ADDA_THEPX
ID ADDA_THEPX Reviewed; 1233 AA.
AC B0K213;
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};
GN OrderedLocusNames=Teth514_0203;
OS Thermoanaerobacter sp. (strain X514).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Thermoanaerobacter;
OC unclassified Thermoanaerobacter.
OX NCBI_TaxID=399726;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=X514;
RG US DOE Joint Genome Institute;
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., Kim E., Hemme C., Fields M.W., He Z., Zhou J., Richardson P.;
RT "Complete sequence of Thermoanaerobacter sp. X514.";
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; CP000923; ABY91521.1; -; Genomic_DNA.
DR RefSeq; WP_009051916.1; NC_010320.1.
DR AlphaFoldDB; B0K213; -.
DR SMR; B0K213; -.
DR PRIDE; B0K213; -.
DR EnsemblBacteria; ABY91521; ABY91521; Teth514_0203.
DR KEGG; tex:Teth514_0203; -.
DR HOGENOM; CLU_001114_3_1_9; -.
DR OMA; KQSIYRW; -.
DR Proteomes; UP000002155; 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.
FT CHAIN 1..1233
FT /note="ATP-dependent helicase/nuclease subunit A"
FT /id="PRO_0000379361"
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; 143748 MW; 3503FE2336A5EF83 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 GDVNPSEVAL HYREKFEEIF VDEYQDSNLI QEEILSIIAR
ENPPNRFMVG DVKQSIYRFR QANPYIFFEK YNSYSLDTGE KNQKILLYKN FRSRIEVIEA
INYIFKKIMS KNIGEVNYTE EEKLNYGAEY EIPPEDSVTG GAVELHLIEK QKVEEEVEEK
EEEKNEEKDF EEEEEDLIDD IQVEARVVAE RIKQLFSQNF MVYDKNIKSY RAVDYRDIVV
LLRATDRWAP VFLEELTQAG IPAFADTGTG YFDTTEIKTI ISLLQVIDNP MQDIPLLAVL
RSPIFSFTEE ELIDLRLEDM EKTIYEAIKK ASQREDELGE KAKNFLDTLK KWQEKAVYMP
VDEFLWYLYK DTGYYSYVAA MPQGVQRQAN LRILFERAKQ YEETSFKGLF NFINFINRLK
VSSGDMGSAK IVGENEKVVR 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
