ID   SCED_STAEQ              Reviewed;         219 AA.
AC   Q5HMC6;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Probable transglycosylase SceD;
DE            EC=3.2.-.-;
DE   Flags: Precursor;
GN   Name=sceD; OrderedLocusNames=SERP1702;
OS   Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176279;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35984 / RP62A;
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).
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   -!- SIMILARITY: Belongs to the transglycosylase family. SceD subfamily.
CC       {ECO:0000305}.
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DR   EMBL; CP000029; AAW55080.1; -; Genomic_DNA.
DR   RefSeq; WP_001829904.1; NC_002976.3.
DR   AlphaFoldDB; Q5HMC6; -.
DR   SMR; Q5HMC6; -.
DR   STRING; 176279.SERP1702; -.
DR   EnsemblBacteria; AAW55080; AAW55080; SERP1702.
DR   GeneID; 50018206; -.
DR   KEGG; ser:SERP1702; -.
DR   eggNOG; COG1388; Bacteria.
DR   HOGENOM; CLU_099865_0_0_9; -.
DR   OMA; AGPSQWV; -.
DR   OrthoDB; 1172354at2; -.
DR   Proteomes; UP000000531; 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; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..219
FT                   /note="Probable transglycosylase SceD"
FT                   /id="PRO_0000320318"
FT   REGION          86..143
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   219 AA;  23056 MW;  7BCCEF11B838E78C CRC64;
     MKKTLVASSL AIGLGVVAGN AGHDAHASET TNVDKAELAQ KALTNDQSLN ESPVQEGAYN
     INFDYNGNSY HFESDGSTWS WSYESTNNAT QPVQPSQSQV ATQQQPVQVS APQNEQTAQP
     QTKSTSTSQT SSSKASSGSS VNVNSHLQQI AQRESGGDIH AINPSSGAAG KYQFLQSTWD
     SVAPSQYKGV SPAKAPESVQ DRAAVKLYNT GGPGHWVTA