ADDA_LACP7
ID ADDA_LACP7 Reviewed; 1377 AA.
AC A9KTE6;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 84.
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=Cphy_3423;
OS Lachnoclostridium phytofermentans (strain ATCC 700394 / DSM 18823 / ISDg)
OS (Clostridium phytofermentans).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=357809;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700394 / DSM 18823 / ISDg;
RA Leschine S.B., Warnick T.A., Blanchard J.L., Schnell D.J., Petit E.L.,
RA LaTouf W.G., Copeland A., Lucas S., Lapidus A., Barry K.,
RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T.,
RA Bruce D., Detter J.C., Han C., Kuske C., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E.A., Richardson P.;
RT "Complete genome sequence of Clostridium phytofermentans ISDg.";
RL Submitted (NOV-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}.
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; CP000885; ABX43776.1; -; Genomic_DNA.
DR RefSeq; WP_012201425.1; NC_010001.1.
DR AlphaFoldDB; A9KTE6; -.
DR SMR; A9KTE6; -.
DR STRING; 357809.Cphy_3423; -.
DR PRIDE; A9KTE6; -.
DR EnsemblBacteria; ABX43776; ABX43776; Cphy_3423.
DR KEGG; cpy:Cphy_3423; -.
DR eggNOG; COG1074; Bacteria.
DR HOGENOM; CLU_001114_3_1_9; -.
DR OMA; KQSIYRW; -.
DR Proteomes; UP000000370; 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; 2.
DR PANTHER; PTHR11070:SF48; PTHR11070:SF48; 2.
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..1377
FT /note="ATP-dependent helicase/nuclease subunit A"
FT /id="PRO_0000379264"
FT DOMAIN 4..478
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT DOMAIN 526..867
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT REGION 1036..1072
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1038..1058
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 25..32
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
SQ SEQUENCE 1377 AA; 158885 MW; AD2EF901F8EEC2E3 CRC64;
MAKTSWTPGQ QKVIDTRDCN LLVSAAAGSG KTAVLVERII NRITSENSPI NIDQLLIVTF
TKAAAGEMRE RIGAAIEKKV LEQPDNVHLQ KQLTLLYSAQ ITTIDSFCLS VIRNHFHTID
LDPSFRIAEE AELMLLKSDV LATLLEEKYE EGAEDFLEFV ECYSASKSDE PIENFILKLY
QFSQSYPYPH EWLEEREKDF LVETAEDINQ TSWMKQLLQY VKAILREASD LCAKAIEITN
YPDGPKPYLD ALLSDQEIIE RLLNSDAGSQ HSYEEYQDAF SNITFARLST KKWPDATEER
KEEVKAIRQM VKKILSDLSD DFFFQPMEDM LTDMRKVRRP MLVLLSLTHD FLERLDASKE
ENNLVDFSDI EHFALNILVT KEDGNLVPTK VATEMSEQFV EIMIDEYQDS NYVQEYILSS
ISKVTRGCPN VFMVGDVKQS IYKFRMARPE LFMEKYEQYS TEEGLYRRID LSKNFRSRAE
VLDSINGVFE KIMTKAMGGI EYTKEVSLYP GAQFPEIGMD LDNTSFLFSD TKTELIILDL
KEEEASIPDS MDRLDVMALE EDAIELSKRE LEAKAVAMRI KQLVHGERGF SVTKRNGEEQ
DLKRCQYRDI VILLRTMSGW SETFTEILKQ EGIPAYSDTQ TGYFQTLEVK TVLNYLRILD
NPRQDAPLTA ILYSPIVGLS AEQLSFLRVK PGKGAEKLSI YDAARECALN YLEIQDEVTQ
PEETQPVYDS IIQADLMYEK SSAEKTVSMD KNLIETGEKL KRFFATYDKL REKAIYLPVH
EIILEFFKET GYDLFVYAMP GGEQRRNNLN LLVQHALSFE ESSYHGLFQF IRYIERLLKF
EIDYGEAGGL SENDNAVRIM SIHKSKGLEF PVVILAGMGK QFNTMDAREK IVLHADYGIG
PECIDYQLRT KCPTLLKQVI KKNIVLDNLG EELRVLYVAL TRAKEKLIMI GSANDANDVF
DKWRQDSTPG VTPLRFQTLA MAKDYFSFVG PAALYDSRIR VITLTPNDLL EDEYEKQTDI
KNKQEELNPY NFLQSFEEES DEQSDEERSD EERSDGEQSD GEQSDGEQPR KDLLTKLSFR
YPYEHEAMLP IKTTVSELKK LSQQVDEELT ETFTQVKDEL TKTWPQVDEE LTEKYPQVEE
LIETSPPVKE ESQMLIEPTI PKFLKEEKEL RGTERGNLYH KILELIDFSD NKTKLNLREF
VSQLANRGLI QEESISSINF ERLSRFFESE LYQRIQIAYQ KGYLYREQPF VIGIPVREIS
TQKFVRTTQA QASSILSKNE DFSHANLCSC PNSQDYENDD LVLIQGIIDV YFEEEDGIVL
VDYKTDAVGE LGEEELIRRY QEQIRYYERA LNQLLDKTVK EKIIYSFSLG KEIRIKS
