ID   SBCC_STAS1              Reviewed;        1009 AA.
AC   Q49XE1;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Nuclease SbcCD subunit C;
GN   Name=sbcC; OrderedLocusNames=SSP1411;
OS   Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM
OS   20229 / NCIMB 8711 / NCTC 7292 / S-41).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=342451;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41;
RX   PubMed=16135568; DOI=10.1073/pnas.0502950102;
RA   Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K., Higashide M.,
RA   Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S., Hattori M., Ohta T.;
RT   "Whole genome sequence of Staphylococcus saprophyticus reveals the
RT   pathogenesis of uncomplicated urinary tract infection.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AP008934; BAE18556.1; -; Genomic_DNA.
DR   RefSeq; WP_011303183.1; NZ_MTGA01000038.1.
DR   AlphaFoldDB; Q49XE1; -.
DR   SMR; Q49XE1; -.
DR   STRING; 342451.SSP1411; -.
DR   PRIDE; Q49XE1; -.
DR   EnsemblBacteria; BAE18556; BAE18556; SSP1411.
DR   KEGG; ssp:SSP1411; -.
DR   PATRIC; fig|342451.11.peg.1414; -.
DR   eggNOG; COG0419; Bacteria.
DR   HOGENOM; CLU_004785_2_1_9; -.
DR   OMA; ISHVQEM; -.
DR   OrthoDB; 1143316at2; -.
DR   Proteomes; UP000006371; 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_0000338477"
FT   COILED          178..214
FT                   /evidence="ECO:0000255"
FT   COILED          243..309
FT                   /evidence="ECO:0000255"
FT   COILED          337..503
FT                   /evidence="ECO:0000255"
FT   COILED          578..842
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;  117910 MW;  8BF12CBB03D635D6 CRC64;
     MRPIKLNLTN FGPFLNETID FNNVENNQLF LISGKTGSGK TMIFDAIVFA LFGEASTKDR
     KESDLRSHFA ESKKPMVVEF EFKLRNQYFK IQRQGAFIKE GNKNKTLGQL AVYQYEQDDY
     ALRESKINSG NQFIKALLGV NAEQFRQLFI LPQGEFKRFL LSKSVEKQDI LRTLFNSQRF
     EEIQKKLSDD VKEVREQIEK RYNDLENHWK ELETFDDETL CEHKVISARQ TNNIIKVLPD
     FKMKAQIIRD DFEQKKEILK NKVNSTENAL NNNIKLEDAL NKLNENQQKY EALLVNENEI
     QEKVKRVTEI NEVRPITNLL EVKENTISKK GKVAQSIEEK SKSIFDLEDK IKQSNLEADN
     LKEKQDDIEE LRRFIEQTQL FFEKANKYKD AYNNYQFTKT AFTDLEAHLT QKNEEIKDTT
     AKLNQRQPDY RKIEQITEAI YNLNNDIKQL KQNEKDKIEY DALEKRKMQK QRNLKDLSQK
     RVQLNEEYNN IDKSKLDLNN KQDVIATVQA ALHTGETCPI CGNEIHTLSS HVDFDEIMER
     HQQLTLLEEK IATVKGDIIK CESELSHIEE QLSKYTIASL ENINYEALED EVEKKYQEKK
     KIDEENNEIE KLKDQLQQYE KSSHDLQMNI QKKEHILKEN ETAINDFENT TGYKRVDEFL
     TKFEDAYNQI RQFDQTLNEI EQKIQNYKST LAIEKNSVTY LKNNLAEIET EINETDMKIN
     EEMQRIGFTS IEQVEKVTAQ ASEKQNLEKE IETFKKEKQS YELYIAQLKA ETNNKKLDDT
     QQLKERFEEM QQVYETASTE LSQHDYKMEF NSKKITEINK IIDELNSELQ SQQEVFQLAE
     ILAGKNEQKL TLENYVLIYY LERILTQANQ RLAIMTGQRY QLTRRAQISQ GYSGLEIDVF
     DAHSNQSRHI TSLSGGETFQ ASLALALGLS EIVQQESGGI SLDSMFVDEG FGTLDQETLE
     TALDTLLSLK STGRMVGIIS HVSELKQRIP LILEVTTEQY QSTTHFKKQ