ID   F5B6Y7_PLAAG            Unreviewed;       655 AA.
AC   F5B6Y7;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   SubName: Full=N-terminal cyanobactin protease {ECO:0000313|EMBL:AED99426.1};
GN   Name=pagA {ECO:0000313|EMBL:AED99426.1};
OS   Planktothrix agardhii NIES-596.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Oscillatoriales; Microcoleaceae; Planktothrix.
OX   NCBI_TaxID=443922 {ECO:0000313|EMBL:AED99426.1};
RN   [1] {ECO:0000313|EMBL:AED99426.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NIES-596 {ECO:0000313|EMBL:AED99426.1};
RX   PubMed=21513887; DOI=10.1016/j.chembiol.2011.01.019;
RA   Donia M.S., Schmidt E.W.;
RT   "Linking chemistry and genetics in the growing cyanobactin natural products
RT   family.";
RL   Chem. Biol. 18:508-519(2011).
RN   [2] {ECO:0007829|PDB:4H6W}
RP   X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 1-303, AND DISULFIDE BONDS.
RX   PubMed=23177196; DOI=10.1016/j.chembiol.2012.09.012;
RA   Agarwal V., Pierce E., McIntosh J., Schmidt E.W., Nair S.K.;
RT   "Structures of cyanobactin maturation enzymes define a family of
RT   transamidating proteases.";
RL   Chem. Biol. 19:1411-1422(2012).
CC   -!- SIMILARITY: Belongs to the peptidase S8 family.
CC       {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR   EMBL; HQ655154; AED99426.1; -; Genomic_DNA.
DR   PDB; 4H6W; X-ray; 2.45 A; A/B=1-303.
DR   PDBsum; 4H6W; -.
DR   AlphaFoldDB; F5B6Y7; -.
DR   SMR; F5B6Y7; -.
DR   MEROPS; S08.156; -.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd07476; Peptidases_S8_thiazoline_oxidase_subtilisin-like_protease; 1.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR   InterPro; IPR040636; PatG_C.
DR   InterPro; IPR040483; PatG_dom.
DR   InterPro; IPR034056; Pep_S8_PatG/PatA-like.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
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   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:4H6W};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU01240};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW   ProRule:PRU01240};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}.
FT   DOMAIN          19..260
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   DOMAIN          380..492
FT                   /note="PatG"
FT                   /evidence="ECO:0000259|Pfam:PF18047"
FT   DOMAIN          538..651
FT                   /note="PatG C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18065"
FT   ACT_SITE        26
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        61
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        221
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   DISULFID        159..161
FT                   /evidence="ECO:0007829|PDB:4H6W"
FT   DISULFID        261..272
FT                   /evidence="ECO:0007829|PDB:4H6W"
SQ   SEQUENCE   655 AA;  70565 MW;  EEDD3FFDE85FD42E CRC64;
     MTNIPGLKKL WSETRGDPKI CVAVLDGIVD QNHPCFIGAD LTRLPSLVSG EANANGSMST
     HGTHVASIIF GQHDSPVTGI APQCRGLIVP VFADESLKLS QLDLSRAIEQ AVNNGANIIN
     VSAGQLTDAG EADTWLEKAI QLCQENNVLL IAATGNDGCE CLHVPASLPT VLAVGAMDDQ
     GKPVDFSNWG DAYQKQGILA PGKDILGAKP NGGTIRLSGT SFATPIVSGV AALLLSLQIK
     RGEKPDPQKV KNALLASATP CNPKDTDDQS RCLMGKLNIL DAIEHLTGET MSEDLELESV
     EASGCGCQDT QINESELDNQ LETASEIKPD EIVASVTTQT PINIPSFPQQ TTNQPTMSNR
     TSNFVTASEA PSELEGKNLV YALGVLGYDF GSEARRDSFK QLMPGVSIEG TMIPANPYDA
     RQMVDYLGEN LPEAKALIWT LNLELTPIYA IEPVGGFSRD VYEVLQGLLS GQIQEENSPE
     FVQRVSIPGV LTGRSVKLFS GQVVPVIEIN NTRGLYGWKV NSLVSAAIES VQSEAGDAQE
     DAIRRTLSSF LNRIYYDLRN LGTTSQDRAL NFASTNAFQA AQTFAQAVGA GYELDSITVE
     KSPFCRLDSD CWDVKLKFFD PENSRRAKKI YRFTIDVSDT IPVTLGEVRS WSSAY
//