ID   SBCC_STAA8              Reviewed;        1009 AA.
AC   Q2FYT3;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 2.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Nuclease SbcCD subunit C;
GN   Name=sbcC; OrderedLocusNames=SAOUHSC_01342;
OS   Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 8325 / PS 47;
RA   Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT   "The Staphylococcus aureus NCTC 8325 genome.";
RL   (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL   Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL   D.C. (2006).
RN   [2]
RP   FUNCTION IN SOS RESPONSE, AND INDUCTION BY CIPROFLOXACIN AND LEXA.
RX   PubMed=17085555; DOI=10.1128/jb.01464-06;
RA   Cirz R.T., Jones M.B., Gingles N.A., Minogue T.D., Jarrahi B.,
RA   Peterson S.N., Romesberg F.E.;
RT   "Complete and SOS-mediated response of Staphylococcus aureus to the
RT   antibiotic ciprofloxacin.";
RL   J. Bacteriol. 189:531-539(2007).
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). Is probably part of the SOS
CC       regulon and involved in DNA recombination and repair. {ECO:0000250,
CC       ECO:0000269|PubMed:17085555}.
CC   -!- SUBUNIT: Heterodimer of SbcC and SbcD. {ECO:0000250}.
CC   -!- INDUCTION: Induced by ciprofloxacin and up-regulated by LexA.
CC       {ECO:0000269|PubMed:17085555}.
CC   -!- SIMILARITY: Belongs to the SMC family. SbcC subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABD30439.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; CP000253; ABD30439.1; ALT_FRAME; Genomic_DNA.
DR   AlphaFoldDB; Q2FYT3; -.
DR   STRING; 1280.SAXN108_1363; -.
DR   EnsemblBacteria; ABD30439; ABD30439; SAOUHSC_01342.
DR   eggNOG; COG0419; Bacteria.
DR   HOGENOM; CLU_004785_2_1_9; -.
DR   Proteomes; UP000008816; 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:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:0009432; P:SOS response; 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   1: Evidence at protein level;
KW   ATP-binding; Coiled coil; DNA damage; DNA recombination; DNA repair;
KW   DNA replication; Endonuclease; Exonuclease; Hydrolase; Nuclease;
KW   Nucleotide-binding; Reference proteome; SOS response.
FT   CHAIN           1..1009
FT                   /note="Nuclease SbcCD subunit C"
FT                   /id="PRO_0000338470"
FT   COILED          176..364
FT                   /evidence="ECO:0000255"
FT   COILED          392..502
FT                   /evidence="ECO:0000255"
FT   COILED          535..802
FT                   /evidence="ECO:0000255"
FT   BINDING         34..41
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1009 AA;  117275 MW;  CAA58BD28A7D1CBB CRC64;
     MKPLHLKLNN FGPFLKEEID FSKIDNNELF LISGKTGSGK TMIFDAMTYA LFGKASTEQR
     EENDLRSHFA DGKQPMSVTF EFQLNHRIYK VHRQGPYIKE GNTTKTNAKF DVFEMVDGKY
     EIRESKVISG TQFIIELLGV NADQFRQLFI LPQGEFKRFL ISNSREKQGI LRTLFDSEKF
     EAIREILKEE VKKEKAQIEN RYQQIDLLWQ EIESFDDDNI KGLLEVATQQ IDKLIENIPL
     LQARSKEILA SVNESKETAI KEFEIIEKKT LENNILKDNI NQLNKNKIDF VQLNEQQPEI
     EGIEAKLKLL QDITNLLNYI ENREKIETKI ANSKKDISKT NNKILNLDCD KRNIDKEKKM
     LEENGDLIES KISFIDKTRV LFNDINKYQQ SYLNIERLRT EGEQLGDELN DLIKGLETVE
     DSIGNNQSDY EKIIELNNTI TNINNEINII KENEKAKAEL DKLLGSKQEL ENQINEETSI
     LKNLEIKLDR YDKTKLDLND KESFISEIKS AVNIGDQCPI CGNEIQDLGH HIDFDSIAKR
     QNEIKEIEAN IHAIKSNIAV HNSEIKFVNE KISNINIKTQ SDFSLEVLNK RLLENENALN
     NQRDLNKFIE QMKEEKDNLT LQIHNKQLRL NKNESELKLC RDLITEFETL SKYNNITNFE
     VDYKKYVQDV NQHQELSKEI EDKLMQLSQR KLIEQNNLNH YENQLETYNN DLELNEQSIE
     MEMSRLNLTD DNDIDEIIAW RGEQEELEQK RDTYKKRYHE FEMEIARLES LTKDKELLDS
     DKLKDEYELK KGKMNTLIDE YSAVHYQCQN NINKTQSIVS HINYLNQELK DQQEIFQLAE
     IVSGKNNKNL TLENFVLIYY LDQIIAQANL RLATMSDNRY QLIRREAVSH GLSGLEIDVF
     DLHSNKSRHI SSLSGGETFQ SSLALALGLS EIVQQQSGGI SLTSIFIDEG FGTLDQETLE
     TALDTLLNLK STGRMVGIIS HVSELKNRIP LVLEVKSDQY QSSTRFKRN