ADDA_LACLM
ID ADDA_LACLM Reviewed; 1203 AA.
AC A2RH77; O54378;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, 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}; Synonyms=rexA;
GN OrderedLocusNames=llmg_0004;
OS Lactococcus lactis subsp. cremoris (strain MG1363).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus; Lactococcus cremoris subsp. cremoris.
OX NCBI_TaxID=416870;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, FUNCTION IN E.COLI, OPERON
RP STRUCTURE, AND DISRUPTION PHENOTYPE.
RX PubMed=9435243; DOI=10.1073/pnas.95.2.626;
RA El-Karoui M., Ehrlich S.D., Gruss A.;
RT "Identification of the lactococcal exonuclease/recombinase and its
RT modulation by the putative Chi sequence.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:626-631(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MG1363;
RX PubMed=17307855; DOI=10.1128/jb.01768-06;
RA Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C.,
RA Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P.,
RA van Sinderen D., Kok J.;
RT "The complete genome sequence of the lactic acid bacterial paradigm
RT Lactococcus lactis subsp. cremoris MG1363.";
RL J. Bacteriol. 189:3256-3270(2007).
RN [3]
RP RECOGNITION OF CHI SEQUENCES.
RX PubMed=10886371; DOI=10.1046/j.1365-2443.2000.00342.x;
RA El Karoui M., Schaeffer M., Biaudet V., Bolotin A., Sorokin A., Gruss A.;
RT "Orientation specificity of the Lactococcus lactis Chi site.";
RL Genes Cells 5:453-461(2000).
RN [4]
RP EXONUCLEASE ACTIVITY, AND MUTAGENESIS OF 1144-ASP--LYS-1146.
RX PubMed=11395472; DOI=10.1128/jb.183.13.4071-4078.2001;
RA Quiberoni A., Biswas I., El Karoui M., Rezaiki L., Tailliez P., Gruss A.;
RT "In vivo evidence for two active nuclease motifs in the double-strand break
RT repair enzyme RexAB of Lactococcus lactis.";
RL J. Bacteriol. 183:4071-4078(2001).
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 L.lactis chi site (5'-GCGCGTG-3'), which stimulates
CC homologous recombination. The AddA nuclease domain is required for chi
CC fragment generation; this subunit has 3'->5' exonuclease activity and
CC probably also performs the helicase function.
CC {ECO:0000269|PubMed:9435243}.
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 RexB. {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene have an increased
CC sensitivity to UV and about 300-fold reduced chromosomal conjugational
CC transfer. {ECO:0000269|PubMed:9435243}.
CC -!- MISCELLANEOUS: This enzyme is a functional homolog of the E.coli RecBCD
CC enzyme; unlike the RecBCD enzyme it degrades both duplex strands
CC symmetrically.
CC -!- SIMILARITY: Belongs to the helicase family. AddA subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01451}.
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DR EMBL; U76424; AAC12966.1; -; Genomic_DNA.
DR EMBL; AM406671; CAL96613.1; -; Genomic_DNA.
DR PIR; T30308; T30308.
DR RefSeq; WP_011834123.1; NZ_WJVF01000016.1.
DR AlphaFoldDB; A2RH77; -.
DR SMR; A2RH77; -.
DR STRING; 416870.llmg_0004; -.
DR PRIDE; A2RH77; -.
DR EnsemblBacteria; CAL96613; CAL96613; llmg_0004.
DR KEGG; llm:llmg_0004; -.
DR eggNOG; COG1074; Bacteria.
DR HOGENOM; CLU_001114_3_1_9; -.
DR OMA; KQSIYRW; -.
DR PhylomeDB; A2RH77; -.
DR BioCyc; LLAC416870:LLMG_RS00020-MON; -.
DR Proteomes; UP000000364; 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; 1.10.10.160; -; 1.
DR Gene3D; 3.40.50.300; -; 4.
DR Gene3D; 3.90.320.10; -; 1.
