ID   THEM_MALCI              Reviewed;          34 AA.
AC   P13858;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Thermomycolin;
DE            EC=3.4.21.65;
DE   AltName: Full=Thermomycolase;
DE   Flags: Fragments;
OS   Malbranchea cinnamomea (Thermophilic fungus) (Malbranchea sulfurea).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Malbranchea.
OX   NCBI_TaxID=5041;
RN   [1]
RP   PROTEIN SEQUENCE, AND ACTIVE SITE.
RX   PubMed=1012007;
RA   Gaucher G.M., Stevenson K.J.;
RT   "Thermomycolin.";
RL   Methods Enzymol. 45:415-433(1976).
RN   [2]
RP   CHARACTERIZATION.
RX   PubMed=4429868; DOI=10.1139/o74-137;
RA   Voordouw G., Gaucher G.M., Roche R.S.;
RT   "Physiochemical properties of thermomycolase, the thermostable,
RT   extracellular, serine protease of the fungus Malbranchea pulchella.";
RL   Can. J. Biochem. 52:981-990(1974).
RN   [3]
RP   CHARACTERIZATION.
RX   PubMed=3173; DOI=10.1042/bj1510527;
RA   Stevenson K.J., Gaucher G.M.;
RT   "The substrate specificity of thermomycolase, an extracellular serine
RT   proteinase from the thermophilic fungus Malbranchea pulchella var.
RT   sulfurea.";
RL   Biochem. J. 151:527-542(1975).
CC   -!- FUNCTION: This is an extracellular proteinase with a general
CC       specificity for apolar residues.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Rather non-specific hydrolysis of proteins. Preferential
CC         cleavage: -Ala-|-Xaa-, -Tyr-|-Xaa-, -Phe-|-Xaa- in small molecular
CC         substrates.; EC=3.4.21.65;
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Temperature dependence:
CC         Thermostable.;
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR   PIR; A24174; A24174.
DR   AlphaFoldDB; P13858; -.
DR   SMR; P13858; -.
DR   MEROPS; S08.057; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrolase; Protease; Secreted; Serine protease.
FT   CHAIN           1..>34
FT                   /note="Thermomycolin"
FT                   /id="PRO_0000076420"
FT   ACT_SITE        33
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10080,
FT                   ECO:0000255|PROSITE-ProRule:PRU10081, ECO:0000255|PROSITE-
FT                   ProRule:PRU10082, ECO:0000269|PubMed:1012007"
FT   UNSURE          6
FT   UNSURE          10
FT   UNSURE          17
FT   UNSURE          31
FT   NON_CONS        28..29
FT                   /evidence="ECO:0000305"
FT   NON_TER         34
SQ   SEQUENCE   34 AA;  3708 MW;  147F90B412F014E6 CRC64;
     ALVTQSNAPS WGLGRISNRQ AGIRDYHYLS GTSM