ID ALP_LECPS Reviewed; 382 AA.
AC Q68GV9;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE RecName: Full=Alkaline serine protease ver112;
DE EC=3.4.21.-;
DE Flags: Precursor;
OS Lecanicillium psalliotae (Verticillium psalliotae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Lecanicillium.
OX NCBI_TaxID=73499;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAU01968.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=YMF1.00112 {ECO:0000312|EMBL:AAU01968.1};
RA Yang J.-K., Huang X.-W., Tian B.-Y., Zhang K.-Q.;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 103-112, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBCELLULAR LOCATION.
RX PubMed=16132863; DOI=10.1007/s10529-005-8461-0;
RA Yang J.-K., Huang X.-W., Tian B.-Y., Wang M., Niu Q.-H., Zhang K.-Q.;
RT "Isolation and characterization of a serine protease from the Nematophagous
RT Fungus, Lecanicillium psalliotae, displaying nematicidal activity.";
RL Biotechnol. Lett. 27:1123-1128(2005).
CC -!- FUNCTION: Serine protease which can degrade the nematode cuticle.
CC {ECO:0000269|PubMed:16132863}.
CC -!- ACTIVITY REGULATION: Inhibited by phenylmethylsulfonyl fluoride (PMSF).
CC {ECO:0000269|PubMed:16132863}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 9-10. {ECO:0000269|PubMed:16132863};
CC Temperature dependence:
CC Optimum temperature is 60-70 degrees Celsius.
CC {ECO:0000269|PubMed:16132863};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16132863}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000255}.
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DR EMBL; AY692148; AAU01968.1; -; Genomic_DNA.
DR PDB; 3F7M; X-ray; 1.60 A; A=104-382.
DR PDBsum; 3F7M; -.
DR AlphaFoldDB; Q68GV9; -.
DR SMR; Q68GV9; -.
DR MEROPS; S08.056; -.
DR EvolutionaryTrace; Q68GV9; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04077; Peptidases_S8_PCSK9_ProteinaseK_like; 1.
DR Gene3D; 3.30.70.80; Peptidase S8 propeptide/proteinase inhibitor I9; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR034193; PCSK9_ProteinaseK-like.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR010259; S8pro/Inhibitor_I9.
DR InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR PANTHER; PTHR43806:SF69; PROTEINASE T; 1.
DR Pfam; PF05922; Inhibitor_I9; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Hydrolase;
KW Protease; Secreted; Serine protease; Signal; Zymogen.
FT SIGNAL 1..15
FT /evidence="ECO:0000255"
FT PROPEP 16..102
FT /evidence="ECO:0000269|PubMed:16132863"
FT /id="PRO_0000026988"
FT CHAIN 103..382
FT /note="Alkaline serine protease ver112"
FT /evidence="ECO:0000269|PubMed:16132863"
FT /id="PRO_0000026989"
FT DOMAIN 56..99
FT /note="Inhibitor I9"
FT /evidence="ECO:0000255"
FT DOMAIN 111..382
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 143
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 173
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 328
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT DISULFID 138..227
FT /evidence="ECO:0000250|UniProtKB:P06873"
FT DISULFID 282..353
FT /evidence="ECO:0000250|UniProtKB:P06873"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:3F7M"
FT HELIX 112..117
FT /evidence="ECO:0007829|PDB:3F7M"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:3F7M"
FT STRAND 126..129
FT /evidence="ECO:0007829|PDB:3F7M"
FT TURN 131..136
FT /evidence="ECO:0007829|PDB:3F7M"
FT STRAND 137..144
FT /evidence="ECO:0007829|PDB:3F7M"
FT HELIX 151..153
FT /evidence="ECO:0007829|PDB:3F7M"
FT STRAND 157..162
FT /evidence="ECO:0007829|PDB:3F7M"
FT STRAND 164..168
FT /evidence="ECO:0007829|PDB:3F7M"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:3F7M"
FT HELIX 173..182
FT /evidence="ECO:0007829|PDB:3F7M"
FT TURN 184..186
FT /evidence="ECO:0007829|PDB:3F7M"
FT STRAND 193..198
FT /evidence="ECO:0007829|PDB:3F7M"
FT HELIX 208..221
FT /evidence="ECO:0007829|PDB:3F7M"
FT HELIX 222..224
FT /evidence="ECO:0007829|PDB:3F7M"
FT STRAND 230..235
FT /evidence="ECO:0007829|PDB:3F7M"
FT HELIX 243..254
FT /evidence="ECO:0007829|PDB:3F7M"
FT STRAND 258..262
FT /evidence="ECO:0007829|PDB:3F7M"
FT STRAND 265..269
FT /evidence="ECO:0007829|PDB:3F7M"
FT HELIX 270..272
FT /evidence="ECO:0007829|PDB:3F7M"
FT TURN 275..277
FT /evidence="ECO:0007829|PDB:3F7M"
FT STRAND 281..287
FT /evidence="ECO:0007829|PDB:3F7M"
FT STRAND 291..293
FT /evidence="ECO:0007829|PDB:3F7M"
FT STRAND 305..308
FT /evidence="ECO:0007829|PDB:3F7M"
FT STRAND 310..315
FT /evidence="ECO:0007829|PDB:3F7M"
FT HELIX 317..319
FT /evidence="ECO:0007829|PDB:3F7M"
FT STRAND 321..324
FT /evidence="ECO:0007829|PDB:3F7M"
FT HELIX 327..344
FT /evidence="ECO:0007829|PDB:3F7M"
FT TURN 349..351
FT /evidence="ECO:0007829|PDB:3F7M"
FT HELIX 352..359
FT /evidence="ECO:0007829|PDB:3F7M"
FT STRAND 360..363
FT /evidence="ECO:0007829|PDB:3F7M"
SQ SEQUENCE 382 AA; 39717 MW; 8D23A86CDE60BF5C CRC64;
MRLSIIAAVL PLALAAPVAE PEIAPLIEAR GAQPIAGKYI VKLKDEAKFG IMNAKSKIPG
IERVYENVLN GFSATLSNEE LERLRRDPDV ESIEQDAIFS INAITQQQGA TWGLTRISHR
ARGSTAYAYD TSAGAGACVY VIDTGVEDTH PDFEGRAKQI KSYASTARDG HGHGTHCAGT
IGSKTWGVAK KVSIFGVKVL DDSGSGSLSN IVAGMDFVAS DRQSRNCPRR TVASMSLGGG
YSAALNQAAA RLQSSGVFVA VAAGNDNRDA ANTSPASEPT VCTVGATDSN DVRSTFSNYG
RVVDIFAPGT SITSTWIGGR TNTISGTSMA TPHIAGLAAY LFGLEGGSAG AMCGRIQTLS
TKNVLTSIPS GTVNYLAFNG AT
//
