ID Q0ATS3_MARMM Unreviewed; 734 AA. AC Q0ATS3; DT 17-OCT-2006, integrated into UniProtKB/TrEMBL. DT 17-OCT-2006, sequence version 1. DT 27-MAR-2024, entry version 83. DE SubName: Full=Prolyl oligopeptidase {ECO:0000313|EMBL:ABI64314.1}; DE EC=3.4.21.26 {ECO:0000313|EMBL:ABI64314.1}; DE Flags: Precursor; GN OrderedLocusNames=Mmar10_0018 {ECO:0000313|EMBL:ABI64314.1}; OS Maricaulis maris (strain MCS10). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Maricaulales; Maricaulaceae; OC Maricaulis. OX NCBI_TaxID=394221 {ECO:0000313|EMBL:ABI64314.1, ECO:0000313|Proteomes:UP000001964}; RN [1] {ECO:0000313|EMBL:ABI64314.1, ECO:0000313|Proteomes:UP000001964} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MCS10 {ECO:0000313|EMBL:ABI64314.1, RC ECO:0000313|Proteomes:UP000001964}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., RA Saunders E., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Viollier P., RA Stephens C., Richardson P.; RT "Complete sequence of Maricaulis maris MCS10."; RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases. 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; CP000449; ABI64314.1; -; Genomic_DNA. DR RefSeq; WP_011641961.1; NC_008347.1. DR AlphaFoldDB; Q0ATS3; -. DR STRING; 394221.Mmar10_0018; -. DR KEGG; mmr:Mmar10_0018; -. DR eggNOG; COG1505; Bacteria. DR HOGENOM; CLU_011290_4_0_5; -. DR OrthoDB; 9801421at2; -. DR Proteomes; UP000001964; Chromosome. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC. DR GO; GO:0006508; P:proteolysis; IEA:InterPro. 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; PTHR42881; PROLYL ENDOPEPTIDASE; 1. DR PANTHER; PTHR42881:SF13; PROLYL ENDOPEPTIDASE; 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. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 4: Predicted; KW Hydrolase {ECO:0000313|EMBL:ABI64314.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001964}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1..24 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 25..734 FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5004168517" FT DOMAIN 50..452 FT /note="Peptidase S9A N-terminal" FT /evidence="ECO:0000259|Pfam:PF02897" FT DOMAIN 515..724 FT /note="Peptidase S9 prolyl oligopeptidase catalytic" FT /evidence="ECO:0000259|Pfam:PF00326" SQ SEQUENCE 734 AA; 80929 MW; BFFC906C8F0D9E76 CRC64; MKFYQTFWAI SASAAILAAC TQPASNEGDQ LADTTPEAPA ERQIVEIDPN NDPRVWLEEV EGEQAIEWVE GQNERTFARL QGDERYQGLY DQALAIAQSE DRIPYGSYSG GYIWNFWQDA EHTHGLWRRT SLESYLTDAP EWDVVLDLDA LSEAEDRNWV WRGSNCLAPA YERCILTLSD GGSDAAVRRE FSITDRAFVD GGFETPEAKG GVSWIDENTL MVGLATSPED STSSGYPSVA YRWERGTDLA DATEVVRGDQ DDVGLFAFRA EDHDGTVYMM ASEANTFYDT SWWYLPADAG PVQLPLPSKS SIQDLYQGEL VFTIEENWTP VEGGETFPQG ALLSFNMAEF AATGELPDVR TVFVPGPRQS LGGMGSTASA FLVAIDENVV GGLEAFHFAD GQWSSETVPV PANMTISLRG TDNHHDVAFM NAEGFLTPDS YFMVDAAELT VEEIKSIPAR FDAEGLVVEQ LEAASPDGTM VPYFVVRRED TVMDGTTPTL LYAYGGFQVS IRPSYSGSRG QLWLENGGAY VVANIRGGGE FGPAWHQAGL KMDRQRIYDD LIAVAEDLST RGITSPRHLG VYGGSNGGLL TGVMYTQRPD LWNAVVSAVP LLDMLRYHTL LAGASWMGEY GNPEDPDEGG FLRSISPYHN VDANGDYPEI YLYTSTKDDR VHPGHARKMA HLLEELGHDY LYYENMAGGH AAAANLEERA RSEALLYTFL MQKLMDDTDP LDAE //