ID   B8Y0M7_9CYAN            Unreviewed;       447 AA.
AC   B8Y0M7;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   SubName: Full=Subtilisin-like protease {ECO:0000313|EMBL:ACK37895.1};
DE   Flags: Fragment;
OS   Planktothrix sp. 28.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Oscillatoriales; Microcoleaceae; Planktothrix.
OX   NCBI_TaxID=283951 {ECO:0000313|EMBL:ACK37895.1};
RN   [1] {ECO:0000313|EMBL:ACK37895.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=28 {ECO:0000313|EMBL:ACK37895.1};
RX   PubMed=19047393; DOI=10.1128/AEM.02134-08;
RA   Leikoski N., Fewer D.P., Sivonen K.;
RT   "Widespread occurrence and lateral transfer of the cyanobactin biosynthesis
RT   gene cluster in cyanobacteria.";
RL   Appl. Environ. Microbiol. 75:853-857(2009).
CC   -!- SIMILARITY: Belongs to the peptidase S8 family.
CC       {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR   EMBL; FJ461740; ACK37895.1; -; Genomic_DNA.
DR   AlphaFoldDB; B8Y0M7; -.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR   InterPro; IPR040636; PatG_C.
DR   InterPro; IPR040483; PatG_dom.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR   InterPro; IPR023830; Peptidase_S8A_PatG.
DR   NCBIfam; TIGR03895; protease_PatA; 1.
DR   PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR   PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR   Pfam; PF18065; PatG_C; 1.
DR   Pfam; PF18047; PatG_D; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:ACK37895.1};
KW   Protease {ECO:0000313|EMBL:ACK37895.1}.
FT   DOMAIN          7..71
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   DOMAIN          190..302
FT                   /note="PatG"
FT                   /evidence="ECO:0000259|Pfam:PF18047"
FT   DOMAIN          348..447
FT                   /note="PatG C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18065"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ACK37895.1"
FT   NON_TER         447
FT                   /evidence="ECO:0000313|EMBL:ACK37895.1"
SQ   SEQUENCE   447 AA;  48623 MW;  3A3800205957EC7B CRC64;
     DAYQKQGILA PGKDILGAKP GGGTVKLSGT SFATPIVSGV AALLLSLQIK RGEKPDPQKV
     KTALLATATP CNPKDTDDQS RCLMGKLNIL DAIEYLTGET MSEDLELESV EASGCGCQDT
     QINESELDNQ LETASEIKPD EIVASVTTQT PINIPSFPQQ TTNQPTMSNR TSNFVTASEA
     PSELEGKNLV YALGVLGYDF GSEARRDSFK QLMPGVSIEG TTIPANPYDA RQMVDYLGEN
     LPEAKALIWT LNLELTPIYA IEPVGGFSRD VYEVLQGLLS GQIQEENSPE FVQRVSIPGV
     LTGRSVKLFS GQVVPVIEIN NTRGLYGWKV NSLVSAAIES VQSEAGDAQE DAIRRTLSSF
     LNRIYYDLRN LGTTSQDRAL NFASTNAFQA AQTFAQAVGA GYELDSITVE KSPFCRLDSD
     CWDVKLKFFD PENSRRAKKI YRFTIDV
//