ADDA_PELTS
ID ADDA_PELTS Reviewed; 1269 AA.
AC A5D1P3;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 88.
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=PTH_1664;
OS Pelotomaculum thermopropionicum (strain DSM 13744 / JCM 10971 / SI).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Desulfotomaculaceae;
OC Pelotomaculum.
OX NCBI_TaxID=370438;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13744 / JCM 10971 / SI;
RX PubMed=18218977; DOI=10.1101/gr.7136508;
RA Kosaka T., Kato S., Shimoyama T., Ishii S., Abe T., Watanabe K.;
RT "The genome of Pelotomaculum thermopropionicum reveals niche-associated
RT evolution in anaerobic microbiota.";
RL Genome Res. 18:442-448(2008).
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; AP009389; BAF59845.1; -; Genomic_DNA.
DR AlphaFoldDB; A5D1P3; -.
DR SMR; A5D1P3; -.
DR STRING; 370438.PTH_1664; -.
DR EnsemblBacteria; BAF59845; BAF59845; PTH_1664.
DR KEGG; pth:PTH_1664; -.
DR eggNOG; COG1074; Bacteria.
DR HOGENOM; CLU_001114_3_1_9; -.
DR OMA; KQSIYRW; -.
DR Proteomes; UP000006556; 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..1269
FT /note="ATP-dependent helicase/nuclease subunit A"
FT /id="PRO_0000379306"
FT DOMAIN 17..492
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT DOMAIN 541..838
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT BINDING 38..45
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
SQ SEQUENCE 1269 AA; 139981 MW; 28B3672B6F3627BC CRC64;
MEQTGPDVPE RVGAMSGGWT AEQLEAISAR GGDVLVAASA GTGKTAVLAE RIIRRITDPI
KPVDVDRLLV VTFTSAAAAE MRERIRLALA REISRRPESG HLQRQAALLG RACISTVHSF
CLDLLRQHFY RIGLDPSFRV ADETEAALIQ TGALEEVFER RYAAEDNIFA ALVDCYGGRH
DDALLQELVL DAYKFARSTP WPEDWLDGLA EGFNLPGGAS FDRTPWSAVL KQAAEIELAG
ARADLEAALR IAREPGGPQA YLANLEQEHD LVCRLLQSCR TNAPWAELYS YFKEVVFSPL
KQCRKEDADL KLAGQARNFR ESAKKKVMQV KSRYFSLPPE DLCADLRRMA PLIKELAGLV
REFDATYRKA KAARGVVDFN DLEHYCLQVL AEKGPSGAVP SQVAHELQEK FVEVLVDEYQ
DINAVQETIL QMVSRKGEGQ SNLFMVGDVK QSIYRFRLAE PGLFLKKYAS FSAGTGGGQG
RRLALTANFR SRQGVVSAVN FIFKQIMTPA VGEMAYGSDA MLVYGADYPP VPEGQGNYEE
AVELHLVERG PAGKDGGGDD PAGEEADGGV EAVEEIEEEL EAGQKEARLV ARRIKELLGG
SPGGEHALEI YDRELKKYRP LTYRDVAVLL RATAGYANSF VEEFRREGIP AYAELSTGYF
ESTEVETVIS LLKVIDNPRQ DIPLAGVLRS PAVGLKAGDL ARIRLASPRG DFYDAVVAAS
LAGQGELSER LADFLKKLEE WRTIARQGTL ADLIWAVYRD TGYYDFTGCL PGGGQRQANL
RALHDRARQF ETTAFRGLFL FLRFIERLRE GGRDFGAARL LSEKENVVRI MSIHKSKGLE
FPVVFVAGLG RNFNFRNLNK AVLFHKDLGL GPQLVDAEAR VTRPTAAKLA LKHRLKMEAL
AEEMRILYVA MTRAQEKLIL VGSARNLPGC ARRWCGPAGT AGWALPDGFL AGAGTCLDWL
MAALARHRDG AAIRELAACA EEPPAEVAAD RSRWRVFFSD SRGRSAEMAE EPVLLAKVRR
MEPLEPAGPL AGMIKARLEW SYPAIAVLGR PAKAAVTELK RRFDQLAAGE EQYGEGHFES
FRLTAGRPLF MQEKRGLTAA EAGEALHLVM QHLDLTGSLD ITAVRSQIED MVWRELLTPE
QAAAVPAEKI AAFFAGPLGR RLLAGFQVLR ELPFTMAVQA AEIYPELVPY PGEAVLVQGV
IDCLVDEGDG YLLLDYKTGK RPLGRPEEAA RRYCGQLNIY ARAVESILGR KVKEKYLYLF
EPGLEIRCD
