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Database: UniProt
Entry: B2G532
LinkDB: B2G532
Original site: B2G532 
ID   ADDA_LACRJ              Reviewed;        1392 AA.
AC   B2G532;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 1.
DT   10-OCT-2018, entry version 62.
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};
GN   OrderedLocusNames=LAR_0048;
OS   Lactobacillus reuteri (strain JCM 1112).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=557433;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 1112;
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.,
RA   Yoshimura T., Itoh K., O'Sullivan D.J., McKay L.L., Ohno H.,
RA   Kikuchi J., Masaoka T., Hattori M.;
RT   "Comparative genome analysis of Lactobacillus reuteri and
RT   Lactobacillus fermentum reveal a genomic island for reuterin and
RT   cobalamin production.";
RL   DNA Res. 15:151-161(2008).
CC   -!- FUNCTION: The heterodimer acts as both an ATP-dependent DNA
CC       helicase and an ATP-dependent, dual-direction single-stranded
CC       exonuclease. Recognizes the chi site generating a DNA molecule
CC       suitable for the initiation of homologous recombination. The AddA
CC       nuclease domain is required for chi fragment generation; this
CC       subunit has the helicase and 3' -> 5' nuclease activities.
CC       {ECO:0000255|HAMAP-Rule:MF_01451}.
CC   -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
CC       {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}.
DR   EMBL; AP007281; BAG24564.1; -; Genomic_DNA.
DR   RefSeq; WP_003669565.1; NC_010609.1.
DR   ProteinModelPortal; B2G532; -.
DR   PRIDE; B2G532; -.
DR   EnsemblBacteria; BAG24564; BAG24564; LAR_0048.
DR   GeneID; 5190144; -.
DR   KEGG; lrf:LAR_0048; -.
DR   HOGENOM; HOG000015621; -.
DR   KO; K16898; -.
DR   OMA; KQSIYRW; -.
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:0004003; F:ATP-dependent 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; 3.90.320.10; -; 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; IPR011604; Exonuc_phg/RecB_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038726; PDDEXK_AddAB-type.
DR   InterPro; IPR011335; Restrct_endonuc-II-like.
DR   InterPro; IPR014016; UvrD-like_ATP-bd.
DR   InterPro; IPR034739; UvrD/AddA_N.
DR   PANTHER; PTHR11070; PTHR11070; 2.
DR   PANTHER; PTHR11070:SF14; PTHR11070:SF14; 2.
DR   Pfam; PF12705; PDDEXK_1; 1.
DR   Pfam; PF00580; UvrD-helicase; 2.
DR   Pfam; PF13361; UvrD_C; 1.
DR   SUPFAM; SSF52540; SSF52540; 4.
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;
KW   Helicase; Hydrolase; Nuclease; Nucleotide-binding.
FT   CHAIN         1   1392       ATP-dependent helicase/nuclease subunit
FT                                A.
FT                                /FTId=PRO_0000379287.
FT   DOMAIN        4    595       UvrD-like helicase ATP-binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_01451}.
FT   DOMAIN      623    929       UvrD-like helicase C-terminal.
FT                                {ECO:0000255|HAMAP-Rule:MF_01451}.
FT   NP_BIND      25     32       ATP. {ECO:0000255|HAMAP-Rule:MF_01451}.
SQ   SEQUENCE   1392 AA;  159710 MW;  FF9599F8233A0394 CRC64;
     MAGFKPTPAQ SKAINDRGEN ILVSASAGSG KTAVLVNRTI ELIKEGQSID RMLLVTFTDA
     AAKNMRDKIR AALQKIVQDS ANPKDLRDRM SNQINRLAAA DISTIHAFCL KLIKRYYYLI
     DLDPQFRLLT DETERLLLQE DVWHEVSEEL YRNAEEKVSG KASFSELVLN FSSDRDDQGL
     DDLILRLYEI ANAQPDPEKW LQKLPDNYDL GSGSLLESNF YQQQLKPLVI EKLNQFIQDY
     RELVTRASDN GLDQAAEVIK SDEELMHQLL SSLGGITVSD VCQMMAQQKF GSFRGRPAAD
     DPRIDVFKDI QKQRNQLKKQ WEQMVSTYLG KQEAQEPIAK EELLTELTTF SDQFTDLLSK
     ATESQLDAKT VDSLQKDQQM MQELLDLLQP PTWNTIRDLF ANAKFARMGG KPKDDELAEE
     VYKSLGSART GIKKQFDQLV DRFFNYREDQ FRLISTHAQE LLRELSAVTI NFRRRYQQTK
     LNRHVLEFSD LEHYAYAILT PPDDQPNWQT LVKDLQNHYQ EIMIDEYQDT NRLQESILMK
     LTSPERKNLF MVGDVKQSIY RFREADPTLF LGKYQNYRQG SDGEAIVLGE NFRSMTNVTS
     FTNILFEQLM DREVGEIDYD EDAHLKYAAT YYEENQDNKV HPTEVLLYDA NALDPEKEDV
     EHEDDKLAGE FRMIGMRIKQ MVENQELIFH PEDGQMHPIQ YGDIVLLERT KAINNSLMEE
     FNKLNIPLTV HDVESYFQAT EVRVMMSLLK IIDNPQQDIP LVAVLRSPIV GLTNQELAFI
     RLQNRSVDYY AALQTFMSNY QRKALRHQSL LTSEQVNALY EKADHFLGLL RVFRQTAQQQ
     TLVDLIWQIY DQTGYLDYVG AMPGGHQRQA NLHALYQRAH SYEQSSFKGL YQFIRFIEKM
     QEHDKDLGVA PTQLTANTVN VMTIHGSKGL QFPVVFLIDA THGFNKGAAR ENAVVDAVAG
     VGIRYMDDQR VIYDTPQRQA VIEEIQRGER AEDLRVLYVA LTRAEQRLVI TGSFNEEMRT
     QSLAGSWQRW QKAYQSKNLL IGPQPRITAN SFMDWVGLAL ARYPEFNAQQ LSRGNVTLEE
     STLADTKVTG LAADPHFTAK TYTALDVSDG LAKIGQNASA NVTEKNNTVA TDASEQKIEQ
     ILRYRYPHLV ATKTTAYQSV TDVKRVFEDP DTRDMARWDY DQQQKVKTQG IYLNNNFDVP
     AFIQQTTHEP VATEIGTATH LVFQKLPLDE GLINVEFVDQ EIQKLVGEKL INPVVAARIN
     REGIVAFYQT AVGQKILKHP ADYHREVPFS MIMNGHELFK GVNVSDDERI LIHGIIDGYL
     RTDEGIILVD YKNDHLNKDY RDFDLARIKD RYRGQLELYK EALNLMEGIP VVQMGLYLLE
     LGEFVLFTKE GD
//
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