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SBCD_STAAE
ID   SBCD_STAAE              Reviewed;         373 AA.
AC   A6QGP7;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Nuclease SbcCD subunit D;
GN   Name=sbcD; OrderedLocusNames=NWMN_1257;
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 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 SbcD family. {ECO:0000305}.
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DR   EMBL; AP009351; BAF67529.1; -; Genomic_DNA.
DR   RefSeq; WP_000691284.1; NZ_CP023390.1.
DR   AlphaFoldDB; A6QGP7; -.
DR   SMR; A6QGP7; -.
DR   EnsemblBacteria; BAF67529; BAF67529; NWMN_1257.
DR   KEGG; sae:NWMN_1257; -.
DR   HOGENOM; CLU_038045_0_1_9; -.
DR   OMA; TSGNHDS; -.
DR   Proteomes; UP000006386; 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: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   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   1: Evidence at protein level;
KW   DNA damage; DNA recombination; DNA repair; DNA replication; Endonuclease;
KW   Exonuclease; Hydrolase; Nuclease; SOS response.
FT   CHAIN           1..373
FT                   /note="Nuclease SbcCD subunit D"
FT                   /id="PRO_0000338489"
SQ   SEQUENCE   373 AA;  42936 MW;  2473F7EBD76CC5BE CRC64;
     MKIIHTADWH LGKILNGKQL LEDQAYILDM FVEKMKEEEP DIIVIAGDLY DTTYPSKDAI
     MLLEQAIGKL NLELRIPIII ISGNHDGKER LNYGASWFEH NQLFIRTDFT SINSPIEING
     VNFYTLPYAT VSEMKHYFED DTIETHQQGI TRCIETIAPE IDEDAVNILI SHLTVQGGKT
     SDSERPLTIG TVESVQKGVF DIFDYVMLGH LHHPFSIEDD KIKYSGSLLQ YSFSEAGQAK
     GYRRVTINDG IINDVFIPLK PLRQLEIISG EYNDVINEKV HVKNKDNYLH FKLKNMSHIT
     DPMMSLKQIY PNTLALTNET FNYNEENNAI EISEKDDMSI IEMFYKHITD KELSDIQSKK
     IKNILENELR KED
 
 
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