ID   SCED_STAAS              Reviewed;         231 AA.
AC   Q6G7L4;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=Probable transglycosylase SceD;
DE            EC=3.2.-.-;
DE   Flags: Precursor;
GN   Name=sceD; OrderedLocusNames=SAS1999;
OS   Staphylococcus aureus (strain MSSA476).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282459;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MSSA476;
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA   Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA   Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA   Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA   Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT   for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
CC   -!- FUNCTION: Is able to cleave peptidoglycan and affects clumping and
CC       separation of bacterial cells. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- INDUCTION: Positively regulated by sigma B factor. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the transglycosylase family. SceD subfamily.
CC       {ECO:0000305}.
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DR   EMBL; BX571857; CAG43807.1; -; Genomic_DNA.
DR   RefSeq; WP_000752008.1; NC_002953.3.
DR   AlphaFoldDB; Q6G7L4; -.
DR   SMR; Q6G7L4; -.
DR   KEGG; sas:SAS1999; -.
DR   HOGENOM; CLU_099865_0_0_9; -.
DR   OMA; AGPSQWV; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd13925; RPF; 1.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   InterPro; IPR010618; RPF.
DR   Pfam; PF06737; Transglycosylas; 1.
DR   SUPFAM; SSF53955; SSF53955; 1.
PE   3: Inferred from homology;
KW   Glycosidase; Hydrolase; Secreted; Signal.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..231
FT                   /note="Probable transglycosylase SceD"
FT                   /id="PRO_0000320316"
FT   REGION          106..153
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   231 AA;  24066 MW;  389994BBC436C11E CRC64;
     MKKTLLASSL AVGLGIVAGN AGHEAHASEA DLNKASLAQM AQSNDQTLNQ KPIEAGAYNY
     TFDYEGFTYH FESDGTHFAW NYHATGTNGA DMSAQAPATN NVAPSAVQAN QVQSQEVEAP
     QNAQTQQPQA STSNNSQVTA TPTESKSSEG SSVNVNAHLK QIAQRESGGN IHAVNPTSGA
     AGKYQFLQST WDSVAPAKYK GVSPANAPES VQDAAAVKLY NTGGAGHWVT A