ID D2R293_PIRSD Unreviewed; 739 AA.
AC D2R293;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=prolyl oligopeptidase {ECO:0000256|ARBA:ARBA00011897};
DE EC=3.4.21.26 {ECO:0000256|ARBA:ARBA00011897};
GN OrderedLocusNames=Psta_0312 {ECO:0000313|EMBL:ADB15002.1};
OS Pirellula staleyi (strain ATCC 27377 / DSM 6068 / ICPB 4128) (Pirella
OS staleyi).
OC Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae;
OC Pirellula.
OX NCBI_TaxID=530564 {ECO:0000313|EMBL:ADB15002.1, ECO:0000313|Proteomes:UP000001887};
RN [1] {ECO:0000313|EMBL:ADB15002.1, ECO:0000313|Proteomes:UP000001887}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27377 / DSM 6068 / ICPB 4128
RC {ECO:0000313|Proteomes:UP000001887};
RX PubMed=21304671; DOI=10.4056/sigs.51657;
RA Clum A., Tindall B.J., Sikorski J., Ivanova N., Mavrommatis K., Lucas S.,
RA Glavina del Rio T., Nolan M., Chen F., Tice H., Pitluck S., Cheng J.F.,
RA Chertkov O., Brettin T., Han C., Detter J.C., Kuske C., Bruce D.,
RA Goodwin L., Ovchinikova G., Pati A., Mikhailova N., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P.,
RA Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P., Lapidus A.;
RT "Complete genome sequence of Pirellula staleyi type strain (ATCC 27377).";
RL Stand. Genomic Sci. 1:308-316(2009).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of Pro-|-Xaa >> Ala-|-Xaa in oligopeptides.;
CC EC=3.4.21.26; Evidence={ECO:0000256|ARBA:ARBA00001070};
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DR EMBL; CP001848; ADB15002.1; -; Genomic_DNA.
DR AlphaFoldDB; D2R293; -.
DR KEGG; psl:Psta_0312; -.
DR eggNOG; COG1505; Bacteria.
DR HOGENOM; CLU_011290_1_1_0; -.
DR OrthoDB; 9801421at2; -.
DR Proteomes; UP000001887; 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:SF2; 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.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:ADB15002.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001887}.
FT DOMAIN 36..449
FT /note="Peptidase S9A N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02897"
FT DOMAIN 525..733
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
SQ SEQUENCE 739 AA; 81151 MW; 77C3AECC38BC67B9 CRC64;
MFARKTPSSP LQQALVVCGY AFLTLGIENT LMAEKPPVAP IKTVAENYHG ETIVDPYRYM
EDFHSPLVQE WVKGQAEFAA NTLKTIRGRD ALLARIAELD AGTPYTISNI TCRPNGDLFY
FKQLASENVA KVFLRDGKTS QERLLIDPET FPKANADDHF TISFFRVSPN GSQLLYGFAA
SGSEETTLKV FDLLTNEDLP LAIDRIEAEY ALPSWMPDGK SFTYSRRRDI AADAPPTEGY
KFTQAFRYTI GDANEKATMI FAHGANGSPA MAEMDFPAVI LPAGSTWALG QVKHGDETDM
SLYVTPQTAL GSPHVEWVKI CDRTDQVTGY AVRGDDIYLL CAQNAPRFKV LRTSLREPSL
AKAETIVPSG EYVVDSLAVA QDALYVDVLQ GVSSQVLRIP FEANAPTETI TLPADEPSGT
VAVAHPEIPG VMIRTRSWTQ TGHLYQYDPV ARSLSETGLQ PQGKYDSPDF LTSVEFMVTS
HDGVKVPLSI IHRKDIRLDG SNPTLLSGYG AYGFTLPMRY DPISLAWLQR GGVLAFAHTR
GGGAFGKQWH HAGRKQTKAN TWKDFIACGE YLVQKGYTSP SKLAGKGGSA GGILIGRAIT
ERPDLFAAAQ ISVGCTDMLR FESTMNGPPN IPEFGTIQKA DEFRSLLAMS TFHHIQNGVK
YPAVILTHGI NDPRVEPWQS AKTTARLQAA SSSGKPILFR VDYHSGHGIG STKKQRQEEL
ADVWSFLLWQ FGDASFQTH
//