DR HAMAP; MF_01451; AddA; 1.
DR InterPro; IPR013986; DExx_box_DNA_helicase_dom_sf.
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 1: Evidence at protein level;
KW ATP-binding; DNA damage; DNA repair; DNA-binding; Exonuclease; Helicase;
KW Hydrolase; Nuclease; Nucleotide-binding.
FT CHAIN 1..1203
FT /note="ATP-dependent helicase/nuclease subunit A"
FT /id="PRO_0000379290"
FT DOMAIN 4..472
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT DOMAIN 503..785
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT BINDING 25..32
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT MUTAGEN 1144..1146
FT /note="Missing: Increase in UV sensitivity and loss of
FT nuclease activity; complete loss of RexAB activities."
FT /evidence="ECO:0000269|PubMed:11395472"
FT CONFLICT 238..267
FT /note="Missing (in Ref. 1; AAC12966)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1203 AA; 138945 MW; 123F0F0EACA92413 CRC64;
MSEVKLTPEQ NEAIHSSGKN ILVSASAGSG KTFVMAQRIV EKVKQGIEID RLFISTFTKK
AASELRMRLE RDLKKARQES SDDEEAHRLT LALQNLSNAD IGTMDSFTQK LTKANFNRVN
IDPNFRILAD QTESDLIRQE VFEQLVESYL SADESLNISK DKFEKLIKNF SKDRNILGFQ
KVVYTIYRFA SATENPISWL ENQFLKGFET YKSLTDLSED FTVNVKENLL TFFELLENSL
TNGVIAKKGA GRDKANLILD NKNELLEAIS KKDFVTCTAL FLSIDTDIRV GSSKDEALSA
LKKDFSAQKQ DLVGSKSKPG ELRKFVDKIK HGQLIEKYQN QAFEIASDLQ KFIIDFYKTY
LERKKNENAF EYSDIAHFAI EILEENPDIR ENLREHYDEI MIDEYQDTSH TQERMLELLS
NGHNLFMVGD IKQSIYGFRL ADPGLFLEKY KSYDQAENPN QLIRLKENFR SRGEVLNFTN
DIFKHLMDEK LGEMTYGKEE ALVQGNISDY PVEAEKDFYP ELLLYKENTS EEEIEDSEVK
ISDGEIKGAA QEIKKLIEYG VEPKDIAILV RSKSNNNKIE DILLSYDIPV VLDEGRVDFL
KSMEVLIMLD VLRAIDNPLY DLSLVAMLRS PLFGFNEDEL TRISVQGSRD LRFWDKILLS
LKKEGKNPEL INLSLEQKLK AFNQKFTEWR KLVNKIPIHR LLWKIYTETY YFDYVGALKN
GEMRQANLQA LSVRAESYES SGYKGLFKFV RLINKFMEQN NDLASVNIKL PQNAVRVMTF
HKSKGLEFDY VFLMNLQSRF NDRDLKEDVI LSREHGLGMK YIADLKAEPD VITDFPYALV
KMETFPYMVN KDLKQRAALS EEMRVLYVAF TRAKKKLYLV GKIKDTDKKA GLELYDAATL
EGKILSDKFR NSSRGFQHWI LALQNATKLP MKLNVYTKDE LETEKLEFTS QPDFKKLVEE
SEKFDNIMSF SDEIKEAQKI MNYQYPHQAA TELSSIQTPS QVKKRSYEKQ LQVGEVQPVS
EFVRVKNLDF SDFGPKKITA AEMGSATHSF MQYADFSQAD LFSFQATLDE MGFDEKIKNQ
IDITKILTLF DTEFGQFLSE NVDKTVKEAP FSMLRTDEFA KEQYIVRGIC DGFVKLADKI
ILFDYKTDRF TNVSAISEIK ERYKDQMNLY SEALQKAYHV NQIDKYLILL GGPRKVFVEK
IDD
