ADDA_SYMTH
ID ADDA_SYMTH Reviewed; 1371 AA.
AC Q67MD5;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 109.
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=STH2173;
OS Symbiobacterium thermophilum (strain T / IAM 14863).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Symbiobacteriaceae;
OC Symbiobacterium.
OX NCBI_TaxID=292459;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T / IAM 14863;
RX PubMed=15383646; DOI=10.1093/nar/gkh830;
RA Ueda K., Yamashita A., Ishikawa J., Shimada M., Watsuji T., Morimura K.,
RA Ikeda H., Hattori M., Beppu T.;
RT "Genome sequence of Symbiobacterium thermophilum, an uncultivable bacterium
RT that depends on microbial commensalism.";
RL Nucleic Acids Res. 32:4937-4944(2004).
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; AP006840; BAD41158.1; -; Genomic_DNA.
DR AlphaFoldDB; Q67MD5; -.
DR SMR; Q67MD5; -.
DR STRING; 292459.STH2173; -.
DR EnsemblBacteria; BAD41158; BAD41158; STH2173.
DR KEGG; sth:STH2173; -.
DR eggNOG; COG1074; Bacteria.
DR HOGENOM; CLU_001114_3_1_9; -.
DR OMA; KQSIYRW; -.
DR Proteomes; UP000000417; 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; 2.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF52980; SSF52980; 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..1371
FT /note="ATP-dependent helicase/nuclease subunit A"
FT /id="PRO_0000379358"
FT DOMAIN 7..489
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT DOMAIN 553..898
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT REGION 544..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1035..1055
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1141..1187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 28..35
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
SQ SEQUENCE 1371 AA; 148869 MW; 0340FC02558E0E3C CRC64;
MRAMSDVRWT PEQEQAITAR GADVLVAAAA GSGKTAVLVE RIIRRLVDER DPLDVDQLLV
VTFTEAAATE MRDRIGAALQ AALAGNPENE RLQRQLALLG RASISTLHSF CLSLVRQYFY
RLGLDPAVSV MGEHEALLLR HEVLDQLFAR RFDEEEDGPF HALVDRYGGG RDDEGLRNLV
LAIYDHMQAL PWPDQWLEES LARFDVPEGA AIEDLPWWPP LRRQIRLELE LAAEALASAR
ALAARPGGPA AYLDVLAAEE AAVRAAAART ETGSYADLAE AVAAVAFGRL PGTKKGEVDE
GLKEAVGKLR ERAKKAVRAV QEQWFCRTAD EWLADLQAIA PHLRTLGGVV REFAEAFREA
KAAQSAIDFN DLERLALQLL RDSTSTPDRL VPSDVARDLR ARYREILVDE YQDINGVQDA
ILTLVARDGQ EGPPNRFMVG DVKQSIYRFR HADPGLFLAK YGAYRPWAGA PEPGAAGARI
VLGANFRSRE GVVNAVNFLF RQIMSARAGE LDYDRDAELV YRAGYPPLPG EEAAEPPVEL
HLLDGEEQGP ADGAGSGQAP AASGPEAASG DGVAGEADGE EEDPALAELA DLTAMEREAR
LIAARIRAMV DGTADQPPVQ VWDRKLKTYR PLQYRDIAIL LRATTGRINT IIEVLSQSGI
PAYGQVSTGY FQATEVQVFL SLLQVLDNPL QDIPLAAVLH SPIVGLSAAD LARIRLANPR
GSFYDALVAA AAPASGAAMA EAAAAPASEA AMAEAAPAPA SGAAMAEAAA AADPAEAGAT
TSTAPGLEGV LVRFLECLDR WRTLARRRPL SQVVWQILQE TGYLHYVGGM PGGAQRQANL
LALYERAREF DQFARQGLFR FLRFIERLQA EQSDMGTAPA LGEGEDVVRI MSIHKSKGLE
FPVVFVAGLG SSFSDRDLRG DLLLNRDLGF GPQVVDPGTR LKYPTLAYHA VREVTRLANL
AEELRVLYVA LTRARERLVL VGSVKSLRAA CARWSRGAGA PGWPLPESLL LSARSYLDWI
GPAVLRHADG APLRELAGEG GTAPGSGPDP ALAGDPSRWE VTIWDPASLQ QILQPRPEAA
PPAVDWARIG AAEPLDRPLD EALHARLRAR FGWRYPFEPV VRRFGKLSVT ELKGYFDPDA
EAPAEEMAPP AEEMAPPAEE MAPPAEGSAP PVEEPAPSTE PSSSTFAARP RFLQQDRRAL
SPTERGTAVH VVMQHLDLSR PLDAEGVGRQ LAEMVERELL TPQQAAAVDA EAIADFFASP
LGLRILQSRD RVSQELSFTL AVPAAEVYGD LPPEAAAGDV VIVQGMIDLL LEEEDGYVLV
DYKTDRRDPV QAAQRYTTQI RFYRRAVEEI LGRPVKEAYL HFLASRRSIA V