ID   SBCC_VIBCH              Reviewed;        1013 AA.
AC   Q9KM67;
DT   05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Nuclease SbcCD subunit C;
GN   Name=sbcC; OrderedLocusNames=VC_A0521;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
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; AE003853; AAF96424.1; -; Genomic_DNA.
DR   PIR; G82450; G82450.
DR   RefSeq; NP_232912.1; NC_002506.1.
DR   RefSeq; WP_001247622.1; NZ_LT906615.1.
DR   AlphaFoldDB; Q9KM67; -.
DR   SMR; Q9KM67; -.
DR   STRING; 243277.VC_A0521; -.
DR   DNASU; 2612669; -.
DR   EnsemblBacteria; AAF96424; AAF96424; VC_A0521.
DR   GeneID; 57741925; -.
DR   KEGG; vch:VC_A0521; -.
DR   PATRIC; fig|243277.26.peg.3147; -.
DR   eggNOG; COG0419; Bacteria.
DR   HOGENOM; CLU_004785_2_1_6; -.
DR   OMA; ISHVQEM; -.
DR   BioCyc; VCHO:VCA0521-MON; -.
DR   Proteomes; UP000000584; Chromosome 2.
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; 1.
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..1013
FT                   /note="Nuclease SbcCD subunit C"
FT                   /id="PRO_0000105869"
FT   COILED          242..262
FT                   /evidence="ECO:0000255"
FT   COILED          281..486
FT                   /evidence="ECO:0000255"
FT   COILED          604..717
FT                   /evidence="ECO:0000255"
FT   COILED          739..838
FT                   /evidence="ECO:0000255"
FT   BINDING         35..42
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1013 AA;  114592 MW;  4050DE39E5CD3885 CRC64;
     MRPLKLILQA FGPFAGREEI DFTKLGDAPL FLINGATGAG KSSILDAICY ALYGETTGSE
     RTGDQMRCDY AAPESLTEVI FEFELAGARY QITRQPDQEI PKKRGEGMTK KSHSATLVAL
     KSDGNELIAN KPNPVAKAVV ELMGLDVKQF RQVMVLPQGK FRELLTANSK EREQIFGQLF
     QTQLYSQIER ALFERAAGIR KEKEEFDQQI KGTLSVVGLE SEEQLQTELT ELAPVLTHAQ
     SQLKAEQQQW DETKAHYQAA LELEQQFIRK QQLVVEIATH QEQATHIEML RQQRQQAQKA
     ARLTAVHQQW HQAQKNLQQA KLKVEQQQTL LQQAKAQQQQ AQQASQQASL ACEEVPKLNE
     QRITWQRAEQ KLLAQENVQQ AVAKAERELQ LATQNALNLQ QASEKLEQEL QNQRLEWEQQ
     QRQLTRLEVQ KARMNQLVQQ VQAREREQSL LNELQTAQQA LLRFEQQHHH IQTQAEQAKL
     TADKLEFAWH TQRAAELALA LTQNEPCPVC GSLEHPNKAQ YSGDVVTKVQ VEQARQQQQD
     WVQRQQEAFH AWQQQGFKTE QIAQNLTTLS SELTLQQVAL LNELIEQQQI LHSDIAALQQ
     LNPDLLKRQI EEGEQRLAHT KMTLEKQNQN QQQAWQTLAQ LQAELASLRQ EIPPELSDLD
     TLRSAIGRVQ NQIEILQKAE HTAREQWVQA QKQFASVQAA YQAAIEAHRE SQRQQEETTS
     AWQQGLLHSG FSDESAYLAA RLTDEAIVNI ERQIAQYEER SAMLSGEQQA LSRKLAEKNR
     PELEPLLVKV TQAEEKMALA LQAFTQHQSR MDGLQRVAKQ LADLYQKNRA LEAEYQVVGT
     LSDIANGKTG AKVSLHRFVL GVLLDDVLLQ ASQRLMKMSR GRYLLKRKEE RAKGNVGSGL
     DLMVEDSYSG KWRDVATLSG GESFMAALSL ALGLSDVVQA YSGGIRLDTL FIDEGFGSLD
     PESLDLAIQT LIDLQQGGRT IGIISHVTEL KEQIGLRLDV LATRMGSTLR LIT