ID   SBCC_CLOAB              Reviewed;        1163 AA.
AC   Q97FK1;
DT   06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Nuclease SbcCD subunit C;
GN   Name=sbcC; OrderedLocusNames=CA_C2736;
OS   Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS   / VKM B-1787).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=272562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX   PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA   Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA   Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA   Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA   Smith D.R.;
RT   "Genome sequence and comparative analysis of the solvent-producing
RT   bacterium Clostridium acetobutylicum.";
RL   J. Bacteriol. 183:4823-4838(2001).
CC   -!- FUNCTION: SbcCD cleaves DNA hairpin structures. These structures can
CC       inhibit DNA replication and are intermediates in certain DNA
CC       recombination reactions. The complex acts as a 3'->5' double strand
CC       exonuclease that can open hairpins. It also has a 5' single-strand
CC       endonuclease activity (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Heterodimer of SbcC and SbcD. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SMC family. SbcC subfamily. {ECO:0000305}.
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DR   EMBL; AE001437; AAK80682.1; -; Genomic_DNA.
DR   PIR; G97236; G97236.
DR   RefSeq; NP_349342.1; NC_003030.1.
DR   RefSeq; WP_010966023.1; NC_003030.1.
DR   AlphaFoldDB; Q97FK1; -.
DR   SMR; Q97FK1; -.
DR   STRING; 272562.CA_C2736; -.
DR   PRIDE; Q97FK1; -.
DR   EnsemblBacteria; AAK80682; AAK80682; CA_C2736.
DR   GeneID; 44999224; -.
DR   KEGG; cac:CA_C2736; -.
DR   PATRIC; fig|272562.8.peg.2925; -.
DR   eggNOG; COG0419; Bacteria.
DR   HOGENOM; CLU_004785_1_2_9; -.
DR   OMA; ISHVQEM; -.
DR   OrthoDB; 1143316at2; -.
DR   Proteomes; UP000000814; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038729; Rad50/SbcC_AAA.
DR   Pfam; PF13476; AAA_23; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
PE   3: Inferred from homology;
KW   ATP-binding; Coiled coil; DNA recombination; DNA replication; Endonuclease;
KW   Exonuclease; Hydrolase; Nuclease; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..1163
FT                   /note="Nuclease SbcCD subunit C"
FT                   /id="PRO_0000105862"
FT   COILED          197..415
FT                   /evidence="ECO:0000255"
FT   COILED          446..1003
FT                   /evidence="ECO:0000255"
FT   BINDING         35..42
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1163 AA;  135508 MW;  CE5F0BD2215D7A92 CRC64;
     MKPIRVRIKG LNSFENEQEI NFEKLTKRGL FGIFGPTGSG KTTILDSITL SLYGEVARKS
     SNFMNTNCNS LNVSFEFQIS GKEIKRYLVE REFRRDNKTG SVRSKSAKIV DITGDEVEVL
     EEGAKSVNEK CQEIIGLSLD DFTRTVVLPQ GKFSEFLKLE GKERRNMLER LFNLQEYGDE
     LSFKLARKIR KEREKENVLV GELKGYENIN EDVLKERREL LKENNDFFNE ASKEYLKAEE
     EYNEGKEVWG LQIEIEEKNR VRKDLMEKKD EIDLKEKRAR LGESSSKVKP YIDNYENTLK
     QIDILKEQIL SRENTMKAIS LEKEDMEKKL SIAKDNKEKA LPKFMIKHHI ILDAIKEKDL
     LDNIKLEKKR LQGKIEKLSL EASNKEELIK QNIKDIDSLT LKIQNLESKI DNLKVPEEYK
     NKINEGIFLL RNYDEKLKHK NKLGLDCDKF QVDFEKAKSK KEMLFNKLEE ERSKLDTYTK
     KLQDLNKDFP KDDVLLTFQE KLNDSRQKWA KYSEYNESLK ASLRVVENSE QVLRTKKEEM
     TKLEDKISKV NIKIESLETE NMAHVLREKL KSGEACPVCG SVHHIKEGFK EVDLKALETL
     KSELEGFEKK RKFENEEIVM CEASIKVEEK NIKKLNESIN NLGEEFKEVS LESMEKKFNY
     LKEKVNKFNL EKIQLDDNIK DLSERSNKIE VEYQKEKTVE KQCEKRIVDL KSELEEAIKE
     FNEVAYTIEN LKAELKIQDF KFEMKEILEK ERVRVEAEGE IKDLRNLLNI RHTEKEQLMD
     KCSRLKEELS KNKAELKEKD KIINEKIELI KNKVGVLDNL YELKEKIEGT IKKIEEQYNL
     CDKKMNEIED KYRKCSDEII KYHSNLSSLK DRKVNDIDKL NKILMEEKFE NIEKAKENYL
     NDKEINLLKS DVEKYKNELS KVNGAVEVLS KKLKNRKLTE EKWIEIQNNR VEKASKAKAL
     QERSIKLEEE VKNIEIKLKE LGKLLKTKQE LEHKLSLLDD LEKLFKGKKF VEFVALNQLK
     YISIEASKRL KEITGGNYGL EVDDNGKFII RDYKNGGAKR DASTLSGGET FVTSLALALS
     LSNQIQLRGS APLELFFLDE GFGTLDSNLL EVVMDSLEKI HSERLSVGII SHLEVIKERM
     PVRLIVSPAE AGVGGSKVKL EIS