TPAP_STRMB
ID TPAP_STRMB Reviewed; 477 AA.
AC P83615; N1NSS3; Q6F4C4;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 48.
DE RecName: Full=Prolyl tri/tetrapeptidyl aminopeptidase;
DE Short=PTP-SM;
DE EC=3.4.11.-;
DE AltName: Full=Tripeptidyl aminopeptidase;
DE Short=SM-TAP;
DE Flags: Precursor;
GN Name=ptp;
OS Streptomyces mobaraensis (Streptoverticillium mobaraense).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=35621 {ECO:0000305};
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 34-53, FUNCTION,
RP ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 29032 / CBS 199.75 / DSM 40847 / NBRC 13819 / NCIMB 11159 /
RC NRRL B-3729 / VKM Ac-928;
RX PubMed=15598885; DOI=10.1093/jb/mvh129;
RA Umezawa Y., Yokoyama K., Kikuchi Y., Date M., Ito K., Yoshimoto T.,
RA Matsui H.;
RT "Novel prolyl tri/tetra-peptidyl aminopeptidase from Streptomyces
RT mobaraensis: substrate specificity and enzyme gene cloning.";
RL J. Biochem. 136:293-300(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 29032 / CBS 199.75 / DSM 40847 / NBRC 13819 / NCIMB 11159 /
RC NRRL B-3729 / VKM Ac-928;
RA Zindel S., Froels S., Kletzin A., Pfeifer F., Fuchsbauer H.L.;
RT "Confirmation of the genes coding a transglutaminase and a prolyl
RT tri/tetrapeptidyl aminopeptidase from Streptomyces mobaraensis.";
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 34-68, FUNCTION, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 27441 / CBS 777.72 / DSM 40587 / JCM 4778 / NBRC 13476 / VKM
RC Ac-879;
RX PubMed=14519127; DOI=10.1046/j.1432-1033.2003.03809.x;
RA Zotzel J., Pasternack R., Pelzer C., Ziegert D., Mainusch M.,
RA Fuchsbauer H.-L.;
RT "Activated transglutaminase from Streptomyces mobaraensis is processed by a
RT tripeptidyl aminopeptidase in the final step.";
RL Eur. J. Biochem. 270:4149-4155(2003).
CC -!- FUNCTION: Has proline-specific tripeptidyl aminopeptidase and
CC tetrapeptidyl aminopeptidase activity. Activity is highest against
CC tripeptides containing an Ala-Pro motif. Involved in the final
CC processing of transglutaminase, by removing either the tetrapeptide
CC Phe-Arg-Ala-Pro left after TAMEP or SAM-P45 hydrolysis, or the
CC tripeptide Arg-Ala-Pro left after SGMP II hydrolysis in a single step.
CC {ECO:0000269|PubMed:14519127, ECO:0000269|PubMed:15598885}.
CC -!- ACTIVITY REGULATION: Completely inhibited by the serine protease
CC inhibitor phenylmethylsulfonyl fluoride. Partially inhibited by the
CC serine protease inhibitor Pefabloc. Not inhibited by cysteine
CC proteinase-specific or metalloproteinase-specific inhibitors. Not
CC inhibited by prolinal or its derivatives. EDTA and EGTA both partially
CC inhibit this enzyme (PubMed:14519127). EDTA has no effect on activity
CC (PubMed:15598885). {ECO:0000269|PubMed:14519127,
CC ECO:0000269|PubMed:15598885}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.072 mM for Gly-Ala-Pro-BNA {ECO:0000269|PubMed:14519127,
CC ECO:0000269|PubMed:15598885};
CC KM=0.26 mM for Gly-Ala-Gly-Pro-BNA {ECO:0000269|PubMed:14519127,
CC ECO:0000269|PubMed:15598885};
CC pH dependence:
CC Optimum pH is 7.0-7.5 (PubMed:14519127). Optimum pH is 6.0-6.5
CC (PubMed:15598885). Active between pH 4.3 and 8.3. Stable after 12
CC hours incubation from pH 4.0 to 9.0. {ECO:0000269|PubMed:14519127,
CC ECO:0000269|PubMed:15598885};
CC Temperature dependence:
CC Optimum temperature is 45 degrees Celsius.
CC {ECO:0000269|PubMed:14519127, ECO:0000269|PubMed:15598885};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Cell surface.
CC Note=Secreted (PubMed:14519127). Cell surface (PubMed:15598885).
CC {ECO:0000269|PubMed:14519127, ECO:0000269|PubMed:15598885}.
CC -!- SIMILARITY: Belongs to the peptidase S37 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; AB159671; BAD30013.1; -; Genomic_DNA.
DR EMBL; HF968463; CCW72545.1; -; Genomic_DNA.
DR RefSeq; WP_004943027.1; NZ_VOKX01000009.1.
DR AlphaFoldDB; P83615; -.
DR SMR; P83615; -.
DR ESTHER; strmb-tpap; Peptidase_S37.
DR MEROPS; S37.001; -.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR008761; Peptidase_S37.
DR Pfam; PF05576; Peptidase_S37; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Aminopeptidase; Direct protein sequencing; Hydrolase; Protease; Secreted;
KW Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT PROPEP 28..33
FT /evidence="ECO:0000269|PubMed:14519127,
FT ECO:0000269|PubMed:15598885"
FT /id="PRO_0000401059"
FT CHAIN 34..477
FT /note="Prolyl tri/tetrapeptidyl aminopeptidase"
FT /id="PRO_0000072645"
FT REGION 448..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..477
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 477 AA; 53702 MW; BA26EE2F66AC2C0E CRC64;
MRKALRSLLA ASMLIGAIGA GSATAEAASI TAPQADIKDR ILKIPGMKFV EEKPYQGYRY
LVMTYRQPVD HRNPGKGTFE QRFTLLHKDT DRPTVFFTSG YNVSTNPSRS EPTRIVDGNQ
VSMEYRFFTP SRPQPADWSK LDIWQAASDQ HRLYQALKPV YGKNWLATGG SKGGMTATYF
RRFYPNDMNG TVAYVAPNDV NDKEDSAYDK FFQNVGDKAC RTQLNSVQRE ALVRRDEIVA
RYEKWAKENG KTFKVVGSAD KAYENVVLDL VWSFWQYHLQ SDCASVPATK ASTDELYKFI
DDISGFDGYT DQGLERFTPY YYQAGTQLGA PTVKNPHLKG VLRYPGINQP RSYVPRDIPM
TFRPGAMADV DRWVREDSRN MLFVYGQNDP WSGEPFRLGK GAAARHDYRF YAPGGNHGSN
IAQLVADERA KATAEVLKWA GVAPQAVQKD EKAAKPLAPF DAKLDRVKND KQSALRP
