PEPX_LACP3
ID PEPX_LACP3 Reviewed; 797 AA.
AC Q038E8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 99.
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=LSEI_1651;
OS Lacticaseibacillus paracasei (strain ATCC 334 / BCRC 17002 / CCUG 31169 /
OS CIP 107868 / KCTC 3260 / NRRL B-441) (Lactobacillus paracasei).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lacticaseibacillus.
OX NCBI_TaxID=321967;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 334 / BCRC 17002 / CCUG 31169 / CIP 107868 / KCTC 3260 / NRRL
RC B-441;
RX PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V.,
RA Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J.R., Hutkins R.,
RA O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T.,
RA Richardson P., Kozyavkin S., Weimer B.C., Mills D.A.;
RT "Comparative genomics of the lactic acid bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006).
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; CP000423; ABJ70424.1; -; Genomic_DNA.
DR RefSeq; WP_011674559.1; NC_008526.1.
DR RefSeq; YP_806866.1; NC_008526.1.
DR AlphaFoldDB; Q038E8; -.
DR SMR; Q038E8; -.
DR STRING; 321967.LSEI_1651; -.
DR ESTHER; lacc3-pepx; Lactobacillus_peptidase.
DR MEROPS; S15.001; -.
DR EnsemblBacteria; ABJ70424; ABJ70424; LSEI_1651.
DR KEGG; lca:LSEI_1651; -.
DR PATRIC; fig|321967.11.peg.1631; -.
DR HOGENOM; CLU_011800_0_0_9; -.
DR OMA; LYTASPY; -.
DR Proteomes; UP000001651; 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; Serine protease.
FT CHAIN 1..797
FT /note="Xaa-Pro dipeptidyl-peptidase"
FT /id="PRO_1000045479"
FT ACT_SITE 370
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00698"
FT ACT_SITE 490
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00698"
FT ACT_SITE 521
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00698"
SQ SEQUENCE 797 AA; 88464 MW; 79AE3BFB3A4B6FF3 CRC64;
MKLNQFARLT PDFKVQVAEL KQIGLQADPD DTFSQSTTDL FNAFFPEAYT LAAKKDKLAQ
VAVNMDQTLA AWLAKKPSKM TRRDFYNVAL QLLGFEAFTD FDLNDPFKMM TATKLPSLDH
DLTSTADLLK AVYLLLNTRT KHLVSYLDDL ANRGFLKDFQ KKQKKPTHLL FNGKVQQVFD
ARQAVREVVW IESDMDTDHD GQRDLLEATI YRPKATDQGL KVPVLFTANP YFHGTNDVTA
VTHVPETTLA VKTHGASKAE VTANPEEPAN LPHHPVNGEA TQAEAYAEEN GMYAFNDYFL
ARGFAVVYSA GVGTRYSDGF RTTGGPEETD GAVAVIEWLT GKRRAFTNRT DGITIKAWWS
TGLVAMTGKS YLATLAMAAA TTGVDGLKTI VADAGISSWY DYYRENGLVV APGGFQGEDA
DVLAVDTFSR QKSGGDLINI KQAWEKHLAT ITHDQDRTTG AYNTWWDARN YRKNANKVKA
DVVLIHGLND WNVKPTNAIK FWEAIADLPI QKKLVLHQGQ HVYVHNVRSL DFLDMMNLWL
THELLGEANG AEDVLPNVVV QDNVAVQTWS AYQNFASPAA EHVTNTRNLK TDFEAATDQF
TDHATATFDA QHDTSASFET AIITPNSAYA NSRLWLTQPP LERDQTLEGI PHLELTLAID
APTGILSVRL IDLGMAKRFG ETAATVALNG LQLGFDYKTT DILEFKPTAK PTPSKLISLG
HINLQNPKNA YEVQRITPGQ PFHISLDLQP THYHLPAGRQ LALVIHGADM AQTIRPIKTT
HYQIDLANSS ITLPYRI
