ID   SCED_STAAN              Reviewed;         231 AA.
AC   Q7A4F2;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=Probable transglycosylase SceD;
DE            EC=3.2.-.-;
DE   Flags: Precursor;
GN   Name=sceD; OrderedLocusNames=SA1898;
OS   Staphylococcus aureus (strain N315).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=158879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=N315;
RX   PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA   Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA   Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA   Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA   Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA   Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA   Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA   Hiramatsu K.;
RT   "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL   Lancet 357:1225-1240(2001).
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; BA000018; BAB43182.1; -; Genomic_DNA.
DR   PIR; E90002; E90002.
DR   RefSeq; WP_000752005.1; NC_002745.2.
DR   AlphaFoldDB; Q7A4F2; -.
DR   SMR; Q7A4F2; -.
DR   CAZy; GH23; Glycoside Hydrolase Family 23.
DR   EnsemblBacteria; BAB43182; BAB43182; BAB43182.
DR   KEGG; sau:SA1898; -.
DR   HOGENOM; CLU_099865_0_0_9; -.
DR   OMA; AGPSQWV; -.
DR   Proteomes; UP000000751; 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_0000320314"
FT   REGION          93..152
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   231 AA;  24077 MW;  D30E43170FE65583 CRC64;
     MKKTLLASSL AVGLGIVAGN AGHEAHASEA DLNKASLAQM AQSNDQTLNQ KPIEAGAYNY
     TFDYEGFTYH FESDGTHFAW NYHATGANGA NMSAQAPATN NVEPSAVQAN QVQSQEVEAP
     QNAQTQQPQA STSNNSQVTA TPTESKASEG SSVNVNAHLK QIAQRESGGN IHAVNPTSGA
     AGKYQFLQST WDSVAPAKYK GVSPANAPES VQDAAAVKLY NTGGAGHWVT A