ADDA_LACAC
ID ADDA_LACAC Reviewed; 1207 AA.
AC Q5FJX0;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 97.
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=LBA1165;
OS Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=272621;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700396 / NCK56 / N2 / NCFM;
RX PubMed=15671160; DOI=10.1073/pnas.0409188102;
RA Altermann E., Russell W.M., Azcarate-Peril M.A., Barrangou R., Buck B.L.,
RA McAuliffe O., Souther N., Dobson A., Duong T., Callanan M., Lick S.,
RA Hamrick A., Cano R., Klaenhammer T.R.;
RT "Complete genome sequence of the probiotic lactic acid bacterium
RT Lactobacillus acidophilus NCFM.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:3906-3912(2005).
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; CP000033; AAV43004.1; -; Genomic_DNA.
DR RefSeq; WP_011254366.1; NC_006814.3.
DR RefSeq; YP_194035.1; NC_006814.3.
DR AlphaFoldDB; Q5FJX0; -.
DR SMR; Q5FJX0; -.
DR STRING; 272621.LBA1165; -.
DR PRIDE; Q5FJX0; -.
DR EnsemblBacteria; AAV43004; AAV43004; LBA1165.
DR GeneID; 56942766; -.
DR KEGG; lac:LBA1165; -.
DR PATRIC; fig|272621.13.peg.1107; -.
DR eggNOG; COG1074; Bacteria.
DR HOGENOM; CLU_001114_3_1_9; -.
DR OMA; KQSIYRW; -.
DR BioCyc; LACI272621:G1G49-1155-MON; -.
DR Proteomes; UP000006381; 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; 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; 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..1207
FT /note="ATP-dependent helicase/nuclease subunit A"
FT /id="PRO_0000379275"
FT DOMAIN 2..472
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT DOMAIN 492..783
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT BINDING 23..30
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
SQ SEQUENCE 1207 AA; 139235 MW; 2A8CC8DC555D2D6A CRC64;
MPQFTKEQQQ AIDDRGHDIL VSASAGSGKT TVLVERVLKE IISGTQVSEL LVVTFTKAAA
EEMKTRIKTA LTKELAKPGV NRKYLREQLN QVDTANISTI DAFCLEVIRR FYYSVNLNPS
FKILTDETQA ALIKERALRE IEAESLTDEN SGIRYFYDNF AGDRDANSPR DLLLDLYNFA
MAKPEYRSWL KNLAKIYEVN NNIVKSKLWQ NQIKSYLLNT FVSLQKKIEE YLNNPTIETK
ELAKVKEDFS LFTQNLDKFI DAIKNDEDYD QQRNLLRLCK FEVKYRKSAK WDEDIQEFYA
ETQKLKSEAK SQIFDIFTAF YATDEKEQTR IMQESQKIVS AISKAELALI DRFNELKRNE
NFLDYSDMEQ LAYQILSADT SNSQMAREFY QNKFKEILID EYQDINALQE RIIQQVKNTD
KNTLFMVGDV KQSIYGFRQA EPSLFLKKYH GFASEENKHE KRILLSDNFR STEPVTKTVN
QLFKSILSSD FGGIDYSKEG QLIFGAKYYP DALPKASEII VHKKQKDIDN DNNGIDFSEV
EMVLARIKQL KKEHFQVLDS TTGEVRALKY SDIAILTRSH GDNLEIMQEF AKRDIPLFIT
DAENYFQTFE LTVIMNYLKI IDNPDQDIPL VTVLRSPLFN FSEKDLAKIR INSKNSGFYS
AVASYVGIGD ELSDRCKNFL NKLDELRKFA TTHRISELIW SIYAQTNLLE IMTGLPNGEQ
RRINLEALYE RASSYESAGF KGLYQFINFI NRMRRSQKDL AQPLLSKEAG NAVRLMTIHG
SKGLEFPVVF YLGMQHQYQL RDLKGNYVIN PDSLGITLRQ EHYRVDSLVK AIGNVTKKRQ
LLEEEARVLY VALTRAKQKL ILVGDIANLD KKVQDWSIEL DQSGQLSLAD KLSVTNPLGF
MGPALAFDKH IVINMNDISN ALDQSQSVLY VEYKDSDNFE FKKDEDKVVG DSKNNNYTMD
KLISTTKKLY QFDYPFKDAS ETTAYQAVSE IKKAFNDPIE TELENSRLLS STNRYLQPID
TKPNFLYQTK FTGAEIGTAT HLILQYYDYT GDGSEKQLDY EIEELIKQKK LNPDIVPSLH
KDQIQWFVHS SFAKSFWKNP ENLQREVDFS SLISAKNLFK DFSDANAKIL VHGTIDGYFV
SNDGIILFDY KTDHVNKSYL DKSINLIKEK YTGQLRLYEQ AINEFGEEKV IGKYLILLDA
KQVVEVK
