIRR RLVGATDEHM KAQVARLALA NISTIHSFCE QLIKRYYYVI
     DLDPQFRLID DAEQQLLKEQ AWQATLDDWV ANPDQVGALH QLIDNFGAGN LESVVQALDT
     EADAQPHPSD WLAGLSGLYQ FEEGADPRQS AFFKRLLEPL VGPQLKELRD QWAALGEVGP
     ARFAEQVEED LAKLATTVDD QGHLLGSWDS LAQTLNKKNF APKLRKRKDD DDPELLDELG
     VQRGGLRDQL GDLHDTYFFQ SAADLVKYGQ KAGALIEILT RVATDFRCHY QIIKQDRRLL
     DFSDLEHYAY AILTGENINP KVTWSDEEAR AKRQAAAQVQ AELQRHYKEI MIDEYQDTNR
     LQDDLLRLLH KSGQNHRFMV GDMKQSIYRF RQADPTLFKD YYDQFSADGQ SSEALDLSDN
     YRSRHEVTDL VNLIFEQLMD QQLGEMVYDD KASLKPKADW GADRDQASPA TPELLLFDGG
     VKKTTANPTG EDAIVVRQPE DKVASEVWLI GQRIRELLAK ETILDPETKR VRPITPGDIA
     ILSRAKRIHS VIAEQFAKLN LPVMVHGVEN YFKATEIRVV MSLLKVIDNP YQDVPLAAVL
     RSPLIQVAPE VAAKFGLSQG ENRIGFTEPE LAYLKVNSTS KDFFGVVQQN YYAWRDQEVE
     AVENHDALTE EELAERVAGD PAGLATKEEL GVNCGLIYLK LARFFELRDH LRRVAQRRPL
     VDLIWTIYQA TGYLDYVGGM SGGPQRQANL HALYERASGY EESGFKGLYQ FIHFIEQMQK
     KNDDLGEATT ALAGDAINVM TIHKSKGLQF PIVFLVETTH QFQADRDPVT IEPQAGLGFT
     YVDSTANETM RVKHPLVQQA ALKEKKKRQD RAEEMRLLYV ALTRAEQRLF ITGYVKDADL
     TKKMDKWNRA FDSASPLLTT TTRLKGQSML DWIMMTLVRT ANFPTLREGV EAAATPLRGL
     TKAAYQIKLQ NADQVQAALN TPLDLHPNAT AEQATPAAAT SRQFKADLER VLNFTYPDQV
     ATQTTAFQAV STVREAFARQ DPTNLEMGRL EIDRDQIKEA GAYLAPEERA FENPAFITGA
     SDQEPTGTAI GTATHLVFQK LPLTEPLDEG AVRALIKSLT ESGLIDNPQV AAGIDVAGVV
     SFYQTGLGQV ITAHPEQVHR EVPFSMLLSA HDLFSGIGAT DDSEVLIHGI IDGYVQHDDQ
     IDLFDYKTDR ISQAHPEEDL QELADKYSGQ LVLYADALTK MTGVPLEKIH RHLYFTRAKR
     VVTLSAPPSS HEPKEEA