ADDA_LISW6
ID ADDA_LISW6 Reviewed; 1235 AA.
AC A0AL18;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 94.
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=lwe2282;
OS Listeria welshimeri serovar 6b (strain ATCC 35897 / DSM 20650 / CIP 8149 /
OS NCTC 11857 / SLCC 5334 / V8).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=386043;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35897 / DSM 20650 / CIP 8149 / NCTC 11857 / SLCC 5334 / V8;
RX PubMed=16936040; DOI=10.1128/jb.00758-06;
RA Hain T., Steinweg C., Kuenne C.T., Billion A., Ghai R., Chatterjee S.S.,
RA Domann E., Kaerst U., Goesmann A., Bekel T., Bartels D., Kaiser O.,
RA Meyer F., Puehler A., Weisshaar B., Wehland J., Liang C., Dandekar T.,
RA Lampidis R., Kreft J., Goebel W., Chakraborty T.;
RT "Whole-genome sequence of Listeria welshimeri reveals common steps in
RT genome reduction with Listeria innocua as compared to Listeria
RT monocytogenes.";
RL J. Bacteriol. 188:7405-7415(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; AM263198; CAK21700.1; -; Genomic_DNA.
DR RefSeq; WP_011703031.1; NC_008555.1.
DR AlphaFoldDB; A0AL18; -.
DR SMR; A0AL18; -.
DR STRING; 386043.lwe2282; -.
DR EnsemblBacteria; CAK21700; CAK21700; lwe2282.
DR GeneID; 61190186; -.
DR KEGG; lwe:lwe2282; -.
DR eggNOG; COG1074; Bacteria.
DR HOGENOM; CLU_001114_3_1_9; -.
DR OMA; KQSIYRW; -.
DR OrthoDB; 137860at2; -.
DR Proteomes; UP000000779; 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..1235
FT /note="ATP-dependent helicase/nuclease subunit A"
FT /id="PRO_0000379299"
FT DOMAIN 12..482
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT DOMAIN 509..800
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT BINDING 33..40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
SQ SEQUENCE 1235 AA; 142654 MW; 376BBA73D4D3034A CRC64;
MGLNIPEKPV NTLWTDDQWK AIQANGNNIL VAAAAGSGKT AVLVTRIIEK LVDETGNLNV
DELLIVTFTN ASAAEMKYRI GKSLEEALSQ NPDSSHLKKQ VALLNYASIS TLHSFCLEII
RKHYFEADID PNFRLIEPIE SSMIRDEVLE ELLEKEYSIA NNEAFFHLVE SFTGDRTDAE
LHMLISKLYD FSRANPNPDL WLEQMVNFYD TKDINSITEL PYFPIIKEDI ELRINQAKSY
LLNAIEYASE NNGPAPYLET LENDLAQINT LSNISWTNWQ DVKLRVESMD FKRIPSLKNK
SDYDEEYVEE TKRFRDAAKK EIKNVLVDWF SREETNYLAD LEKMKPDIKT ISELVKNFAN
NFFEEKQRRG VLDFNDLEHL ALKILLKNDV PSDVAKSYQK QFKEVLIDEY QDTNMVQETI
LLLVTNSEES KGNLFMVGDV KQSIYRFRLA EPTLFMTKYQ EYQQNGEGEG IRIDLSQNFR
SRKEVLDATN FIFHQLMDKH VAEIDYDEAA ELTLGANFPK SNHMATELLL IDMKSNENES
EDELSPQELQ KNQVEARAIA TKIREMIDNK FPIYDKKLQQ NRSIQYRDIV ILSRAMTSAP
DMEEAMKVQD IPFYASNNSG YFETTEVATM IALLKVIDNP YQDIPLAAVL RSPIVGLNEE
ELGQIRMAKK KGYFFDALLA YKDITVSAAA DRISDFITQL NNWRELSIRE NLTALIWQIY
QETNFYEFVG GLPGGKQRQA NLRALYDRAN QYEKTAFRGL FRFVRFVERL EVRGDDLGTA
KTLGEKEDVV RMMTIHASKG LEFPVVIISG LSKKFNMRDI YSKTLLDKDY GFASNYRDIE
KMIVYPTIMQ QAIKQKKSRE MIAEEMRVLY VALTRAEEKL ILTATVPDFE KTSKNWLQVS
NQKETILPAS IRAKAKCYLD WIGNTIIRHT SFKDLLCEER IQTLPTEMKL QIEIKTKEMF
LTTELEEHKA DNWLENVKAH EPVPVQSAYK DEIERFMNYK YKDVAATEIR AKQSVTELKR
QFSLQDSWSD TSILKEFQKV SLDRPKFLQQ NKLSATEIGT AMHTLMQAVS LTYKPSEKDL
TSLLQSMQEK DILTEAQIKA INIKQIMGFF DSPLGETVLQ KSDQVKREVP FSYLLPVAKL
YKQSDLEEHV LIQGVVDSMI EEEDAITLID YKTDKIEGRY ANWEAAEKVM KERYQIQIKL
YAEAIQAITG KKVSNAYLYF FDGQHICQIN IEEGF
