ID   SBCC_STAEQ              Reviewed;        1009 AA.
AC   Q5HPJ3;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Nuclease SbcCD subunit C;
GN   Name=sbcC; OrderedLocusNames=SERP0918;
OS   Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176279;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35984 / RP62A;
RX   PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA   Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA   Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA   Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA   Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA   Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA   Fraser C.M.;
RT   "Insights on evolution of virulence and resistance from the complete genome
RT   analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT   a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT   strain.";
RL   J. Bacteriol. 187:2426-2438(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; CP000029; AAW54293.1; -; Genomic_DNA.
DR   RefSeq; WP_002456208.1; NC_002976.3.
DR   AlphaFoldDB; Q5HPJ3; -.
DR   STRING; 176279.SERP0918; -.
DR   PRIDE; Q5HPJ3; -.
DR   EnsemblBacteria; AAW54293; AAW54293; SERP0918.
DR   GeneID; 50018844; -.
DR   KEGG; ser:SERP0918; -.
DR   eggNOG; COG0419; Bacteria.
DR   HOGENOM; CLU_004785_2_1_9; -.
DR   OMA; ISHVQEM; -.
DR   OrthoDB; 1143316at2; -.
DR   Proteomes; UP000000531; 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; Reference proteome.
FT   CHAIN           1..1009
FT                   /note="Nuclease SbcCD subunit C"
FT                   /id="PRO_0000338475"
FT   COILED          397..499
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;  118668 MW;  FB81A7452336EE20 CRC64;
     MKPLHIVMEN FGPFIKETID FEQVETDQLF LISGKTGSGK TMIFDAIVYA LYGMASTKTR
     KEGDLRSHFA DGKSPMSVIY QFKVNNQTFK IHREAPFIKE GNITKTQAKL NIYELVDNQF
     ELRESKVNQG NQFIVQLLGV NAEQFRQLFI LPQGEFKKFL QSNSKDKQSI LRTLFNSERF
     DEIRHLLVEN VKQEKVQIEN RYTQIENLWN DIDTFNNDEL ALYKELESSQ TDKMIEKFPQ
     FNDYGCKILK SFEEAKNKIT KELDDLNHKY KVNVELSENT KKLKAEKIKF DDLKKEQNYI
     DKLKQELKMI QESKVLITYF TRLQSLKKDK DELVSLHEQS KLNETNYHNE IKGFQKQLEH
     LSTRENEITQ FNQYLEKNQV FFNQLDKIIS SYQQKPVIEE EIKRLYSEYN DLITKKEELT
     KEMNNKNKDF AIIEHYTEEI YKLKKIIDES ERQKKDEKLF DKLQLDKSSY LSKLKEKKEQ
     LNEIESSITN IDATLIDLND KKDFVNEIKS AMSIGDTCPI CGNEIHSLGE HIDFESIAQK
     NNKIKRLESK KVKIRDEIIK IETRIEELNH RENELNFEKQ EKKDISELQK QLNHLNQLKD
     EQQSINKLVE NFEKQEKEIV NKIHQFDLDL SRKNTQKEKL EIQINDFERH SQFSSVNDFE
     TYYSHAKKQV ETYEYENEKT KDKLNELNNK LKIEMNDQKH LTENLTQTSK EINNLELKME
     KEMQQLGFES YDQVKSAADL SAQKDEIERE INIYNKNYQS YEIEINRLKE LVKGKKLLNL
     EELRQSIEKT NLKLDETNSQ IATISYKIDN NSNKFNKIKN IIQILDDELK VQKEIFLLSE
     ILAGKNDYKL TLENYVLIYY LEKIIFQANQ RLSFMSGNRY QLIRREAISL GLSGLEIDVF
     DFHSNKSRHI SSLSGGETFQ ASLALALGLS EVVQQESGGI TLDSMFIDEG FGTLDQETLE
     TAIDTLINLK SSGRMVGIIS HVSELKQRIP LILEVTSNQY ESHTQFRKN