ID Y4SO_SINFN Reviewed; 705 AA. AC P55656; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 27-MAR-2024, entry version 125. DE RecName: Full=Uncharacterized peptidase y4sO; DE EC=3.4.21.-; GN OrderedLocusNames=NGR_a01580; ORFNames=y4sO; OS Sinorhizobium fredii (strain NBRC 101917 / NGR234). OG Plasmid sym pNGR234a. OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium. OX NCBI_TaxID=394; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBRC 101917 / NGR234; RX PubMed=9163424; DOI=10.1038/387394a0; RA Freiberg C.A., Fellay R., Bairoch A., Broughton W.J., Rosenthal A., RA Perret X.; RT "Molecular basis of symbiosis between Rhizobium and legumes."; RL Nature 387:394-401(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBRC 101917 / NGR234; RX PubMed=19376903; DOI=10.1128/aem.00515-09; RA Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A., RA Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A., RA Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A., RA Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.; RT "Rhizobium sp. strain NGR234 possesses a remarkable number of secretion RT systems."; RL Appl. Environ. Microbiol. 75:4035-4045(2009). CC -!- SIMILARITY: Belongs to the peptidase S9A family. {ECO:0000305}. 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; U00090; AAB91854.1; -; Genomic_DNA. DR RefSeq; NP_444067.1; NC_000914.2. DR RefSeq; WP_010875194.1; NC_000914.2. DR AlphaFoldDB; P55656; -. DR SMR; P55656; -. DR ESTHER; rhisn-y4so; S9N_PREPL_Peptidase_S9. DR KEGG; rhi:NGR_a01580; -. DR PATRIC; fig|394.7.peg.145; -. DR eggNOG; COG1770; Bacteria. DR HOGENOM; CLU_011290_0_1_5; -. DR OrthoDB; 9801421at2; -. DR Proteomes; UP000001054; Plasmid sym pNGR234a. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1. DR Gene3D; 2.130.10.120; Prolyl oligopeptidase, N-terminal domain; 1. DR InterPro; IPR029058; AB_hydrolase. DR InterPro; IPR023302; Pept_S9A_N. DR InterPro; IPR001375; Peptidase_S9. DR InterPro; IPR002470; Peptidase_S9A. DR PANTHER; PTHR11757:SF19; PROLYL ENDOPEPTIDASE-LIKE; 1. DR PANTHER; PTHR11757; PROTEASE FAMILY S9A OLIGOPEPTIDASE; 1. DR Pfam; PF00326; Peptidase_S9; 1. DR Pfam; PF02897; Peptidase_S9_N; 1. DR PRINTS; PR00862; PROLIGOPTASE. DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1. DR SUPFAM; SSF50993; Peptidase/esterase 'gauge' domain; 1. PE 3: Inferred from homology; KW Hydrolase; Plasmid; Protease; Reference proteome; Serine protease. FT CHAIN 1..705 FT /note="Uncharacterized peptidase y4sO" FT /id="PRO_0000122407" FT ACT_SITE 554 FT /note="Charge relay system" FT /evidence="ECO:0000250" FT ACT_SITE 676 FT /note="Charge relay system" FT /evidence="ECO:0000250" SQ SEQUENCE 705 AA; 79768 MW; EA4985F696A89880 CRC64; MENKSLQPPL PRSERRIRVL HNDVTIDSYG WLRDREDPDV LAYLEAENHY ADEVTSYVAE LKADLIAEIE KRDSCDGAPP PFQVGFFFYF QKSQSGLLHS AWWRRPVTGG PEELVFDPNT LPGAEVFYSL GALEPSDDGR YIAFSFDLIG NERYELRVRD MTNGREIWRD PSRAGRLVWA ADNRTLFFTR ERADRRQHDR VVRLDVETGR SEVVFEEVNE RLALVVRRSG SGAYLFIDVI ITSDMSSRIQ RAAAEVWCLP AERPTDMWRR ILARELGHEI YAEHWGNEFL FRVNDTGPNL RLVRTAIDDT SPSRWQEVVP HRAGITLEEI HVLEEHVIVL EREGIQPRLV AHHRNGRVGP SIVPVEHSCT VTVGLSAGGS YSCARHPYRV SALTYKICSF VTPDIFIQHD LLTDKSKVLY RTLVSGFEPE LYEARVVMAK AEDGVEVPIS IVARRDRGED GPVLLNVYGC YGAQSLPAFF GWPSSMTARL SLLDRGVAFG IVHVRGGGEL GRAWHEAATR DQKRLTHTDL IAAAECLVEH RFASRDGIVI EGRSAGGGTV LAAAVLRPDL FRAVLAEVPL ADIIDTELDF TLPYALRETA EYGDPHLAND YQYLRSYDPY YNLTPDRRYP PTYIDAALHD SQVLYYQPAR YVAQRRSKAV DRDPDLIFRT RMIGGHMGVS HGPGVAEEAA FRMAWILHRL GQSGR //