ID   ISAA_STAA8              Reviewed;         233 AA.
AC   Q2FV52;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=Probable transglycosylase IsaA;
DE            EC=3.2.-.-;
DE   AltName: Full=Immunodominant staphylococcal antigen A;
DE   Flags: Precursor;
GN   Name=isaA; OrderedLocusNames=SAOUHSC_02887;
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 30-45, 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).
RN   [3]
RP   INDUCTION.
RX   PubMed=15870358; DOI=10.1128/aem.71.5.2663-2676.2005;
RA   Resch A., Rosenstein R., Nerz C., Goetz F.;
RT   "Differential gene expression profiling of Staphylococcus aureus cultivated
RT   under biofilm and planktonic conditions.";
RL   Appl. Environ. Microbiol. 71:2663-2676(2005).
RN   [4]
RP   FUNCTION, CELL WALL HYDROLYTIC ACTIVITY, INDUCTION, AND DISRUPTION
RP   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).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND INDUCTION.
RC   STRAIN=RN4220;
RX   PubMed=20472795; DOI=10.1128/jb.01452-09;
RA   Sibbald M.J., Winter T., van der Kooi-Pol M.M., Buist G., Tsompanidou E.,
RA   Bosma T., Schafer T., Ohlsen K., Hecker M., Antelmann H., Engelmann S.,
RA   van Dijl J.M.;
RT   "Synthetic effects of secG and secY2 mutations on exoproteome biogenesis in
RT   Staphylococcus aureus.";
RL   J. Bacteriol. 192:3788-3800(2010).
CC   -!- FUNCTION: Is able to cleave peptidoglycan.
CC       {ECO:0000269|PubMed:17675373}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11681202,
CC       ECO:0000269|PubMed:20472795}.
CC   -!- INDUCTION: Increased expression in vivo during human sepsis. Highly
CC       expressed under biofilm conditions after 8 hours of growth. Positively
CC       regulated by SarA and the two-component system YycFG. Also positively
CC       regulated by the two-component sensor-regulator SrrAB under aerated
CC       conditions. More protein is secreted in a secG or double secG/secY2
CC       mutant (at protein level). {ECO:0000269|PubMed:11681202,
CC       ECO:0000269|PubMed:15870358, ECO:0000269|PubMed:17675373,
CC       ECO:0000269|PubMed:20472795}.
CC   -!- DISRUPTION PHENOTYPE: Up-regulation of ssaA and sceD. Its inactivation
CC       shows no clumping and results in an apparent increased degree of cell
CC       separation which could be due to the up-regulation of sceD.
CC       Inactivation of both isaA and sceD genes results in a high degree of
CC       clumping and the double mutant is also attenuated for virulence.
CC       {ECO:0000269|PubMed:17675373}.
CC   -!- SIMILARITY: Belongs to the transglycosylase family. IsaA subfamily.
CC       {ECO:0000305}.
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DR   EMBL; CP000253; ABD31883.1; -; Genomic_DNA.
DR   RefSeq; WP_000751267.1; NZ_LS483365.1.
DR   RefSeq; YP_501340.1; NC_007795.1.
DR   AlphaFoldDB; Q2FV52; -.
DR   SMR; Q2FV52; -.
DR   STRING; 1280.SAXN108_2819; -.
DR   EnsemblBacteria; ABD31883; ABD31883; SAOUHSC_02887.
DR   GeneID; 3921556; -.
DR   KEGG; sao:SAOUHSC_02887; -.
DR   PATRIC; fig|93061.5.peg.2609; -.
DR   eggNOG; COG0741; Bacteria.
DR   HOGENOM; CLU_099865_0_0_9; -.
DR   OMA; MWNTIVM; -.
DR   PRO; PR:Q2FV52; -.
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   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   InterPro; IPR008258; Transglycosylase_SLT_dom_1.
DR   Pfam; PF01464; SLT; 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..29
FT                   /evidence="ECO:0000269|PubMed:11681202"
FT   CHAIN           30..233
FT                   /note="Probable transglycosylase IsaA"
FT                   /id="PRO_0000272657"
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