ADDA_NATTJ
ID ADDA_NATTJ Reviewed; 1282 AA.
AC B2A610;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 80.
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=Nther_1855;
OS Natranaerobius thermophilus (strain ATCC BAA-1301 / DSM 18059 /
OS JW/NM-WN-LF).
OC Bacteria; Firmicutes; Clostridia; Natranaerobiales; Natranaerobiaceae;
OC Natranaerobius.
OX NCBI_TaxID=457570;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1301 / DSM 18059 / JW/NM-WN-LF;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Lykidis A., Mesbah N.M., Wiegel J.;
RT "Complete sequence of chromosome of Natranaerobius thermophilus JW/NM-WN-
RT LF.";
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001034; ACB85427.1; -; Genomic_DNA.
DR RefSeq; WP_012448292.1; NC_010718.1.
DR AlphaFoldDB; B2A610; -.
DR SMR; B2A610; -.
DR STRING; 457570.Nther_1855; -.
DR PRIDE; B2A610; -.
DR EnsemblBacteria; ACB85427; ACB85427; Nther_1855.
DR KEGG; nth:Nther_1855; -.
DR eggNOG; COG1074; Bacteria.
DR HOGENOM; CLU_001114_3_1_9; -.
DR OMA; KQSIYRW; -.
DR OrthoDB; 137860at2; -.
DR Proteomes; UP000001683; 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; -; 3.
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..1282
FT /note="ATP-dependent helicase/nuclease subunit A"
FT /id="PRO_0000379302"
FT DOMAIN 10..481
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT DOMAIN 516..820
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT BINDING 31..38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
SQ SEQUENCE 1282 AA; 148738 MW; E55357F769681237 CRC64;
MVQENNNTQS KWTDSQRQVI DENYHHILVS AGAGAGKTAV LVQRIISKLI DPHDDLTVNG
LLVVTFTEKA ANEMRDRIAR ELKKALSQDP ENDHLKKQLY LLNKANISTL HSFCLEILRH
YFYYLDIDPA FSVASEYDVE LLRQSVIDNY LEEEYGLGEQ SFYLLVDSYG GDKNDEKLKK
MILTLHRFSR SHPRPRKWLQ SVKDHFEVST DDDLTNTVYY LEIQKDIETL FKQCINYFKR
ALQTSEQPGG PYQYAETLLE EIEQVQNFTQ QLVEVENHSF DWNSFAERVA GFKFSKLPSV
SKNDDVDEDL KKDCKKLRDH GKKTFQKLVQ NYFTRSKDEL LRDLQQLSPL MNKLIDMVIN
MDDKYEEVKK QRGIMDFSDL EHYVYELLDQ YPEIVSELHQ RYDEVMVDEY QDINQVQNAI
LEKLTGQQSI SPDLFMVGDV KQSIYRFRLA EPELFLNKYD TFDQRSEEGS LIELQENFRS
SPMVLESVNY LFSRIMTGSL SGIEYNEKVK LIPASKPREL YLNEDDNEDD KYEGQAENEN
QVIDGRTEVH LLENKDTNSR EEDTEREAQL IATTINSLVE EEYRIYDRDL DDYRKLDYSD
FVILSRKTKE QAELVTNVFQ EHGVPLYAEL DTGYFAAQEV QVMLSLLKII DNPRQDIPLA
GVLRSPLVGL DSNELVEIRR SNPGTDYYEA CKRVLTNSIE QQNQCSEKTI QKMQKFFSQL
ERWRRISRER SLAELIWDIY QITDYLDYVA GFPGGRERQA NLWSFYDRAL QFDSFSHSGL
VKFLNFIEKL VEQDFDLGKA RTVSENENVV RLMSIHKSKG LEFPVVFVMG LGNNFNFNDQ
KGDLLLHKDL GLGPKLVDLT NRIKYPTIAH QAIKGSLGRE TLAEEMRILY VAMTRAEEKL
FLVGSGKDIE SKISVPEEPA AAQNYLDWIY PQLGEDSELF HKIWNDIPGQ QDGKSVEYNW
KSYFESLLSQ TFTWEVDQEE FEDQKRTLEQ AISYSYPYNI ATEIVGKMSV TDLAKSDTYI
DSKIVSQNQS LSSVQDHYKK LAATQIPMFL ETTEDAGDNK YESYKEHHTP SKRPEFLKSN
SGLTGAEAGT SIHLAFQHLP INSDLNSQEF SEEQISNQLD DLVNKEIITQ AQRDVISEDL
IMKFFQSELG QAILERPKGL KRELPFTLGV PAWEMLAGSE ECQAELEAEN IETTELQGLS
DETVVIQGVI DYLFWDGTNY YLIDFKTDKL NTSNMDEIEK RLQGKYRMQI QMYLRAITEI
FNITPTKAYL YHVPTGNWIQ VE
