ADDA_LACDA
ID ADDA_LACDA Reviewed; 1227 AA.
AC Q1GAA9;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 1.
DT 03-AUG-2022, entry version 99.
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=Ldb1001;
OS Lactobacillus delbrueckii subsp. bulgaricus (strain ATCC 11842 / DSM 20081
OS / BCRC 10696 / JCM 1002 / NBRC 13953 / NCIMB 11778 / NCTC 12712 / WDCM
OS 00102 / Lb 14).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=390333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11842 / DSM 20081 / BCRC 10696 / JCM 1002 / NBRC 13953 / NCIMB
RC 11778 / NCTC 12712 / WDCM 00102 / Lb 14;
RX PubMed=16754859; DOI=10.1073/pnas.0603024103;
RA van de Guchte M., Penaud S., Grimaldi C., Barbe V., Bryson K., Nicolas P.,
RA Robert C., Oztas S., Mangenot S., Couloux A., Loux V., Dervyn R., Bossy R.,
RA Bolotin A., Batto J.-M., Walunas T., Gibrat J.-F., Bessieres P.,
RA Weissenbach J., Ehrlich S.D., Maguin E.;
RT "The complete genome sequence of Lactobacillus bulgaricus reveals extensive
RT and ongoing reductive evolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:9274-9279(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; CR954253; CAI97803.1; -; Genomic_DNA.
DR RefSeq; WP_011543869.1; NZ_JQAV01000012.1.
DR AlphaFoldDB; Q1GAA9; -.
DR SMR; Q1GAA9; -.
DR STRING; 390333.Ldb1001; -.
DR PRIDE; Q1GAA9; -.
DR EnsemblBacteria; CAI97803; CAI97803; Ldb1001.
DR KEGG; ldb:Ldb1001; -.
DR PATRIC; fig|390333.13.peg.585; -.
DR eggNOG; COG1074; Bacteria.
DR HOGENOM; CLU_001114_3_1_9; -.
DR OMA; KQSIYRW; -.
DR BioCyc; LDEL390333:LDB_RS04380-MON; -.
DR Proteomes; UP000001259; 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; Reference proteome.
FT CHAIN 1..1227
FT /note="ATP-dependent helicase/nuclease subunit A"
FT /id="PRO_0000379279"
FT DOMAIN 3..477
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT DOMAIN 505..788
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 1227 AA; 138763 MW; ABD61E8DB8B2FDE2 CRC64;
MAVKYTPDQA RAIESRGQDL LVSASAGSGK TSVLVERVIR EIMDDHLEVN QLLVITFTRA
AASEMKQRIK QRLQDRLQEE TDASQADFLR RQLAEIDTAI ISTIDSFCLD VIRRFYFAID
IDPDFSILTD ATQIELLKER ALRDVENGYL QNEDQAKKDR FLALYDAFAG DSNANSARDL
LLDLYQFAMA RPNYRAWLQK LAAPYQLETS DVVDSALWQE KIKPYLEEEF SNLADKLTAL
MAEADFDHEK FAKYQPAFTA FATSLASYRE SLATDDPFDR QRELLAACQF DGTLRTNKEI
ADFVEEAKEV KEAGKQLVFN VYTGFYASSN ADQQALLAKG AEIASAAAEV ELAFIDRFNE
LKRADRVLDF SDMEQLAYEI LTQDSSNSDL ARAYYQSRFK EIMVDEYQDT NALQDGLIQR
LKKAGKNNLF MVGDVKQSIY GFRQAEPSLF IAKYDEYGQE NSAGKQRIIF AENFRSSQPV
TQAVNLIFDS LLTKDFGGID YQKEGQLKFA AGYDPEAALP TETEVLYQED SSATDDDGEL
NQGDLAMVIS RIQKLIADQT PIFDPKTGQT RPVSYGDIAI LTRSKTSNLD IKQEFDRYGV
PLFVMDVQNY FQTFELTVIM SYLKIIDNPD QDIPLVAVLR SPIFNFSSSD LAEIRLVNKS
VSFYAALRTY AKKDTDLAAR CRDFLAQLQD LRDFSLSHRI SELLWTIYER TSFLEIVTAM
TNGQQRRLNL TALYERASAY ESSGFKDLYQ FINFIARMRK NQKDLAQPIL SENAGNSVKL
MTIHASKGLE FPVVFVLGLE HRYNYQQDIT GSYVLDASGL GLSFAYPFDE AEYRADTLAN
VWLKIAKKQK LLEEEARLLY VALTRAKQKL ILAANIKLPA RTDLAGLEEK WAKEISAGRL
TLLDKMKVAK PLDFLAPALA RAKQVKRLGE KAVSDLATGQ EGSLVFVHFD PKKDQAQLPD
SEAVAASGAD LTEDEAAVFK QAEKLYTFSQ GGYPYLDASR TTAYQAVSEI KKVFGDPIED
ELADSHISEL QSANRYLQPI DTEPDFLFQN TVSSAELGTA SHLVLQYYDY AKGDKNAIDS
CIAGLVEKGR LSQTLASMLD REALSWFVKS DFAKDFYQQP DRLHREENFA TILSPKTLFK
DFSDFPGKIL VHGTIDGYYE AENGIILFDY KTDHVNPRKQ EEAIQKLKEK YQGQLRLYER
ALNESGRLPV LKKYLVLLSC REIVEVD
