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Database: UniProt
Entry: Q043G6
LinkDB: Q043G6
Original site: Q043G6 
ID   ADDA_LACGA              Reviewed;        1204 AA.
AC   Q043G6;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   05-DEC-2018, entry version 83.
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=LGAS_1031;
OS   Lactobacillus gasseri (strain ATCC 33323 / DSM 20243 / JCM 1131 /
OS   NCIMB 11718 / AM63).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=324831;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33323 / DSM 20243 / JCM 1131 / NCIMB 11718 / AM63;
RX   PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA   Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B.,
RA   Koonin E.V., Pavlov A., Pavlova N., Karamychev V., Polouchine N.,
RA   Shakhova V., Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K.,
RA   Goodstein D.M., Hawkins T., Plengvidhya V., Welker D., Hughes J.,
RA   Goh Y., Benson A., Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B.,
RA   Smeianov V., Wechter W., Barabote R., Lorca G., Altermann E.,
RA   Barrangou R., Ganesan B., Xie Y., Rawsthorne H., Tamir D., Parker C.,
RA   Breidt F., Broadbent J.R., Hutkins R., O'Sullivan D., Steele J.,
RA   Unlu G., Saier M.H. Jr., Klaenhammer T., Richardson P., Kozyavkin S.,
RA   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
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:
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}.
DR   EMBL; CP000413; ABJ60406.1; -; Genomic_DNA.
DR   RefSeq; WP_003652957.1; NZ_BALQ01000002.1.
DR   ProteinModelPortal; Q043G6; -.
DR   SMR; Q043G6; -.
DR   PRIDE; Q043G6; -.
DR   EnsemblBacteria; ABJ60406; ABJ60406; LGAS_1031.
DR   GeneID; 29638792; -.
DR   KEGG; lga:LGAS_1031; -.
DR   eggNOG; ENOG4107R2I; Bacteria.
DR   eggNOG; COG1074; LUCA.
DR   HOGENOM; HOG000015621; -.
DR   KO; K16898; -.
DR   OMA; KQSIYRW; -.
DR   BioCyc; LGAS324831:G1G6Y-1031-MONOMER; -.
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; 1.
DR   PANTHER; PTHR11070:SF14; PTHR11070:SF14; 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;
KW   Helicase; Hydrolase; Nuclease; Nucleotide-binding.
FT   CHAIN         1   1204       ATP-dependent helicase/nuclease subunit
FT                                A.
FT                                /FTId=PRO_0000379282.
FT   DOMAIN        2    469       UvrD-like helicase ATP-binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_01451}.
FT   DOMAIN      497    784       UvrD-like helicase C-terminal.
FT                                {ECO:0000255|HAMAP-Rule:MF_01451}.
FT   NP_BIND      23     30       ATP. {ECO:0000255|HAMAP-Rule:MF_01451}.
SQ   SEQUENCE   1204 AA;  139135 MW;  414B921B5C2C4DA8 CRC64;
     MTNFTKEQDQ AINDAGKDIL VSASAGSGKT TVLVERVLKK ILSGTPVSSL LIITFTKAAA
     REMKERIKQK ISDQLEIEPD NQFLRSQLLD VDTANISTID SFCLDVIRRF YYVIDLDPQF
     SVLTDETQAE LLKERALREI EADYLEGDNQ DFQDFYDNFS GDRDAEGARN LLLQLYNTAT
     TEPNYEKFLD NLPTCYEVGD NLIRSNLWQQ QIKPLLLKEI SDLKAEVEAL LAEPEINSSD
     LVKVKENYDI FSNRLDSFWE SLNTDQPYNE IRANLMNCKF EKAVRKSKKW SDESIEVYQD
     SQDLKLDLND QLKKIFASFF VVEEKEQIAV LQKSEKIVKT IVAAEKKLIQ KFSQLKREQN
     LIDYSDMEQF AFSILTTDTS NAHIAQEYYQ EKFNEILIDE YQDVNALQEN IIKAIKKKGQ
     NTLFMVGDVK QSIYGFRQAR PDLFLSKYHT YGKDNDSEKI ILADNFRSTK RVTKTVNDLF
     NPILTTNFGG IDYKKEGQLQ FGASYYPSDL PTASEYIFTD KKQTQSAYED QYGDEMDFSE
     VQMVIARIKQ LKAENFQVWD RRTQLKRPLE YSDIAIITRT RSDNLQVMQE FAKADLPLFV
     TDAQNYFQTF ELIMIMNYLR LIDNPQQDIP LVAVMRSPLF NFKEPELAQI RVKTPAGNFY
     TALTSFASVN SSLGKKCKEF LQQLETLRSF AATHRISELI WSIYEKTHLL EIVTGLPNGQ
     QRRVNLESLY ERATSYESAG FKGLYQFISF IERMRKNQKD LAQPLLSDKA DNAVKLMTIH
     ASKGLEFPIV FVMGLGHQYQ TRDLSGNFTI SQNELGLTIK EKNYRIDSLV KSLADVQKRQ
     QMLEEEARIL YVGLTRAQQK LILVASVNEI ENKRKKWVSE LDQKKDIIPL VKKINAQSPL
     DFLGPKLEQK HEFDQTIRDM TSALEEQDKL YYLKFNLDLE PEKIKDQNED SQEVNSNVNK
     VVKELYNFKY PFEDATKTTA YQSVSEIKKA FNDPIDTELE NSRLISSSNR YLQPIDETPT
     FLEGQKFTGA EIGTAMHLVL QYYNYEGNKD QENLDQEIDQ LVELGKLNSL MVPHLSKEAL
     NWFVMSDFAK EFWKQPDKLH RESQFSSLVN ASELFNDFSD PSAKVLVHGT VDGYFEAKDG
     LILFDYKTDF VDKTNEEQAI EKIKQKYTGQ LRLYEQALNE MNNDKKVIGK YLILLDARKV
     VPVD
//
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