ID Q52QI9_PRODI Unreviewed; 702 AA. AC Q52QI9; DT 24-MAY-2005, integrated into UniProtKB/TrEMBL. DT 24-MAY-2005, sequence version 1. DT 27-MAR-2024, entry version 77. DE SubName: Full=Subtilisin-like protein {ECO:0000313|EMBL:AAY21150.1}; GN Name=patA {ECO:0000313|EMBL:AAY21150.1}; OS Prochloron didemni. OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Prochloraceae; OC Prochloron. OX NCBI_TaxID=1216 {ECO:0000313|EMBL:AAY21150.1}; RN [1] {ECO:0000313|EMBL:AAY21150.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Reef {ECO:0000313|EMBL:AAY21150.1}; RX PubMed=15883371; DOI=10.1073/pnas.0501424102; RA Schmidt E.W., Nelson J.T., Rasko D.A., Sudek S., Eisen J.A., Haygood M.G., RA Ravel J.; RT "Patellamide A and C biosynthesis by a microcin-like pathway in Prochloron RT didemni, the cyanobacterial symbiont of Lissoclinum patella."; RL Proc. Natl. Acad. Sci. U.S.A. 102:7315-7320(2005). RN [2] {ECO:0007829|PDB:4H6V} RP X-RAY CRYSTALLOGRAPHY (1.70 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). RN [3] {ECO:0007829|PDB:3ZXX, ECO:0007829|PDB:3ZXY} RP X-RAY CRYSTALLOGRAPHY (1.58 ANGSTROMS) OF 10-289, AND DISULFIDE BONDS. RX PubMed=23169461; DOI=10.1002/cbic.201200661; RA Houssen W.E., Koehnke J., Zollman D., Vendome J., Raab A., Smith M.C., RA Naismith J.H., Jaspars M.; RT "The discovery of new cyanobactins from Cyanothece PCC 7425 defines a new RT signature for processing of patellamides."; RL ChemBioChem 13:2683-2689(2012). CC -!- SIMILARITY: Belongs to the peptidase S8 family. CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY986476; AAY21150.1; -; Genomic_DNA. DR PDB; 3ZXX; X-ray; 1.95 A; A=2-295. DR PDB; 3ZXY; X-ray; 1.58 A; A=10-289. DR PDB; 4H6V; X-ray; 1.70 A; A=1-303. DR PDBsum; 3ZXX; -. DR PDBsum; 3ZXY; -. DR PDBsum; 4H6V; -. DR AlphaFoldDB; Q52QI9; -. DR SMR; Q52QI9; -. DR MEROPS; S08.156; -. DR BioCyc; MetaCyc:MONOMER-21085; -. 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:3ZXX, ECO:0007829|PDB:3ZXY}; 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 15..260 FT /note="Peptidase S8/S53" FT /evidence="ECO:0000259|Pfam:PF00082" FT DOMAIN 426..539 FT /note="PatG" FT /evidence="ECO:0000259|Pfam:PF18047" FT DOMAIN 588..698 FT /note="PatG C-terminal" FT /evidence="ECO:0000259|Pfam:PF18065" FT REGION 336..370 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 346..370 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 23 FT /note="Charge relay system" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240" FT ACT_SITE 58 FT /note="Charge relay system" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240" FT ACT_SITE 218 FT /note="Charge relay system" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240" FT DISULFID 156..158 FT /evidence="ECO:0007829|PDB:3ZXX, ECO:0007829|PDB:3ZXY" FT DISULFID 258..269 FT /evidence="ECO:0007829|PDB:3ZXX, ECO:0007829|PDB:3ZXY" SQ SEQUENCE 702 AA; 74899 MW; BD921C16363DAF34 CRC64; MNRDILRTLS LKGDHNIRVA ILDGPVDIAH PCFQGADLTV LPTLAPTAAR SDGFMSAHGT HVASIIFGQP ETSVPGIAPQ CRGLIVPIFS DDRRRITQLD LARGIERAVN AGAHIINISG GELTDFGEAD GWLENAVSLC RQNNVLLVAA AGNNGCDCLH VPAALPAVLA VGAMDDHGHP LDFSNWGSTY EQQGILAPGE DILGAKPGGG TERLSGTSFA TPIVSGVAAL LLSEQVRRGE TPDPQKVRQL LLQSALPCDD DAPEQARRCL AGRLNVSGAF TLLKGGNMSE ELATASFPSV EASCGCNGGL VAAEPTTNSG SMPALSVSSF AGASPATMEA AGPLDEPQPL PSPAQPLTQM PAQPLPSPAQ PLTQMPAQPL PFPAQPLTQM PAQPLTQMPA PTQTLSMTTN QVTPSQAPSE LANSQFAYVL GTLGYDFGTE ARRDTFKQLM PPFDFAGNMV PANPYDARQM VDYLGNNISE ARSLIWTVNI ELTPVYAIDP TGPFASSTYH ALQELLSGQI QAEDNEEYVE RVSIPGVLTN RSVKLFSGQV VPVVEPQSTR GLYGWKVNGL VNAALEAVRA EGGDAGEARI RQTLDGFLNR IYYDLRNLGT TSQDRALNFA VTNAFQAAQT FSQSVAAGME LDSVTVEKSP FCRLDSDCWD IKLKFFDPEN NRRAKKIYRF TIDVSDLVPV TMGEVRSWSS SY //