ID   SCED_STAAR              Reviewed;         231 AA.
AC   Q6GEX9;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=Probable transglycosylase SceD;
DE            EC=3.2.-.-;
DE   Flags: Precursor;
GN   Name=sceD; OrderedLocusNames=SAR2184;
OS   Staphylococcus aureus (strain MRSA252).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282458;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MRSA252;
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; BX571856; CAG41165.1; -; Genomic_DNA.
DR   RefSeq; WP_000752015.1; NC_002952.2.
DR   AlphaFoldDB; Q6GEX9; -.
DR   SMR; Q6GEX9; -.
DR   KEGG; sar:SAR2184; -.
DR   HOGENOM; CLU_099865_0_0_9; -.
DR   OMA; AGPSQWV; -.
DR   OrthoDB; 1172354at2; -.
DR   Proteomes; UP000000596; Chromosome.
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_0000320315"
FT   REGION          92..153
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   231 AA;  24087 MW;  0658E321C1F71970 CRC64;
     MKKTLLASSL AVGLGIVAGN AGHEAQASEA DLNKASLAQM AQSNDQTLNQ KPIEAGAYNY
     TFDYEGFTYH FESDGTHFAW NYHATGANGA DMSAQAPATN NVAPSADQSN QVQSQEVEAP
     QNAQTQQPQA STSNNSQVTA TPTESKASEG SSVNVNDHLK QIAQRESGGN IHAVNPTSGA
     AGKYQFLQST WDSVAPAKYK GVSPANAPES VQDAAAVKLY NTGGAGHWVT A