ID   SCED_STAA8              Reviewed;         231 AA.
AC   Q2FWF8;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=Probable transglycosylase SceD;
DE            EC=3.2.-.-;
DE   Flags: Precursor;
GN   Name=sceD; OrderedLocusNames=SAOUHSC_02333;
OS   Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 8325 / PS 47;
RA   Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT   "The Staphylococcus aureus NCTC 8325 genome.";
RL   (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL   Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL   D.C. (2006).
RN   [2]
RP   PROTEIN SEQUENCE OF N-TERMINUS, CELL WALL HYDROLYTIC ACTIVITY, FUNCTION,
RP   INDUCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=17675373; DOI=10.1128/jb.00734-07;
RA   Stapleton M.R., Horsburgh M.J., Hayhurst E.J., Wright L., Jonsson I.-M.,
RA   Tarkowski A., Kokai-Kun J.F., Mond J.J., Foster S.J.;
RT   "Characterization of IsaA and SceD, two putative lytic transglycosylases of
RT   Staphylococcus aureus.";
RL   J. Bacteriol. 189:7316-7325(2007).
CC   -!- FUNCTION: Is able to cleave peptidoglycan and affects clumping and
CC       separation of bacterial cells. Is required for normal growth under
CC       stressful conditions. Is essential for nasal colonization.
CC       {ECO:0000269|PubMed:17675373}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- INDUCTION: Highest expression during the exponential phase. Expression
CC       is increased about 3-fold by inactivation of isaA. Up-regulated by the
CC       presence of NaCl in a IsaA independent manner. Seems to be negatively
CC       regulated by SarA. Negatively regulated by the two-component systems
CC       LytSR and SaeRS whereas is positively regulated by sigma-B factor, agr
CC       and the two-component system YycFG. {ECO:0000269|PubMed:17675373}.
CC   -!- DISRUPTION PHENOTYPE: Cells grow slightly less well than wild-type in
CC       the presence of 2.5 M NaCl. Inactivation of both isaA and sceD genes
CC       results in a high degree of clumping and the double mutant is also
CC       attenuated for virulence. {ECO:0000269|PubMed:17675373}.
CC   -!- SIMILARITY: Belongs to the transglycosylase family. SceD subfamily.
CC       {ECO:0000305}.
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DR   EMBL; CP000253; ABD31367.1; -; Genomic_DNA.
DR   RefSeq; WP_000752008.1; NZ_LS483365.1.
DR   RefSeq; YP_500812.1; NC_007795.1.
DR   AlphaFoldDB; Q2FWF8; -.
DR   SMR; Q2FWF8; -.
DR   STRING; 1280.SAXN108_2341; -.
DR   CAZy; GH23; Glycoside Hydrolase Family 23.
DR   EnsemblBacteria; ABD31367; ABD31367; SAOUHSC_02333.
DR   GeneID; 3920958; -.
DR   KEGG; sao:SAOUHSC_02333; -.
DR   PATRIC; fig|93061.5.peg.2114; -.
DR   eggNOG; COG1388; Bacteria.
DR   HOGENOM; CLU_099865_0_0_9; -.
DR   OMA; AGPSQWV; -.
DR   Proteomes; UP000008816; 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; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000250"
FT   CHAIN           28..231
FT                   /note="Probable transglycosylase SceD"
FT                   /id="PRO_0000320309"
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