ID   SBCC_STAAR              Reviewed;        1009 AA.
AC   Q6GH60;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Nuclease SbcCD subunit C;
GN   Name=sbcC; OrderedLocusNames=SAR1357;
OS   Staphylococcus aureus (strain MRSA252).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282458;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MRSA252;
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA   Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA   Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA   Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA   Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT   for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
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; BX571856; CAG40355.1; -; Genomic_DNA.
DR   RefSeq; WP_000803176.1; NC_002952.2.
DR   AlphaFoldDB; Q6GH60; -.
DR   SMR; Q6GH60; -.
DR   KEGG; sar:SAR1357; -.
DR   HOGENOM; CLU_004785_2_1_9; -.
DR   OMA; ISHVQEM; -.
DR   OrthoDB; 1143316at2; -.
DR   Proteomes; UP000000596; 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..1009
FT                   /note="Nuclease SbcCD subunit C"
FT                   /id="PRO_0000338464"
FT   COILED          176..208
FT                   /evidence="ECO:0000255"
FT   COILED          264..366
FT                   /evidence="ECO:0000255"
FT   COILED          392..501
FT                   /evidence="ECO:0000255"
FT   COILED          535..638
FT                   /evidence="ECO:0000255"
FT   COILED          664..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;  117508 MW;  8F6E504F5765086C CRC64;
     MKPLHLKLNN FGPFLKEEID FSKIDNNELF LISGKTGSGK TMIFDAMTYA LFGKASTEQR
     EENDLRSHFA DGKQPMSVTF EFQLNNRIYK VHRQGPYIKE GNTTKTNAKF DVFEMVDGKY
     EIRESKVISG TQFIIELLGV NADQFRQLFI LPQGEFKRFL ISNSREKQGI LRTLFDSEKF
     EAIREILKEE VKKENAQIEN RYQQIDLLWQ EIESFDDDKI KGLLEVATQQ IDKVIENIPL
     LQARSKEILA FVNESKETAI KDYEIIEKKT LENNILKDNI NQLNKNKIDF VQLKEQQPEI
     EEIEAKLKLL QDITNLLNYI ENREKIETKI ANSKKDISET NNKILNLECD KRNIDKEKRM
     LEENGDLIES KISFIDKTRV LFNDINKYQQ SYLNIERLRT EGEQLADELN NLIEGLEKVE
     DSIGNNESDY EKIIELNNAI TNINNEINVI KENEKAKAEL DKLLGSKQEL ENQINEETST
     LKNLEIKLDR YDKSKLDLND KESFISEIKS AVKIGDQCPI CGNEIQDLGH HIDFDSIAKR
     QNEIKEIEAN IHTMKSNIAV HNSEIKFVNE KISNINIKTQ SDFSLEVLNK RLLENENALN
     NQRELNKFIE QMKEEKDNLT LQIHNKQLRL NKNESELKLC RNLITEFETL SKYNNITNFE
     VDYKKYVQDV NQHQEHSNQI EDKLIQLSQR KLIEQNNLNH YEKQLETYNN DLELNEQSIE
     MEMSRLNLTD NNDINEIIAW RGEQEELEQK RDTYKKRYHE FEMEIARLES LTKDKELLDS
     DKLKDEYELK KGKMNTLIDE YSAVHYQCQN NINKTQSIVS HINYLNQELK DQQEIFQLAE
     IVSGKNNKNL TLENFVLIYY LDQIIAQANL RLATMSDNRY QLIRREAVSH GLSGLEIDVF
     DLHSNKSRHI SSLSGGETFQ SSLALALGLS EIVQQQSGGI SLESIFIDEG FGTLDQETLE
     TALDTLLNLK STGRMVGIIS HVSELKNRIP LVLEVKSDQY QSSTRFKRN