ID ADDA_RUMCH Reviewed; 1248 AA.
AC B8I2Y2;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 85.
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=5.6.2.4 {ECO:0000255|HAMAP-Rule:MF_01451};
DE AltName: Full=ATP-dependent helicase/nuclease AddA {ECO:0000255|HAMAP-Rule:MF_01451};
DE AltName: Full=DNA 3'-5' helicase AddA {ECO:0000255|HAMAP-Rule:MF_01451};
GN Name=addA {ECO:0000255|HAMAP-Rule:MF_01451}; OrderedLocusNames=Ccel_1774;
OS Ruminiclostridium cellulolyticum (strain ATCC 35319 / DSM 5812 / JCM 6584 /
OS H10) (Clostridium cellulolyticum).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Ruminiclostridium.
OX NCBI_TaxID=394503;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35319 / DSM 5812 / JCM 6584 / H10;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Saunders E., Brettin T.,
RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Ivanova N., Zhou J., Richardson P.;
RT "Complete sequence of Clostridium cellulolyticum H10.";
RL Submitted (JAN-2009) 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=Couples ATP hydrolysis with the unwinding of duplex DNA by
CC translocating in the 3'-5' direction.; EC=5.6.2.4;
CC Evidence={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=5.6.2.4;
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; CP001348; ACL76125.1; -; Genomic_DNA.
DR RefSeq; WP_015925240.1; NC_011898.1.
DR AlphaFoldDB; B8I2Y2; -.
DR SMR; B8I2Y2; -.
DR STRING; 394503.Ccel_1774; -.
DR KEGG; cce:Ccel_1774; -.
DR eggNOG; COG1074; Bacteria.
DR HOGENOM; CLU_001114_3_1_9; -.
DR OrthoDB; 9810135at2; -.
DR Proteomes; UP000001349; 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:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:UniProtKB-UniRule.
DR CDD; cd18807; SF1_C_UvrD; 1.
DR Gene3D; 3.90.320.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 4.
DR HAMAP; MF_01451; AddA; 1.
DR InterPro; IPR014152; AddA.
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 NCBIfam; TIGR02785; addA_Gpos; 1.
DR PANTHER; PTHR11070:SF48; ATP-DEPENDENT HELICASE_NUCLEASE SUBUNIT A; 1.
DR PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR Pfam; PF12705; PDDEXK_1; 1.
DR Pfam; PF00580; UvrD-helicase; 1.
DR Pfam; PF13361; UvrD_C; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF52980; Restriction endonuclease-like; 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; Isomerase; Nuclease; Nucleotide-binding; Reference proteome.
FT CHAIN 1..1248
FT /note="ATP-dependent helicase/nuclease subunit A"
FT /id="PRO_0000379256"
FT DOMAIN 4..480
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT DOMAIN 523..820
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT BINDING 25..32
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
SQ SEQUENCE 1248 AA; 143543 MW; BAA03DAF0D2340B1 CRC64;
MSETKWTKEQ YAAITQKDCN LLVAAAAGAG KTAVLVERII RKITDKENPV DIDSLLVVTF
TNAAATEMRE RIGAAISDTI EKNQGSKNIS RQLILLNKAS ITTIHSFCLE VIRSNFQSIE
IDPGFKILDE TEATLLKSET LSDLFEEIYE DAEENEDFFE LLESYGGNRD DLKIQDMVMS
IYSFVQSYPW PEKWLEQQIE SYNFEVGNDF GETTWGRILL ETSLMRLEGL RDIMNEACAK
IKNAQGLEKY LSVFIEDNDN LEKLIGICKT GMNWDQLYNY VNSFEFRNLP RCGKDAEKSV
QESVKKIRDE LKSVINGLRD EVFFMESDEI ASDLKTMYPI LKCVSRLVMD FGRRYAHKKS
QRASVDFNDL EHFCLNILAE TDKDGNIRPT KIAQNYKDKF TEILVDEYQD SNLVQEIIIN
MISKKDIGSP NVFMVGDVKQ SIYRFRQAKP ELFLEKYNNY SIDEDSSYRK ILLFKNFRSR
KDVVDGINYI FKQIMSQKVG ELDYNEIEEL NPGAGFSPCQ NEETVVGGAI ELHLIETSVG
DNTVLSEGSE PMDEQDFPEE DEILDNIQKE ARMVANRIIE LFQADKDGKK YAVYDKKLGE
YRNVRFSDIV ILLRTTRNWT EVFSAELANA DIPVFADTGS GFFKTPEVQV VLSLLQIIDN
PYQDIPLLAV LRSPIVNFST ADLTDVRLMN RNASIFEALK ETAVHDTQVS KKASDFLQKL
EKWRDMSLYM STHELIWQLY NETGYFSIVG AMQDGERKQA NLKILFERAL QYENTSYSGL
FNFISFIDKL KTNKGDMGSA KVLGENDNVV RLMSIHKSKG LEFPVVFLCG CGKKFNMQDM
YKSILLHQEL GFGPDFVDYK KRIKYPSIPK QAIAQKIRIE TLSEEMRILY VAMTRAREKL
IITGSVNNIE KSALKWLGTA QSNDNKFPPH NMLKAQNYLD WICPSVMRHK DSVILRNAAG
LGVDYSGPTI SDDSSWTIIL ADQSDIAVAK RFETDTQDRE DITKWLQEKG SADSGDSHEI
HRRLDWKYTY RDFAQIPSKI SVTELKRYFH LNNDEDNSQL QYKTATIKKP AFLEGKKGLS
PAEKGTAMHF VMQHLDFHNE DIAGQVKIMV KKELLTEIQA KSIDIMKISA FINSVIGKRM
LKSVKVYREV PFNIELPYKE IYPQLPDVSD YEDKILLQGV VDCYFEEEDH IVLIDYKTDY
IPYGDKQSVK EKYRLQISYY SRALEMLTLK RVKERYIYLF STGEIVEM
//
