ADDA_LEUMM
ID ADDA_LEUMM Reviewed; 1230 AA.
AC Q03W49;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 103.
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=LEUM_1481;
OS Leuconostoc mesenteroides subsp. mesenteroides (strain ATCC 8293 / DSM
OS 20343 / BCRC 11652 / CCM 1803 / JCM 6124 / NCDO 523 / NBRC 100496 / NCIMB
OS 8023 / NCTC 12954 / NRRL B-1118 / 37Y).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Leuconostoc.
OX NCBI_TaxID=203120;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8293 / DSM 20343 / BCRC 11652 / CCM 1803 / JCM 6124 / NCDO 523
RC / NBRC 100496 / NCIMB 8023 / NCTC 12954 / NRRL B-1118 / 37Y;
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; CP000414; ABJ62573.1; -; Genomic_DNA.
DR RefSeq; WP_011680160.1; NC_008531.1.
DR AlphaFoldDB; Q03W49; -.
DR SMR; Q03W49; -.
DR STRING; 203120.LEUM_1481; -.
DR EnsemblBacteria; ABJ62573; ABJ62573; LEUM_1481.
DR KEGG; lme:LEUM_1481; -.
DR eggNOG; COG1074; Bacteria.
DR HOGENOM; CLU_001114_3_1_9; -.
DR OMA; KQSIYRW; -.
DR OrthoDB; 137860at2; -.
DR Proteomes; UP000000362; 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..1230
FT /note="ATP-dependent helicase/nuclease subunit A"
FT /id="PRO_0000379294"
FT DOMAIN 3..473
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT DOMAIN 500..782
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 1230 AA; 139091 MW; A993C10405434C9B CRC64;
MATKFTKNQQ RAIEEKGHNI LVAASAGSGK TTVLIERLIQ KILSGVSVEK FLIVTFTNAA
AKEMRERLEV AIEKRLKVAD ESQKRFLQEQ LLILPAANIS TIDAYALRII EMYYHIIGLD
PQFRLLSDTA ERKLLQQDVL TDVLADFYDE NNIHHEQFLT LVNNFGNPNQ DDQLQKIILK
LSDFAEARAD GNEWLEKLRE PYEVTGEPLT ATALYVRSIR PIILEIIKNL IKKVEEVQLT
ITGIDELKKT QDAFLEIQDY LLLIQDKAMV APWDELREAI LDTPSGKINS QTKAIKEDPD
LSATLEVARQ IKGQVVGVKS QMNSLITSYF ALDEKSWQLV QKESYKLIDT LILVTQAFRE
SFRRTKREEK LLDFPDLGTL ALAILSDDVT KQTIQGQFDE ILVDEYQDIN QLQETLLTSV
SNGHNMYMVG DVKQSIYGFR QAEPSLFTNK YKQFAKKESD DIRIDLADNF RSQNNVTNIT
NLIFTQIMDE TLGDIAYAGE AKLVPKAAYP DDVPAVFHMD IIVEDAEEDL ETDTEVFEKR
QAQYALLAER ILKLRETSIF DRKADPAGLR PVEYSDIAIL TRAKSGYIDL VSTLRAAGIP
VQVEGVGNYF QTMEVYLMLD ILRVIDNPHQ DIPLAAVLRS PVFNFDENEL AAIRIADKMH
DYWTALQAYA QQDQKAQNFL NLIEKWHAIA TQNDLVALIW AIYDDTAWLD YVAGMPGGAQ
RQANLHALYE YARTYQNNTH SGLFRFIRYI EQLQSGDSDL GEAAQETDAQ AVRIMTIHAS
KGLEFPIVFL PEFDKSFNTQ DLKGGLLIQK NEGIGVEYIQ PDALVMIPTL QKLVVQQALK
RQSWSEEMRL LYVALTRAEQ QLYIVGSVKV KGEAGNQSLK SLWQQSKNAN GQFLPEFLRL
QADSYLKWTI MSLARTKNKV LEDWLGDGQL PRLVGSETPL TGKVAVTLTN QNEIHAPIAS
TKGSELVEDG TYSPMDFDRA KTILNYQYAN LQATQTAAYQ SVSEIKQIFE DPDLAQMQTA
VITENGQLQP ANVLKVDELP LPDFMNDGSQ KPSSSAVGTA THLILQLIDF TKINTVQSIE
KLRDELVENK RILPSVAPLI EIDEILAFLQ SDFAKQIIAH QKTLHREATF AMIMPANDIY
DTLEDSAPVL IHGIIDGYFV DEASQTITLF DYKTDFVRNA QIDEDLTKLQ ARYKGQLHLY
QQALQREYVG YQVGDPQLIA LNVGRVISVK
