ID ADDA_LACH4 Reviewed; 1204 AA.
AC A8YVK0;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 91.
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=5.6.2.4 {ECO:0000255|HAMAP-Rule:MF_01451};
DE AltName: Full=ATP-dependent helicase/nuclease AddA {ECO:0000255|HAMAP-Rule:MF_01451};
DE AltName: Full=DNA 3'-5' helicase AddA {ECO:0000255|HAMAP-Rule:MF_01451};
GN Name=addA {ECO:0000255|HAMAP-Rule:MF_01451}; OrderedLocusNames=lhv_1273;
OS Lactobacillus helveticus (strain DPC 4571).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=405566;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DPC 4571;
RX PubMed=17993529; DOI=10.1128/jb.01295-07;
RA Callanan M., Kaleta P., O'Callaghan J., O'Sullivan O., Jordan K.,
RA McAuliffe O., Sangrador-Vegas A., Slattery L., Fitzgerald G.F.,
RA Beresford T., Ross R.P.;
RT "Genome sequence of Lactobacillus helveticus: an organism distinguished by
RT selective gene loss and IS element expansion.";
RL J. Bacteriol. 190:727-735(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=Couples ATP hydrolysis with the unwinding of duplex DNA by
CC translocating in the 3'-5' direction.; EC=5.6.2.4;
CC Evidence={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=5.6.2.4;
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; CP000517; ABX27287.1; -; Genomic_DNA.
DR RefSeq; WP_012211953.1; NC_010080.1.
DR AlphaFoldDB; A8YVK0; -.
DR SMR; A8YVK0; -.
DR KEGG; lhe:lhv_1273; -.
DR eggNOG; COG1074; Bacteria.
DR HOGENOM; CLU_001114_3_1_9; -.
DR Proteomes; UP000000790; 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:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:UniProtKB-UniRule.
DR CDD; cd17932; DEXQc_UvrD; 1.
DR Gene3D; 3.90.320.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 4.
DR HAMAP; MF_01451; AddA; 1.
DR InterPro; IPR014152; AddA.
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 NCBIfam; TIGR02785; addA_Gpos; 1.
DR PANTHER; PTHR11070:SF48; ATP-DEPENDENT HELICASE_NUCLEASE SUBUNIT A; 1.
DR PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR Pfam; PF00580; UvrD-helicase; 1.
DR Pfam; PF13361; UvrD_C; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF52980; Restriction endonuclease-like; 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; Isomerase; Nuclease; Nucleotide-binding.
FT CHAIN 1..1204
FT /note="ATP-dependent helicase/nuclease subunit A"
FT /id="PRO_0000379283"
FT DOMAIN 2..472
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT DOMAIN 500..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 1204 AA; 139431 MW; 1C17EB96CC6335DB CRC64;
MPQFTKEQEK AINDRGHDIL VSASAGSGKT TVLVERVLKE ILAGTQVDEL LVVTFTKAAA
EEMKTRIKAA LTKEMAKPGV DYRYLREQLN QIDTANISTI DAFCLDVIHR FYYSIELDPS
FTILTDDTQA TLLKERALRE IEGEMLTSKD KAFRHFYDNF AGDRDADSPR DLLLDLYNFA
MAKPEYKKWL AQLPQIYEIE DSVIGSKIWQ KQIKPYIATK FSKLQEKIAS YLTQAIMETK
ELAKVKESFT LFAQNLNNFV QAVKEDDDYD KQRELLRSCV FTINFRKSKK WDEDLLEFYN
EIQSLKDEAK SQVFDTFTSF YAVTEKEQIK IMQESQKIVT AISTAEIKLI ERFNQLKRNE
NLLDYSDMEQ LAYQILSQDT SSSQMARDFY QNKFKEILID EYQDINALQE RIIQQIKSEK
KNTLFMVGDV KQSIYGFRQA EPSLFLQKYH QFAEDENEHE ERILLSDNFR STEPVTQTVN
AVFKSILSTD FGGIDYQKEG QLIFGAKYYP KSLPQASEVI VHEKKNNNEK SENEIDFSEI
QMVLARIKQL EDEHVQIFDS NTGKMRDMEY SDIAILTRSR SDNLEIMQEF AKQDIPLFVT
DAENYFQTFE LTVMMNYLKI IDNPDQDIPL VTVLRSPLFN FDEKELAKIR IKSKNSNFYS
ALTSYVGTND VLSKKCKNFL NQLAELRSFA TTHRISELIW SIYERTNLLE IMTALPNGEQ
RRVNLEALYE RATSYESAGF KGLYQFINFI DRMRRSQKDL AQPLLTKEAG NAVRLMTIHG
SKGLEFPIVF YVGMQHHYQM RDLNGNYIIN SDSMGITLRE QNYRVDSLVK AMGNITKKQQ
LLEEEARILY VALTRAKQKL ILVGDVPSFN KKVKEWSTEL NHAGQLPLIN KLSATSPLSF
IGPSLRFDRH VAIKLNDITK SIDQSQKILF IDYQDEDTKF IKKDEDTDNQ NENTRKSALL
TQTVNKLYQF NYPFRDASET TAYQAVSEIK KAFNDPIDAE LENSHLLTST NRYLQPIDTK
PNFLYQTKFT GAEIGTATHL ILQYYDYTND SADNLDQEIA TLIEQKKLNP DIVSSLNKDQ
IDWFVHGDFA KDFWKEPTNL KREVDFSSLL SARTLFKDFS DPDAKILVHG TIDGYFVAKN
GIILFDYKTD HVNKTNIDKS IELIKEKYTG QLRLYEQALN EFSEKKVIGK YLILLDAKQV
VEVK
//
