PEPX_STRT2
ID PEPX_STRT2 Reviewed; 755 AA.
AC Q5M2X3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Xaa-Pro dipeptidyl-peptidase {ECO:0000255|HAMAP-Rule:MF_00698};
DE EC=3.4.14.11 {ECO:0000255|HAMAP-Rule:MF_00698};
DE AltName: Full=X-Pro dipeptidyl-peptidase {ECO:0000255|HAMAP-Rule:MF_00698};
DE AltName: Full=X-prolyl-dipeptidyl aminopeptidase {ECO:0000255|HAMAP-Rule:MF_00698};
DE Short=X-PDAP {ECO:0000255|HAMAP-Rule:MF_00698};
GN Name=pepX {ECO:0000255|HAMAP-Rule:MF_00698}; OrderedLocusNames=stu1672;
OS Streptococcus thermophilus (strain ATCC BAA-250 / LMG 18311).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=264199;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-250 / LMG 18311;
RX PubMed=15543133; DOI=10.1038/nbt1034;
RA Bolotin A., Quinquis B., Renault P., Sorokin A., Ehrlich S.D.,
RA Kulakauskas S., Lapidus A., Goltsman E., Mazur M., Pusch G.D., Fonstein M.,
RA Overbeek R., Kyprides N., Purnelle B., Prozzi D., Ngui K., Masuy D.,
RA Hancy F., Burteau S., Boutry M., Delcour J., Goffeau A., Hols P.;
RT "Complete sequence and comparative genome analysis of the dairy bacterium
RT Streptococcus thermophilus.";
RL Nat. Biotechnol. 22:1554-1558(2004).
CC -!- FUNCTION: Removes N-terminal dipeptides sequentially from polypeptides
CC having unsubstituted N-termini provided that the penultimate residue is
CC proline. {ECO:0000255|HAMAP-Rule:MF_00698}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolyzes Xaa-Pro-|- bonds to release unblocked, N-terminal
CC dipeptides from substrates including Ala-Pro-|-p-nitroanilide and
CC (sequentially) Tyr-Pro-|-Phe-Pro-|-Gly-Pro-|-Ile.; EC=3.4.14.11;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00698};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00698}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00698}.
CC -!- SIMILARITY: Belongs to the peptidase S15 family. {ECO:0000255|HAMAP-
CC Rule:MF_00698}.
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DR EMBL; CP000023; AAV61274.1; -; Genomic_DNA.
DR RefSeq; WP_011226486.1; NC_006448.1.
DR AlphaFoldDB; Q5M2X3; -.
DR SMR; Q5M2X3; -.
DR STRING; 264199.stu1672; -.
DR ESTHER; strtr-pepx; Lactobacillus_peptidase.
DR MEROPS; S15.001; -.
DR EnsemblBacteria; AAV61274; AAV61274; stu1672.
DR GeneID; 66899417; -.
DR KEGG; stl:stu1672; -.
DR PATRIC; fig|264199.4.peg.1647; -.
DR eggNOG; COG2936; Bacteria.
DR HOGENOM; CLU_011800_0_0_9; -.
DR OMA; LYTASPY; -.
DR Proteomes; UP000001170; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008239; F:dipeptidyl-peptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; -; 1.
DR HAMAP; MF_00698; Aminopeptidase_S15; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR008252; Pept_S15_Xpro.
DR InterPro; IPR015251; PepX_N_dom.
DR InterPro; IPR036313; PepX_N_dom_sf.
DR InterPro; IPR000383; Xaa-Pro-like_dom.
DR InterPro; IPR013736; Xaa-Pro_dipept_C.
DR Pfam; PF02129; Peptidase_S15; 1.
DR Pfam; PF08530; PepX_C; 1.
DR Pfam; PF09168; PepX_N; 1.
DR PRINTS; PR00923; LACTOPTASE.
DR SMART; SM00939; PepX_C; 1.
DR SMART; SM00940; PepX_N; 1.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR SUPFAM; SSF81761; SSF81761; 1.
PE 3: Inferred from homology;
KW Aminopeptidase; Cytoplasm; Hydrolase; Protease; Reference proteome;
KW Serine protease.
FT CHAIN 1..755
FT /note="Xaa-Pro dipeptidyl-peptidase"
FT /id="PRO_1000045496"
FT ACT_SITE 348
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00698"
FT ACT_SITE 468
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00698"
FT ACT_SITE 498
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00698"
SQ SEQUENCE 755 AA; 85574 MW; 6C8FD2DFF032CE87 CRC64;
MKFNQFSYIP VSPETAYQEL RSLGFEVSLD ASAKANFESF VRKYFLFFED TDLALKNWIA
DPETDLLSFF QSDRPLTAEV FGLVALQLLG FVPNVDFTDS VAFLEKMAFP IAFDGSLNNL
HQLLATRTQS GNTLIDQLVA QDLIPISNDY VFFNGKSLAT FDTNQLHREV VYVETPVDTD
KDGLLDLVKV TILRPNVDFP VPAMMTASPY QQGTNEPSSD KLTHKMEGDL LVKPAGKISL
SRPEIKAPEA DLTPINPVTK AEERFAHTDT YTLNDYMLAR GVASIYVSGV GTFNSEGFMT
SGDYQQVLAY KAVIDWLNGR ARAFTSRSRQ HTITADWASG KVTTTGLSYL GTMSNALATT
GVDGLEMVIA EAGISSWYDY YRENGLLVSP GGYPGEDLDT LTEFTYSRAL LAGEYLRHQK
DYEAYLNELS TAIDRKHGDY NQFWHDRNYV QFADRVKATV VFTHGSQDWN VKPINVYQMF
RALPKSLEKH LFFHNGAHVY MNAWQSIDFR ESMNALICQK LLGLDNGYTL PTVIWQNNQS
EQTWEVLDNF GHDNGKHIQL GKSEASIANH YEEEIFAKYG KAYQSFKDDL FMDKANAITL
DFELDQDIQI NGRVHLELRV KSSTNRGLIS AQVLEMGDKK YLAPIPAPKR MSLDNGRLFK
EEALRELPFK QAKYRVITKG HLNLQNRKDL LSIENVTPNE WMTIGLDLQP TIYKLNKGDK
LRLVLYTTDF EHTIRDNSDY EVTVDLSQSK MTLPY