ADDA_CLOBH
ID ADDA_CLOBH Reviewed; 1279 AA.
AC A5HYY0; A7G0X7;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-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};
GN OrderedLocusNames=CBO0436, CLC_0511;
OS Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=441771;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hall / ATCC 3502 / NCTC 13319 / Type A;
RX PubMed=17519437; DOI=10.1101/gr.6282807;
RA Sebaihia M., Peck M.W., Minton N.P., Thomson N.R., Holden M.T.G.,
RA Mitchell W.J., Carter A.T., Bentley S.D., Mason D.R., Crossman L.,
RA Paul C.J., Ivens A., Wells-Bennik M.H.J., Davis I.J., Cerdeno-Tarraga A.M.,
RA Churcher C., Quail M.A., Chillingworth T., Feltwell T., Fraser A.,
RA Goodhead I., Hance Z., Jagels K., Larke N., Maddison M., Moule S.,
RA Mungall K., Norbertczak H., Rabbinowitsch E., Sanders M., Simmonds M.,
RA White B., Whithead S., Parkhill J.;
RT "Genome sequence of a proteolytic (Group I) Clostridium botulinum strain
RT Hall A and comparative analysis of the clostridial genomes.";
RL Genome Res. 17:1082-1092(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hall / ATCC 3502 / NCTC 13319 / Type A;
RX PubMed=18060065; DOI=10.1371/journal.pone.0001271;
RA Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C.,
RA Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.;
RT "Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4
RT and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within
RT plasmids.";
RL PLoS ONE 2:E1271-E1271(2007).
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; AM412317; CAL81989.1; -; Genomic_DNA.
DR EMBL; CP000727; ABS36619.1; -; Genomic_DNA.
DR RefSeq; YP_001252980.1; NC_009495.1.
DR RefSeq; YP_001386396.1; NC_009698.1.
DR AlphaFoldDB; A5HYY0; -.
DR SMR; A5HYY0; -.
DR KEGG; cbh:CLC_0511; -.
DR KEGG; cbo:CBO0436; -.
DR PATRIC; fig|413999.7.peg.440; -.
DR HOGENOM; CLU_001114_3_1_9; -.
DR OMA; KQSIYRW; -.
DR PRO; PR:A5HYY0; -.
DR Proteomes; UP000001986; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0033202; C:DNA helicase complex; IBA:GO_Central.
DR GO; GO:0043138; F:3'-5' DNA helicase activity; IBA:GO_Central.
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: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 GO; GO:0000725; P:recombinational repair; IBA:GO_Central.
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..1279
FT /note="ATP-dependent helicase/nuclease subunit A"
FT /id="PRO_0000379252"
FT DOMAIN 4..499
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT DOMAIN 526..853
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 CONFLICT 1156
FT /note="N -> S (in Ref. 2; ABS36619)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1279 AA; 150163 MW; DC20F0868CF3BCB0 CRC64;
MSGTKWTDEQ RQAIFTKDCN LLVAAGAGAG KTAVLVQRII EKILDKGEPI DIDKLLVVTF
TNAAAAEMRE RIGDAISKGL DEDPESKVLR KQLTLLNKSN IMTIHSFCLQ VIKNNFHTME
IDPNFRICDE TEGILMKQEA IDELFDELYE IENEDFINLV ESYASRKDTR LQEVVLELHR
FAKSAPFSYD WLLNMAEEFN VGEEFNFEET PWADMIMEDM KVLLHGFKNM LQQSIDVILN
SEGIDYYYEP FKMDLSFINS LLEKSSFKEF RGEIIAYDFP KLPLKRNKDA DKEAKERVKK
LRDKVKKKIV ELKNILDSYE NEFIKKEFIF LYPSMKALSN LVILFDKKYE AKKRERDLID
FNDIEHLCLS ILTDKNSEGH IIPSDIALDY RKKFAEVLID EYQDSNLVQE VIMSMVSRVK
GYWSFYNGQL MFNEEEINLE EPQICLDIPN RFMVGDVKQS IYRFRQAKPE IFLDKYNEYS
EEEGTKNRKV KLFKNFRSRK EVINGVNYLF KQIMSKTIGE LDYTEEEALK VGASYGEEVK
GEPIELCLMD KKYEISEEVL KEYNVDEEEA LDNIQLEGRL VAKKIQKLVG NNLEGGLKVF
DKKLGEYRNL QYRDIVILMR ATSNWAPIFV EELAKEGIPV FADTNSGYFD TAEIKTMISL
LQIIDNPLQD IPLLSVLRSP IASFTDDELI DIRMVNKNIT FYECMEIIYR LYKNEKLDSY
YSFYIEDENK INKIIKDMNE KLKNKICSFI EKLKLWREKS IHIDIDEFIW FLYVETGYYG
YAGALQAGEQ RQANLRILFQ RAKQYAKTSY KGLFNFINFI NKLKFSSGDM GSAKILGENE
NVVRIMSIHK SKGLEFPVVI LSGTGKNFNM TDLNKNILFH RDLGYGPDYV DTERRIAYPS
LVKNIIKNKI RLETLSEEMR ILYVALTRAR EKLIITGLIN NMDKTVEDWL NLSEDKNKVP
EYAVMSGKTY LDWIGPALIK HKDAVSFREE LKMTSELSNI VDDKSKWKIE LWNKRELLKE
KVEEDEVEIS EKIKETLMNL EESNYKEEIY KRLSFKYKYD NASSIPTKLS VSDVKKQFIL
DEKENTEELF KKLELRKPMF MEEKKKISPS ERGTIIHLFM QHLDLKKAEN EEDIKEQINR
LIEREFITYE QSKVINPYKI LKFCRGELGK RILNSNNVNK EMPFSIEIPA LEIYKELDKE
IYKDEKLIIQ GVIDCYFEEE DGLVLLDYKT DYVNDIEEIK NRYEIQIKYY EEALNRITGK
NVKDKYLYLF SVDNYIKID
