ID   SBCC_STAHJ              Reviewed;        1011 AA.
AC   Q4L655;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Nuclease SbcCD subunit C;
GN   Name=sbcC; OrderedLocusNames=SH1561;
OS   Staphylococcus haemolyticus (strain JCSC1435).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=279808;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCSC1435;
RX   PubMed=16237012; DOI=10.1128/jb.187.21.7292-7308.2005;
RA   Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA   Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA   Hiramatsu K.;
RT   "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT   extreme plasticity of its genome and the evolution of human-colonizing
RT   staphylococcal species.";
RL   J. Bacteriol. 187:7292-7308(2005).
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; AP006716; BAE04870.1; -; Genomic_DNA.
DR   RefSeq; WP_011275852.1; NC_007168.1.
DR   AlphaFoldDB; Q4L655; -.
DR   SMR; Q4L655; -.
DR   STRING; 279808.SH1561; -.
DR   EnsemblBacteria; BAE04870; BAE04870; SH1561.
DR   KEGG; sha:SH1561; -.
DR   eggNOG; COG0419; Bacteria.
DR   HOGENOM; CLU_004785_2_0_9; -.
DR   OMA; ISHVQEM; -.
DR   OrthoDB; 1143316at2; -.
DR   Proteomes; UP000000543; 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; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Coiled coil; DNA recombination; DNA replication; Endonuclease;
KW   Exonuclease; Hydrolase; Nuclease; Nucleotide-binding.
FT   CHAIN           1..1011
FT                   /note="Nuclease SbcCD subunit C"
FT                   /id="PRO_0000338476"
FT   COILED          181..210
FT                   /evidence="ECO:0000255"
FT   BINDING         34..41
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1011 AA;  118626 MW;  9CEBEB3977E8D4FA CRC64;
     MRPTKLILNN FGPFIHEVID FEQINKEQLF LISGKTGSGK TMLFDGIVYA LFGKASTEGR
     NEGELRSHFA DGKSPMSVEY EFKINDKKFK ISRQAGFIKE GNTSLTPGKL DVFEFDEESQ
     LYELRESKIS SGNGFIKDLL GINAEQFRQL FILPQGEFKK FLVSNSSDKQ SILRTLFNSI
     RFEEMQNLLL NQVKDEKKQI ESRYSRIQIL WEDIETFEND ELIQFKSLNS MQTKDIIKAI
     PQFELVGQHL NEEYEQLKSE HNDALEAIKR KIEENNKLIE SLKELDRNKD KKVQLEKNKD
     SIEKLKAELR KIIEIKPLSQ LYNQRNTKEQ KYENTKVKLN SILEELNELN DKLEKFKKEK
     EILNEQLEDI NIKSEYIDKT KQFYSNINKY REAFNEIKQN ETYLKENNQK QEENKNLIDK
     LNNDIAKIDV NNENIDEITQ EIFQLTNTFD KKVTLRENKK KYQSLSQKYN ETENSIKKTK
     EQISDLKLQL ENIDKSNIDL NDKQTFIQEI QNALHVGDTC PICGNEIESL NEHIKFDEIA
     KNQNLIKEVN NQLNKKINEL TKLETTSDYI SNQMSELEIN DDEICDINEI EQQLRTKNKE
     KEKLQIQIKQ REKLKSALDK HKDIKHSLQI KHEKLLSLKH QFETLINEFK SYTNYDETNK
     FEQCFKQYEQ IVTDYVSKSE VLEKEINQTK QQIEIETNNL NNNKLAIKEL EQEISGHSDE
     INQEMKRIGL NSYKDVEILL SKLENKEQIE MKIQQYEHDH QKLTLEIERL SKLTKDNKSE
     SVEKLEATKT EIESNYNKYV EASATIQYQV QKNKDKFNSI MDHINYLEKE LKEQQEIFEL
     SEVLSGKNSK KLTLENYVLI YYLERIIHQA NIRLERMSGE RYQLKRRESI SHGYSGLEIE
     VFDFHSNKSR HISSLSGGET FQASLALALG LSEVVQQESG GITLESMFID EGFGTLDQET
     LETALDTLVK LKTSGRMVGI ISHVSELKQR IPLILEVTSN QYQSHTRFKW N