ADDA_THEP3
ID ADDA_THEP3 Reviewed; 1233 AA.
AC B0KDB7;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 1.
DT 03-AUG-2022, entry version 81.
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=Teth39_2010;
OS Thermoanaerobacter pseudethanolicus (strain ATCC 33223 / 39E) (Clostridium
OS thermohydrosulfuricum).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Thermoanaerobacter.
OX NCBI_TaxID=340099;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33223 / DSM 2355 / 39E;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Bruce D., Goodwin L., Saunders E., Brettin T.,
RA Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Lykidis A., Hemme C., Fields M.W., He Z., Zhou J.,
RA Richardson P.;
RT "Complete sequence of Thermoanaerobacter pseudethanolicus 39E.";
RL Submitted (JAN-2008) 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; CP000924; ABY95636.1; -; Genomic_DNA.
DR RefSeq; WP_012269714.1; NC_010321.1.
DR AlphaFoldDB; B0KDB7; -.
DR SMR; B0KDB7; -.
DR STRING; 340099.Teth39_2010; -.
DR EnsemblBacteria; ABY95636; ABY95636; Teth39_2010.
DR KEGG; tpd:Teth39_2010; -.
DR eggNOG; COG1074; Bacteria.
DR HOGENOM; CLU_001114_3_1_9; -.
DR OMA; KQSIYRW; -.
DR Proteomes; UP000002156; 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..1233
FT /note="ATP-dependent helicase/nuclease subunit A"
FT /id="PRO_0000379360"
FT DOMAIN 3..474
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT DOMAIN 518..809
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT REGION 533..555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 539..555
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 24..31
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
SQ SEQUENCE 1233 AA; 143718 MW; 452F787C82B0E930 CRC64;
MGTKWTEEQK QAITTRGSNL LVAAAAGSGK TAVLVERIIN LITDEENPVD IDRLLVVTFT
NAAASEMRER IAEALIAILD QNPEDKRLAN QLTLLNKATI TTIHSFCLEV VRNNFFLLDL
DPNFRIGDDT ETLLLQLEAS EELFEEMYAK EDKDKEGFLT LVESYGGTKD DQDLQDILLR
LYGFVRSLPW PEKWLKDVIN TFRVEDNFKF ETSKWAEVIL DSLKVEISGI LNTMLVAVDK
LKNEAGLEGY FHAFQREAYE IEQLLQYDNW NEFKNHIQAI EFERLPNAGK DANKNVKEEV
SNIRKKVKDK IKEIKEKFFS DSVEEIKDEI KALYPIMEAL ADLILLFDKK YKEKKREKGI
IDFNDIEHFA LQILTEIDEE GAVNPSEVAL HYREKFEEIF VDEYQDSNLI QEEILSIIAR
ENPPNRFMVG DVKQSIYRFR QANPYIFFEK YNSYSLDTGE KNQKILLYKN FRSRIEVIEA
INYIFKKIMS KNIGEVNYTE EEKLNYGAEY EIPPEDSVTG GAVELHLIEK QKVEEEVEEK
EEEKNEEKDF EEEEEDLIDD IQVEARVVAE RIKQLFSQNF MVYDKNIKSY RVVDYRDIVV
LLRATDRWAP VFLEELTQAG IPAFADTGTG YFDTTEIKTI ISLLQVIDNP MQDIPLLAVL
RSPIFSFTEE ELIDLRLEDM EKTIYEAIKK ASQREDELGE KAKNFLDTLK KWQEKAVYMP
VDEFLWYLYK DTGYYSYVAA MPQGVQRQAN LRILFERAKQ YEETSFKGLF NFINFINRLK
VSSGDMGSAK IVGENENVVR IMSIHKSKGL EFPVVIVAGL GKQFNTKDLY QKILYHHFLG
LGPEFVDFRR RISYPSIVKE AIKYKIKLEG LSEEMRVLYV ALTRAKEKLI LVGSARDIKK
NVRKWANAAI LQEKVSEYDI LNGKSYMDWI GAAVIRHKDL EPLREFAGVS LSEEEDASKW
EVKLWNKKDV LLEKEKNDKV DVVERLRSLD LDAHYSEFYK EVERRLNYVY PYEKACYLPA
KLSVTEVKRI LNAEVVDEDT TSIFEREVLK TPIFLEKKKG LTAAEKGIAM HLVMQKLDLD
KDLSLEGIKE QIKDMVDREI LTEEQAKEVN IHKIEGFFKT SLGERMLSSK NVKREVPFHI
KLSSREIYKD LPEEYENEFI QVQGIIDCFF EEEDGLVLID YKTDYVQEGK VEEIKERYKV
QIELYSKALE NITGKKVKEK YIYLFFNGNI LEY
