ADDA_ALKOO
ID ADDA_ALKOO Reviewed; 1197 AA.
AC A8MJ41;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 1.
DT 03-AUG-2022, entry version 82.
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=Clos_2290;
OS Alkaliphilus oremlandii (strain OhILAs) (Clostridium oremlandii (strain
OS OhILAs)).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Alkaliphilus.
OX NCBI_TaxID=350688;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OhILAs;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Stolz J.F., Dawson A., Fisher E.,
RA Crable B., Perera E., Lisak J., Ranganathan M., Basu P., Richardson P.;
RT "Complete genome of Alkaliphilus oremlandii OhILAs.";
RL Submitted (OCT-2007) 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; CP000853; ABW19823.1; -; Genomic_DNA.
DR RefSeq; WP_012160130.1; NC_009922.1.
DR AlphaFoldDB; A8MJ41; -.
DR SMR; A8MJ41; -.
DR STRING; 350688.Clos_2290; -.
DR PRIDE; A8MJ41; -.
DR EnsemblBacteria; ABW19823; ABW19823; Clos_2290.
DR KEGG; aoe:Clos_2290; -.
DR eggNOG; COG1074; Bacteria.
DR HOGENOM; CLU_001114_3_1_9; -.
DR OMA; KQSIYRW; -.
DR OrthoDB; 137860at2; -.
DR Proteomes; UP000000269; 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..1197
FT /note="ATP-dependent helicase/nuclease subunit A"
FT /id="PRO_0000379228"
FT DOMAIN 2..458
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT DOMAIN 485..774
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT BINDING 23..30
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
SQ SEQUENCE 1197 AA; 138760 MW; 8C286E572C08BB13 CRC64;
MRQWTKEQQA AIDARGSNLL VAAAAGSGKT AVLVERIIQI ILKDRIDIDR LLIVTFTNAA
AGEMRERIAG AIMTEMEKKT GGEEHLRRQL SLLNRASITT VHSFCIDVVR RHFHMIDVDP
GFRIGDVTET SIMKLEALEE LFEDEYEKGN EEFFNLVEAF GGTREDRPLQ DLVLKIYGFI
QSQPYPEIWL RERVEDFALS IEAFNQSPWI RTIKKRMGIL LKGAMDLLEI AQTIALEPGG
PDVYEEAILS DLDQIKELYH SLENPITDFY EQLNCINFIR LKTSKDSDPI LKEECKDLRD
KAKDIVKDIR ENIFNVSPEE YVEDLNRLYP LMDYLYRLVI GFTERYTEKK TDKGIVDFND
LEHFALRILA NDLAAQEYRE KFEYIFVDEY QDSNIVQETL IQSIKREDNL FMVGDVKQSI
YRFRLADPTL FIEKYETFGT EEGHINRRID LAKNFRSRGQ VLNGVNYIFK HMMSKELGEI
DYDERAALYQ GTEFEPIQDP SIEINLIEKN MEIDEEMEEE LQELADIEVE ARIVAKRIKA
LLNEEIYDPR VEGYRKIEYK DIVVLLRTTQ NWAQSFLEVF VREGIPAYAD ANTGYFEAIE
VNMFLNLLRV IDNKRQDIPL LSVMRSPIGD FTTEELIHIR VNDKTGTYYD AIEKYVEEKT
DDLKYKLVSF IEKLNQWAND ARYIKIDQFI WKLFMDTGYY YYVGAMPGGL QRQANLRVLF
DRANQFEKTS IKGLFNFIKF IEKLQSSKGD MGAAKILGEN DNVVRIMSIH KSKGLEFPVV
ITAGMGKNFN LRDTSADVLL HKDLGLGPKF TDPNLRTYRD TIAKLAMKDQ IKIESLSEEM
RILYVAFTRP KDKLIVVGSI RNIEKQVKKW SKADNVYSLM NAKNYLDWIG TALVKHPDGQ
ALRELGGLGF DAASDGMEDS EWTINILGRQ VIVLEEQDKV LKEEDYREKL LYFNREDFSS
GGYTEYKEEI ENRLNWKYDH PHSVQIPSKL SVSDIKKAHI NEIDVIAHQI PILVKSPKFM
EGKTTFTAAE RGTVIHFVLQ HLDLNKVGSE EDIREQIHWM VARELITEEE SKVVDTKKIL
NYFYSPIGER MRKAKKVYRE SPFIIEKSAG EVIEGLSDDI EDKLLVQGII DCYFEEKDGL
ILIDYKNDIV LNGNIAAVVA RYELQLSLYR EALERITGRE VKETYLYLFD VDQGVRL