ID   PH_STAA8                Reviewed;         484 AA.
AC   Q2FYD8;
DT   12-SEP-2018, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=Probable autolysin PH {ECO:0000305};
DE            EC=3.5.1.28 {ECO:0000269|PubMed:25690309};
GN   OrderedLocusNames=SAOUHSC_01515 {ECO:0000312|EMBL:ABD30597.1};
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   FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=ATCC 35556 / SA113;
RX   PubMed=25690309; DOI=10.1007/s00253-015-6443-2;
RA   Osipovitch D.C., Therrien S., Griswold K.E.;
RT   "Discovery of novel S. aureus autolysins and molecular engineering to
RT   enhance bacteriolytic activity.";
RL   Appl. Microbiol. Biotechnol. 99:6315-6326(2015).
CC   -!- FUNCTION: Has weak lytic activity toward S.aureus cells. Full-length
CC       protein has no activity, but fusion of the Peptidase C51 domain to the
CC       lysostaphin SH3 cell wall binding domain yields an active chimeric
CC       enzyme, suggesting that PH may be functional.
CC       {ECO:0000269|PubMed:25690309}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolyzes the link between N-acetylmuramoyl residues and L-
CC         amino acid residues in certain cell-wall glycopeptides.; EC=3.5.1.28;
CC         Evidence={ECO:0000269|PubMed:25690309};
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DR   EMBL; CP000253; ABD30597.1; -; Genomic_DNA.
DR   RefSeq; WP_000909202.1; NZ_LS483365.1.
DR   RefSeq; YP_500032.1; NC_007795.1.
DR   AlphaFoldDB; Q2FYD8; -.
DR   SMR; Q2FYD8; -.
DR   STRING; 1280.SAXN108_0369; -.
DR   MEROPS; C51.001; -.
DR   EnsemblBacteria; ABD30597; ABD30597; SAOUHSC_01515.
DR   GeneID; 3919056; -.
DR   KEGG; sao:SAOUHSC_01515; -.
DR   PATRIC; fig|93061.5.peg.1378; -.
DR   eggNOG; COG0860; Bacteria.
DR   eggNOG; COG1388; Bacteria.
DR   HOGENOM; CLU_046701_0_0_9; -.
DR   OMA; LMTKNQA; -.
DR   Proteomes; UP000008816; Chromosome.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IBA:GO_Central.
DR   GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IBA:GO_Central.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR   CDD; cd02696; MurNAc-LAA; 1.
DR   InterPro; IPR007921; CHAP_dom.
DR   InterPro; IPR002508; MurNAc-LAA_cat.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR003646; SH3-like_bac-type.
DR   Pfam; PF01520; Amidase_3; 1.
DR   Pfam; PF05257; CHAP; 1.
DR   Pfam; PF08460; SH3_5; 1.
DR   SMART; SM00646; Ami_3; 1.
DR   SMART; SM00287; SH3b; 1.
DR   SUPFAM; SSF54001; SSF54001; 1.
DR   PROSITE; PS50911; CHAP; 1.
PE   1: Evidence at protein level;
KW   Antimicrobial; Bacteriolytic enzyme; Cell wall biogenesis/degradation;
KW   Hydrolase; Reference proteome.
FT   CHAIN           1..484
FT                   /note="Probable autolysin PH"
FT                   /id="PRO_0000445039"
FT   DOMAIN          5..148
FT                   /note="Peptidase C51"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00048"
FT   DOMAIN          181..363
FT                   /note="MurNAc-LAA"
FT                   /evidence="ECO:0000305|PubMed:25690309"
FT   DOMAIN          402..472
FT                   /note="SH3b"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01117"
SQ   SEQUENCE   484 AA;  53830 MW;  53E38D36789BE8C1 CRC64;
     MLITKNQAEK WFDNSLGKQF NPDLFYGFQC YDYANMFFMI ATGERLQGLY AYNIPFDNKA
     RIEKYGQIIK NYDSFLPQKL DIVVFPSKYG GGAGHVEIVE SANLNTFTSF GQNWNGKGWT
     NGVAQPGWGP ETVTRHVHYY DDPMYFIRLN FPDKVSVGDK AKSVIKQATA KKQAVIKPKK
     IMLVAGHGYN DPGAVGNGTN ERDFIRKYIT PNIAKYLRHA GHEVALYGGS SQSQDMYQDT
     AYGVNVGNNK DYGLYWVKSH GYDIVLEIHL DAAGESASGG HVIISSQFNA DTIDKSIQDV
     IKNNLGQIRG VTPRNDLLNV NVSAEININY RLSELGFITN KNDMDWIKKN YDLYSKLIAG
     AIHGKPIGGL VAGNVKTSAK NQKNPPVPAG YTLDKNNVPY KKETGYYTVA NVKGNNVRDG
     YSTNSRITGV LPNNATIKYD GAYCINGYRW ITYIANSGQR RYIATGEVDK AGNRISSFGK
     FSTI