ADDA_CLOK5
ID ADDA_CLOK5 Reviewed; 1235 AA.
AC A5N628;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 93.
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=CKL_0706;
OS Clostridium kluyveri (strain ATCC 8527 / DSM 555 / NCIMB 10680).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=431943;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8527 / DSM 555 / NCIMB 10680;
RX PubMed=18218779; DOI=10.1073/pnas.0711093105;
RA Seedorf H., Fricke W.F., Veith B., Brueggemann H., Liesegang H.,
RA Strittmatter A., Miethke M., Buckel W., Hinderberger J., Li F.,
RA Hagemeier C., Thauer R.K., Gottschalk G.;
RT "The genome of Clostridium kluyveri, a strict anaerobe with unique
RT metabolic features.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:2128-2133(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=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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000673; EDK32759.1; -; Genomic_DNA.
DR RefSeq; WP_011989274.1; NC_009706.1.
DR AlphaFoldDB; A5N628; -.
DR SMR; A5N628; -.
DR STRING; 431943.CKL_0706; -.
DR EnsemblBacteria; EDK32759; EDK32759; CKL_0706.
DR KEGG; ckl:CKL_0706; -.
DR eggNOG; COG1074; Bacteria.
DR HOGENOM; CLU_001114_3_1_9; -.
DR OMA; KQSIYRW; -.
DR OrthoDB; 137860at2; -.
DR Proteomes; UP000002411; 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..1235
FT /note="ATP-dependent helicase/nuclease subunit A"
FT /id="PRO_0000379258"
FT DOMAIN 3..471
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT DOMAIN 509..808
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 1235 AA; 144485 MW; 53D572FBA27C126B CRC64;
MNTKWTETQK SAIFTPNCNL LVAAGAGTGK TAVLVERILQ KVINDSEEVD IDKLLVVTFT
NAAASEMKER VGEALSKLLE LNCTSKNLQR QLALLNQSNI MTIHSFCLKV IKNNFHRIDL
DPNFRICDDT ESKLLKQDAL LELFEEKYEE ENLGFLNLAD GYGGKNDSKL QDIVLSLYEF
SQGSPWPKRW LQDVLKDFNL GSDFDFGDTK WAKVLMHNVT VELKGCKNKM KNILNTIENI
EGLEHYLEPF KSDIESIDKL INITTWDEIR DEFIKLSFNK LPSKRTDPLV KSYKDKARNT
RDEVKKKLIS IREDIILCTD DIYENFKEVY PLMKSLTFLV MDFYEKYHNK KSERNMIDFN
DIEHFCLEIL TSKDKNGDII PSEAALEYRE YFEEIFIDEY QDSNEVQEVI MNMISRKNIY
ANLFMVGDVK QSIYRFRQAR PELFLEKYNS YDEKEGSKNR KIKLSENFRS RKEIIDAINY
IFKQIMCREV GELDYGEEEC LKSSARYEPF EGNCGGDVEL HVVDKKENEN KLEDENEEEL
LDAISVEARL VASKINELVN PSLDQYSFKV YDKEIDNYRS IMYKDIVILM RATQNWAPAF
VEELNNSGIP VFADTSVGYF QAIEIKTIIS LLQIIDNPLQ DIPFIALLRS PIGGFSPEDL
IDLRVVNREI SFYEILKAIK EHSLELKYSL EHIDERLEYK VEQFFNKLCL WRRKVIHMPI
DEFIWHIYIE TGYYGFVGAM PGGIQRQANL RMLFERAKQY KNISYKGLFN FINFINKLKS
SSTDMGNAKI LGENENVVRI MSIHKSKGLE FPVIILSGAG KRFNLTDINK SVLFHKELGL
GPEYVNSERH ISYPTIVKQV LKRKLKMETL SEEMRILYVA FTRAKEKLII TGTVDNIENT
FQRWCEAAYC EEDKLPEYSL INSRNFLDWI GPAVARHPCG EIIRKVCPFE YNLNLITGDD
SKWKVFVYSK DNFKSTLDEN IDEDIIGKIK SLELDNNKEI YKNEVYRRLN WTYKYEQSSK
IAAKFSVSEL KRRFKLIDTE NGIEFMEPIY LKKPAFLRES KGLTPSERGI VMHLVMQHID
IDKVGSYEQI KEQVDKLVFR EFITEAEAKS ISVYKIIKFF NSEIGIRMKK SNNVYREVPF
YMEIESTELY KQLPQHIYRD EKVLIQGIID CYFEENNELI LVDYKTDHVG DIDSIKEKYQ
VQIYYYGRAL EKLTGKKVKK KYLYLFSKDY ILDLS
