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ISAA_STAAS
ID   ISAA_STAAS              Reviewed;         233 AA.
AC   Q6G6A5;
DT   21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=Probable transglycosylase IsaA;
DE            EC=3.2.-.-;
DE   AltName: Full=Immunodominant staphylococcal antigen A;
DE   Flags: Precursor;
GN   Name=isaA; OrderedLocusNames=SAS2455;
OS   Staphylococcus aureus (strain MSSA476).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282459;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MSSA476;
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; BX571857; CAG44271.1; -; Genomic_DNA.
DR   RefSeq; WP_000751267.1; NC_002953.3.
DR   AlphaFoldDB; Q6G6A5; -.
DR   SMR; Q6G6A5; -.
DR   KEGG; sas:SAS2455; -.
DR   HOGENOM; CLU_099865_0_0_9; -.
DR   OMA; MWNTIVM; -.
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_0000021529"
SQ   SEQUENCE   233 AA;  24203 MW;  A76C4C225D17DEB2 CRC64;
     MKKTIMASSL AVALGVTGYA AGTGHQAHAA EVNVDQAHLV DLAHNHQDQL NAAPIKDGAY
     DIHFVKDGFQ YNFTSNGTTW SWSYEAANGQ TAGFSNVAGA DYTTSYNQGS NVQSVSYNAQ
     SSNSNVEAVS APTYHNYSTS TTSSSVRLSN GNTAGATGSS AAQIMAQRTG VSASTWAAII
     ARESNGQVNA YNPSGASGLF QTMPGWGPTN TVDQQINAAV KAYKAQGLGA WGF
 
 
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