ID   ISAA_STAAR              Reviewed;         233 AA.
AC   Q6GDN1;
DT   21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Probable transglycosylase IsaA;
DE            EC=3.2.-.-;
DE   AltName: Full=Immunodominant staphylococcal antigen A;
DE   Flags: Precursor;
GN   Name=isaA; OrderedLocusNames=SAR2650;
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. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the transglycosylase family. IsaA subfamily.
CC       {ECO:0000305}.
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DR   EMBL; BX571856; CAG41627.1; -; Genomic_DNA.
DR   RefSeq; WP_000751265.1; NC_002952.2.
DR   AlphaFoldDB; Q6GDN1; -.
DR   KEGG; sar:SAR2650; -.
DR   HOGENOM; CLU_099865_0_0_9; -.
DR   OMA; MWNTIVM; -.
DR   OrthoDB; 1574792at2; -.
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   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   InterPro; IPR008258; Transglycosylase_SLT_dom_1.
DR   Pfam; PF01464; SLT; 1.
DR   SUPFAM; SSF53955; SSF53955; 1.
PE   3: Inferred from homology;
KW   Glycosidase; Hydrolase; Secreted; Signal.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000250"
FT   CHAIN           30..233
FT                   /note="Probable transglycosylase IsaA"
FT                   /id="PRO_0000021528"
SQ   SEQUENCE   233 AA;  24213 MW;  A5BE9C225D14DDB2 CRC64;
     MKKTIMASSL AVALGVTGYA AGTGHQAHAA EVNVDQAHLV DLAHNHQDQL NAAPIKDGAY
     DIHFVKDGFQ YNFTSNGTTW SWSYEAANGQ TAGFSNVAGA DYTTSYNQGS NVQSVSYNAQ
     SSNSNVEAVS APTYHNYSTS TTSSSVRLSN GNTAGATGSS AAQIMAQRTG VPASTWAAII
     ARESNGQVNA YNPSGASGLF QTMPGWGPTN TVDQQINAAV KAYKAQGLGA WGF