ADDA_CLOPE
ID ADDA_CLOPE Reviewed; 1268 AA.
AC Q8XPE2;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 112.
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=CPE0021;
OS Clostridium perfringens (strain 13 / Type A).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=195102;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=13 / Type A;
RX PubMed=11792842; DOI=10.1073/pnas.022493799;
RA Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT eater.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002).
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; BA000016; BAB79727.1; -; Genomic_DNA.
DR RefSeq; WP_011009572.1; NC_003366.1.
DR AlphaFoldDB; Q8XPE2; -.
DR SMR; Q8XPE2; -.
DR STRING; 195102.gene:10489249; -.
DR EnsemblBacteria; BAB79727; BAB79727; BAB79727.
DR KEGG; cpe:CPE0021; -.
DR HOGENOM; CLU_001114_3_1_9; -.
DR OMA; KQSIYRW; -.
DR Proteomes; UP000000818; 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..1268
FT /note="ATP-dependent helicase/nuclease subunit A"
FT /id="PRO_0000379261"
FT DOMAIN 3..476
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT DOMAIN 528..824
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 1268 AA; 146904 MW; 4631AEE9E0D53234 CRC64;
MGTKWTEEQE LAINTRKCNL LVAAAAGSGK TAVLVERIIK MITEGENPVD IDKLLVVTFT
NAAASEMRER IGDAISKALE KDPSSKVLQR QLALLNRASI TTMHSFCLEV IKNNFHLIDL
DPGFRIGDQT ECELIKQDIL ADLFEDMYAK DDECFKDLVE AYGGSKSDDN LNSIILKFYN
FIMSGPWPEA WLKDKVEEFN INSIEELEGK KWIEVLKESI ILDLNNAYSM LTQARDIAEM
GGGLEPYLVN INPEIIQVEE LKIALSEGIV KFYNNLMGAS FGRLKSVRKA SVDDERALEK
TKSLRDESKK IIENLRDNVF ETSLEEAVLG MKKMYPLMKC LSGLVIEFSN RYRDKKREKD
ILDFNDLEHL CLEILIDKDE EGNIKPSQVA LEFKDRFEEV LVDEYQDSNT IQETIVGMVS
RRDIENPNVF MVGDVKQSIY KFRQANPELF LEKYINYREF EDSNRKIMLY KNFRSREEII
NGVNYIFKTL MSNTVGELEY DEKEALNLGA SYGELNEENV EKEYIDEIEN LKVAGDIELN
ILNKAGNKDY SDEDELGEEE EDLDSIQLEA RIIGKKINEL MNPEDGSHYM VFDKDLGKYR
KIKYKDIVIL LRATKNWAET FVDELGTYGI PVYADTGTGY FQTIEIRTIL ALLHIIDNPM
QDIYILSALR SPIFSFTSEE FADLRLLNKD KYFFEIIKEV VDGIYDESIS KDLKGKCKYF
LDYLNKWREK AAYMPIDEFI WFLYSDTSYY GYVGTMPNGV QRQANLRILF QRAKQYESTS
FKGLFNFINF INKLKKSSGD MGSAKILGEN ENVVRIMSIH KSKGLEFPVV ILGGTGKQFN
KMDLREDILL HETLGIGTNC IDIKKRIKYD TLQKHAIKKK CELEVLSEEM RILYVAFTRA
KEKLIITGAV SDLEKSCENW CKASASSEDN RINPGNVLKG KSYLDWIGMA LTKHKDGDAI
RNIGNGDITL NLDDKSNWSF KSWDRSELLE TNNNKKEKNN IDIFESNNWI ESKKDIKEVI
EIRDRLGFKY KYIESCNTPS NISVTELKRA HQEEEFMQES YNIIDNESNE ENKKEKIKRK
PRFMEERQEE FSAAKKGTIT HFVMQHIDLD KVTYIDEIRE EVLKMVKKEL LTEEEGKVVN
VFKIQKFFKS DLGQRMLSSY KSGKKVYREL PFITEIPSSI IEKNLDPKIY GEEKVRLQGI
IDAFFKEEDG YVLLDYKTDY VKEGEEENFI NKYKIQINLY KDTLNKILGE EVKEAYLYSF
YLEKELKI
