ID C6WQ36_ACTMD Unreviewed; 705 AA.
AC C6WQ36;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE RecName: Full=prolyl oligopeptidase {ECO:0000256|ARBA:ARBA00011897};
DE EC=3.4.21.26 {ECO:0000256|ARBA:ARBA00011897};
GN OrderedLocusNames=Amir_1137 {ECO:0000313|EMBL:ACU35092.1};
OS Actinosynnema mirum (strain ATCC 29888 / DSM 43827 / JCM 3225 / NBRC 14064
OS / NCIMB 13271 / NRRL B-12336 / IMRU 3971 / 101).
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Actinosynnema.
OX NCBI_TaxID=446462 {ECO:0000313|EMBL:ACU35092.1, ECO:0000313|Proteomes:UP000002213};
RN [1] {ECO:0000313|EMBL:ACU35092.1, ECO:0000313|Proteomes:UP000002213}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29888 / DSM 43827 / JCM 3225 / NBRC 14064 / NCIMB 13271 /
RC NRRL B-12336 / IMRU 3971 / 101 {ECO:0000313|Proteomes:UP000002213};
RX PubMed=21304636; DOI=10.4056/sigs.21137;
RA Land M., Lapidus A., Mayilraj S., Chen F., Copeland A., Del Rio T.G.,
RA Nolan M., Lucas S., Tice H., Cheng J.F., Chertkov O., Bruce D., Goodwin L.,
RA Pitluck S., Rohde M., Goker M., Pati A., Ivanova N., Mavromatis K.,
RA Chen A., Palaniappan K., Hauser L., Chang Y.J., Jeffries C.C., Brettin T.,
RA Detter J.C., Han C., Chain P., Tindall B.J., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Actinosynnema mirum type strain (101).";
RL Stand. Genomic Sci. 1:46-53(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};
CC -!- SIMILARITY: Belongs to the peptidase S9A family.
CC {ECO:0000256|ARBA:ARBA00005228}.
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DR EMBL; CP001630; ACU35092.1; -; Genomic_DNA.
DR RefSeq; WP_012783754.1; NC_013093.1.
DR AlphaFoldDB; C6WQ36; -.
DR STRING; 446462.Amir_1137; -.
DR MEROPS; S09.076; -.
DR KEGG; ami:Amir_1137; -.
DR eggNOG; COG1505; Bacteria.
DR HOGENOM; CLU_011290_4_0_11; -.
DR Proteomes; UP000002213; 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; IPR002471; Pept_S9_AS.
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.
DR PROSITE; PS00708; PRO_ENDOPEP_SER; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ACU35092.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002213}.
FT DOMAIN 17..426
FT /note="Peptidase S9A N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02897"
FT DOMAIN 493..702
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
SQ SEQUENCE 705 AA; 75957 MW; A1888C946FAF9C79 CRC64;
MTEHSAATLP ATTAYPPATR LDLVEDLHGH RVADPYRWLE DPADPETERW SAAQDGLTAS
WLGALPGREA LAARLTELSR TGSVGAPTWR AGRAFFTRRD PDQDHAVLRV REPDGSERVL
LDPVALDPTG ATTLDSWSPS REGTRLAYQV SVGGDEHSLL HVLDVDSGEL VEGPIDRCRY
SPVGWLPGGE EFFYVRQLDP GLVPEDERLF HRRVWRHRVG ADPSTDANVH GDELDHTYYY
GLSVSADGRW LVVSGAAGTV QRNSVWIADL AAGVGPAGGG LRPVITADAG AQTSASVARD
GRLYLTTSLG APRFRLCVTD PADPGAPEDW TELAPEQQDS VLEGAGLLAG SLVLLRTRHA
VSELHLHDAT GAHVREIPTP GTGSVHGWST TDALTDPDDD RLWFGWTDFA TPVSVHRFSI
STGGTELDTP NPGSVRLPDV TTRQVEFTSP DGTTVRMFLV AGSAEPDLPR PALVTGYGGF
AVGRGPGYAS TALAWAEAGG VWAHVSLRGG DEEGEEWHRA GRRERKQNVF DDFHAAAEHL
VGQGWTTPQQ LAIMGGSNGG LLVGAALTQR PELYAAVVCS APLLDMVRYE RFLLGRLWAE
EYGSAAVPEE LGWLLSYSPY HRVAPGVEYP SVLFTVFESD SRVDPNHARK MCAALQAATA
SDPVKHPVLI RRETEVGHAG RSVSRSVALA ADQVSFLAWA TGLEL
//