ID   SCED_STAAC              Reviewed;         231 AA.
AC   Q5HEA4;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Probable transglycosylase SceD;
DE            EC=3.2.-.-;
DE   Flags: Precursor;
GN   Name=sceD; OrderedLocusNames=SACOL2088;
OS   Staphylococcus aureus (strain COL).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93062;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=COL;
RX   PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA   Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA   Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA   Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA   Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA   Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA   Fraser C.M.;
RT   "Insights on evolution of virulence and resistance from the complete genome
RT   analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT   a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT   strain.";
RL   J. Bacteriol. 187:2426-2438(2005).
RN   [2]
RP   PROTEIN SEQUENCE OF 28-37, SUBCELLULAR LOCATION, AND INDUCTION.
RX   PubMed=11681202;
RX   DOI=10.1002/1615-9861(200104)1:4<480::aid-prot480>3.0.co;2-o;
RA   Ziebandt A.-K., Weber H., Rudolph J., Schmid R., Hoeper D., Engelmann S.,
RA   Hecker M.;
RT   "Extracellular proteins of Staphylococcus aureus and the role of SarA and
RT   sigma B.";
RL   Proteomics 1:480-493(2001).
CC   -!- FUNCTION: Is able to cleave peptidoglycan and affects clumping and
CC       separation of bacterial cells. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:11681202}.
CC   -!- INDUCTION: Positively regulated by sigma B factor.
CC       {ECO:0000269|PubMed:11681202}.
CC   -!- SIMILARITY: Belongs to the transglycosylase family. SceD subfamily.
CC       {ECO:0000305}.
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DR   EMBL; CP000046; AAW37049.1; -; Genomic_DNA.
DR   RefSeq; WP_000752009.1; NC_002951.2.
DR   AlphaFoldDB; Q5HEA4; -.
DR   SMR; Q5HEA4; -.
DR   CAZy; GH23; Glycoside Hydrolase Family 23.
DR   EnsemblBacteria; AAW37049; AAW37049; SACOL2088.
DR   KEGG; sac:SACOL2088; -.
DR   HOGENOM; CLU_099865_0_0_9; -.
DR   OMA; AGPSQWV; -.
DR   Proteomes; UP000000530; 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   1: Evidence at protein level;
KW   Direct protein sequencing; Glycosidase; Hydrolase; Secreted; Signal.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000269|PubMed:11681202"
FT   CHAIN           28..231
FT                   /note="Probable transglycosylase SceD"
FT                   /id="PRO_0000320311"
FT   REGION          103..153
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   231 AA;  24096 MW;  799994ABC53AB002 CRC64;
     MKKTLLASSL AVGLGIVAGN AGHEAHASEA DLNKASLAQM AQSNDQTLNQ KPIEAGAYNY
     TFDYEGFTYH FESDGTHFAW NYHATGTNGA DMSAQAPTTN NVAPSAVQAN QVQSQEVEAP
     QNAQTQQPQA STSNNSQVTA TPTESKSSEG SSVNVNAHLK QIAQRESGGN IHAVNPTSGA
     AGKYQFLQST WDSVAPAKYK GVSPANAPES VQDAAAVKLY NTGGAGHWVT A