ID   P73670_SYNY3            Unreviewed;       430 AA.
AC   P73670;
DT   01-FEB-1997, integrated into UniProtKB/TrEMBL.
DT   01-FEB-1997, sequence version 1.
DT   02-SEP-2026, entry version 133.
DE   RecName: Full=Pitrilysin {ECO:0000256|PROSITE-ProRule:PRU10096};
DE            EC=3.4.24.55 {ECO:0000256|PROSITE-ProRule:PRU10096};
GN   OrderedLocusNames=sll2008 {ECO:0000313|EMBL:BAA17715.1};
OS   Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa).
OC   Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC   Merismopediaceae; Synechocystis.
OX   NCBI_TaxID=1111708 {ECO:0000313|EMBL:BAA17715.1, ECO:0000313|Proteomes:UP000001425};
RN   [1] {ECO:0000313|EMBL:BAA17715.1, ECO:0000313|Proteomes:UP000001425}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27184 / PCC 6803 / Kazusa
RC   {ECO:0000313|Proteomes:UP000001425};
RX   PubMed=8590279; DOI=10.1093/dnares/2.4.153;
RA   Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N.,
RA   Sugiura M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region
RT   from map positions 64% to 92% of the genome.";
RL   DNA Res. 2:153-166(1995).
RN   [2] {ECO:0000313|EMBL:BAA17715.1, ECO:0000313|Proteomes:UP000001425}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27184 / PCC 6803 / Kazusa
RC   {ECO:0000313|Proteomes:UP000001425};
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Preferential cleavage of 16-Tyr-|-Leu-17 and 25-Phe-|-Tyr-26
CC         bonds of oxidized insulin B chain. Also acts on other substrates of
CC         Mw less than 7 kDa such as insulin and glucagon.; EC=3.4.24.55;
CC         Evidence={ECO:0000256|PROSITE-ProRule:PRU10096};
CC   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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DR   EMBL; BA000022; BAA17715.1; -; Genomic_DNA.
DR   PIR; S77157; S77157.
DR   AlphaFoldDB; P73670; -.
DR   STRING; 1148.gene:10498582; -.
DR   PaxDb; 1148-gene:10498582; -.
DR   EnsemblBacteria; BAA17715; BAA17715; BAA17715.
DR   KEGG; syn:sll2008; -.
DR   eggNOG; COG0612; Bacteria.
DR   InParanoid; P73670; -.
DR   PhylomeDB; P73670; -.
DR   Proteomes; UP000001425; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 2.
DR   InterPro; IPR011249; Metalloenz_LuxS/M16.
DR   InterPro; IPR050361; MPP/UQCRC_Complex.
DR   InterPro; IPR011765; Pept_M16_N.
DR   InterPro; IPR001431; Pept_M16_Zn_BS.
DR   InterPro; IPR007863; Peptidase_M16_C.
DR   PANTHER; PTHR11851; METALLOPROTEASE; 1.
DR   PANTHER; PTHR11851:SF49; MITOCHONDRIAL-PROCESSING PEPTIDASE SUBUNIT ALPHA; 1.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 1.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
DR   PROSITE; PS00143; INSULINASE; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:BAA17715.1};
KW   Protease {ECO:0000313|EMBL:BAA17715.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001425}.
FT   DOMAIN          33..175
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          183..362
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   ACT_SITE        66
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10096"
FT   BINDING         63
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10096"
FT   BINDING         67
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10096"
SQ   SEQUENCE   430 AA;  47977 MW;  4C888D30B9A40C38 CRC64;
     MDIRLVSVQL CPTKPDFPAK IFTFDQGLTL IHQDVPTVPV AVVDVWVRAG AIAEPDAWPG
     VAHLLEHMIF KGTKRVPPGA FDQVIEYNGG MANAATSHDY AHFYLTTAAD YLPRTLPYLA
     EILLQAEVPE ECLFYEREVV LEEIRGSEDD PDWLGFQALC QLLHPQHAYG RSVLGDAPSV
     QNYTANQLRC FHRTHYQPEN MTVVMVGDIR EKAAIAYMEE IFDHFGVRSE CPPTTRLPNH
     PIQTIKRETL RIPELGPSRL TMGWNGPGID RLQDNIGLDL LAVVLAGSHC ARLVQRLREE
     LGLVFDIQSC FSLQKEASLF TINAYLTSAQ AERVEAEICA AIQTLQTTPI STAELARAQR
     LLCNDFIFST ETPAQLAGLY GYYQTLATAE LAIAYPQIVR QYWPEALQTL AQRYLSTGAY
     ALVLLEAAES
//