ID   SBCD_STAS1              Reviewed;         376 AA.
AC   Q49XE0;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=Nuclease SbcCD subunit D;
GN   Name=sbcD; OrderedLocusNames=SSP1412;
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 SbcD family. {ECO:0000305}.
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DR   EMBL; AP008934; BAE18557.1; -; Genomic_DNA.
DR   RefSeq; WP_011303184.1; NZ_MTGA01000038.1.
DR   AlphaFoldDB; Q49XE0; -.
DR   SMR; Q49XE0; -.
DR   STRING; 342451.SSP1412; -.
DR   EnsemblBacteria; BAE18557; BAE18557; SSP1412.
DR   KEGG; ssp:SSP1412; -.
DR   PATRIC; fig|342451.11.peg.1415; -.
DR   eggNOG; COG0420; Bacteria.
DR   HOGENOM; CLU_038045_0_1_9; -.
DR   OMA; TSGNHDS; -.
DR   OrthoDB; 1831911at2; -.
DR   Proteomes; UP000006371; Chromosome.
DR   GO; GO:0008408; F:3'-5' exonuclease activity; IEA:InterPro.
DR   GO; GO:0004519; F:endonuclease 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   CDD; cd00840; MPP_Mre11_N; 1.
DR   Gene3D; 3.60.21.10; -; 1.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR041796; Mre11_N.
DR   InterPro; IPR004593; SbcD.
DR   InterPro; IPR026843; SbcD_C.
DR   Pfam; PF00149; Metallophos; 1.
DR   Pfam; PF12320; SbcD_C; 1.
DR   SUPFAM; SSF56300; SSF56300; 1.
DR   TIGRFAMs; TIGR00619; sbcd; 1.
PE   3: Inferred from homology;
KW   DNA recombination; DNA replication; Endonuclease; Exonuclease; Hydrolase;
KW   Nuclease; Reference proteome.
FT   CHAIN           1..376
FT                   /note="Nuclease SbcCD subunit D"
FT                   /id="PRO_0000338495"
SQ   SEQUENCE   376 AA;  43708 MW;  9598FFE0357B8EA1 CRC64;
     MKIIHTADWH LGRILNGKSL LEDQAYILDK FIEAMKLEQP DVIVIAGDLY DTSYPNKDAI
     QLLEQTIDIL NLEMSIPLIM INGNHDSKER LNYGSKWFEK SHMYIRTDLN DMNKPVTIGN
     VDFYTMPFAT INEMQYFFDD KAIETHQQAL NRVLAYMHEV IDENKVNIFV GHLTVQGGIR
     SESERPLTIG TVESVDENLF NQFDRVMLGH LHHPFSIESN FINYSGSLLQ YSFSETKQPK
     GYKIVEIKNQ KITDKFIPLK PLRQLEVIEG NYEDAIQEKL EVKHKENYLH FKLKHMSHVS
     DPMMHLKQIY PNTLALTNQT FDFNTSIHHE NIEIQKLDDE TIIDNFYNSI TGEHLTTNQS
     KKIEKIMTAL LEEGSK