ID   SP1_RARFA               Reviewed;         525 AA.
AC   Q05308;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Serine protease 1;
DE            EC=3.4.21.-;
DE   AltName: Full=Serine protease I;
DE            Short=RPI;
DE   Flags: Precursor;
OS   Rarobacter faecitabidus.
OC   Bacteria; Actinobacteria; Micrococcales; Rarobacteraceae; Rarobacter.
OX   NCBI_TaxID=13243;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 212-222; 224-238
RP   AND 240-244.
RC   STRAIN=YLM-50;
RX   PubMed=1339445; DOI=10.1016/s0021-9258(19)74023-x;
RA   Shimoi H., Iimura Y., Obata T., Tadenuma M.;
RT   "Molecular structure of Rarobacter faecitabidus protease I. A yeast-lytic
RT   serine protease having mannose-binding activity.";
RL   J. Biol. Chem. 267:25189-25195(1992).
RN   [2]
RP   PROTEIN SEQUENCE OF 212-247.
RX   PubMed=1778983; DOI=10.1093/oxfordjournals.jbchem.a123628;
RA   Shimoi H., Tadenuma M.;
RT   "Characterization of Rarobacter faecitabidus protease I, a yeast-lytic
RT   serine protease having mannose-binding activity.";
RL   J. Biochem. 110:608-613(1991).
CC   -!- FUNCTION: Major serine protease exhibiting lytic activity toward living
CC       yeast cells. Similar to elastase in its substrate specificity and has a
CC       lectin-like affinity for mannose. Mannoproteins may be the native
CC       substrate for RPI.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000305}.
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DR   EMBL; D10753; BAA01585.1; -; Genomic_DNA.
DR   PIR; A45053; A45053.
DR   AlphaFoldDB; Q05308; -.
DR   SMR; Q05308; -.
DR   CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR   MEROPS; S01.276; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005537; F:mannose binding; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00161; RICIN; 1.
DR   Gene3D; 2.40.10.10; -; 2.
DR   Gene3D; 3.30.300.50; -; 2.
DR   InterPro; IPR004236; Pept_S1_alpha_lytic.
DR   InterPro; IPR001316; Pept_S1A_streptogrisin.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR035992; Ricin_B-like_lectins.
DR   InterPro; IPR000772; Ricin_B_lectin.
DR   InterPro; IPR035070; Streptogrisin_prodomain.
DR   Pfam; PF02983; Pro_Al_protease; 1.
DR   Pfam; PF00652; Ricin_B_lectin; 1.
DR   PRINTS; PR00861; ALYTICPTASE.
DR   SMART; SM00458; RICIN; 1.
DR   SUPFAM; SSF50370; SSF50370; 1.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   PROSITE; PS50231; RICIN_B_LECTIN; 1.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Hydrolase; Lectin;
KW   Mannose-binding; Protease; Secreted; Serine protease; Signal; Zymogen.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000255"
FT   PROPEP          33..211
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000026919"
FT   CHAIN           212..525
FT                   /note="Serine protease 1"
FT                   /id="PRO_0000026920"
FT   DOMAIN          396..525
FT                   /note="Ricin B-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT   REGION          401..525
FT                   /note="Essential for the lytic activity, but not for
FT                   protease function"
FT   ACT_SITE        238
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        270
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        352
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   DISULFID        223..239
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT   DISULFID        310..320
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT   DISULFID        346..376
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT   DISULFID        412..431
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT   DISULFID        453..472
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT   DISULFID        496..514
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
SQ   SEQUENCE   525 AA;  55654 MW;  DA2BCF7D330EBB61 CRC64;
     MKCKKPSALF SALALVGALG AASVLGAASA NSASPVAAAT VQASSGSAKT SVAATSKSQD
     GDVLAAIVRD LKITKTQAKK RIKLEEKARQ LEPRLQKKLG KKFAGLWISK NGKKIVVGVT
     TKKAAKVVKK AGATPKIVKS NLTTLKKRAT KISKNAPSDI KNVNSWWVDP ATNKVVIEAR
     SKKAAKAAAT AAGLTAGTYE ITVSDDVIVP VRDYWGGDAL SGCTLAFPVY GGFLTAGHCA
     VEGKGHILKT EMTGGQIGTV EASQFGDGID AAWAKNYGDW NGRGRVTHWN GGGGVDIKGS
     NEAAVGAHMC KSGRTTKWTC GYLLRKDVSV NYGNGHIVTL NETSACALGG DSGGAYVWND
     QAQGITSGSN MDTNNCRSFY QPVNTVLNKW KLSLVTSTDV TTSYVQGYQN NCIDVPNSDF
     TDGKQLQVWN CNGTNAQKVS FHPDGTLRIN GKCLDARWAW THNGTEVQLM NCNGHIAQKF
     TLNGAGDLVN VHANKCVDVK DWGGQGGKLQ LWECSGGANQ KWWRR