ID   SBCC_STAAE              Reviewed;        1009 AA.
AC   A6QGP8;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Nuclease SbcCD subunit C;
GN   Name=sbcC; OrderedLocusNames=NWMN_1258;
OS   Staphylococcus aureus (strain Newman).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=426430;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Newman;
RX   PubMed=17951380; DOI=10.1128/jb.01000-07;
RA   Baba T., Bae T., Schneewind O., Takeuchi F., Hiramatsu K.;
RT   "Genome sequence of Staphylococcus aureus strain Newman and comparative
RT   analysis of staphylococcal genomes: polymorphism and evolution of two major
RT   pathogenicity islands.";
RL   J. Bacteriol. 190:300-310(2008).
RN   [2]
RP   FUNCTION IN THE REPRESSION OF TYPE 5 CAPSULE PRODUCTION AND SOS RESPONSE,
RP   DEVELOPMENTAL STAGE, AND INDUCTION BY CIPROFLOXACIN AND MITOMYCIN C.
RX   PubMed=17704228; DOI=10.1128/jb.01079-07;
RA   Chen Z., Luong T.T., Lee C.Y.;
RT   "The sbcDC locus mediates repression of type 5 capsule production as part
RT   of the SOS response in Staphylococcus aureus.";
RL   J. Bacteriol. 189:7343-7350(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 involved in the repression of
CC       type 5 capsule production by down-regulating cap5 genes via the arl-mgr
CC       pathway. Is probably part of the SOS regulon and involved in DNA
CC       recombination and repair. {ECO:0000250, ECO:0000269|PubMed:17704228}.
CC   -!- SUBUNIT: Heterodimer of SbcC and SbcD. {ECO:0000250}.
CC   -!- DEVELOPMENTAL STAGE: Expressed very early in the exponential growth
CC       phase. {ECO:0000269|PubMed:17704228}.
CC   -!- INDUCTION: Induced by ciprofloxacin or mitomycin C in subinhibitory
CC       concentration. {ECO:0000269|PubMed:17704228}.
CC   -!- SIMILARITY: Belongs to the SMC family. SbcC subfamily. {ECO:0000305}.
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DR   EMBL; AP009351; BAF67530.1; -; Genomic_DNA.
DR   RefSeq; WP_000803164.1; NZ_CP023390.1.
DR   AlphaFoldDB; A6QGP8; -.
DR   SMR; A6QGP8; -.
DR   EnsemblBacteria; BAF67530; BAF67530; NWMN_1258.
DR   KEGG; sae:NWMN_1258; -.
DR   HOGENOM; CLU_004785_2_1_9; -.
DR   OMA; ISHVQEM; -.
DR   Proteomes; UP000006386; 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; SOS response.
FT   CHAIN           1..1009
FT                   /note="Nuclease SbcCD subunit C"
FT                   /id="PRO_0000338471"
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;  117317 MW;  8CB613CE529CE036 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 VQLKEQQPEI
     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 SLESIFIDEG FGTLDQETLE
     TALDTLLNLK STGRMVGIIS HVSELKNRIP LVLEVKSDQY QSSTRFKRN