ID   PEPX_LACRH              Reviewed;         797 AA.
AC   Q9RDW6;
DT   22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 95.
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};
OS   Lacticaseibacillus rhamnosus (Lactobacillus rhamnosus).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lacticaseibacillus.
OX   NCBI_TaxID=47715;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=1-6;
RX   PubMed=10613874; DOI=10.1128/jb.182.1.146-154.2000;
RA   Varmanen P., Savijoki K., Avall S., Palva A., Tynkkynen S.;
RT   "X-prolyl dipeptidyl aminopeptidase gene (pepX) is part of the glnRA operon
RT   in Lactobacillus rhamnosus.";
RL   J. Bacteriol. 182:146-154(2000).
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; AJ224996; CAB58995.1; -; Genomic_DNA.
DR   PIR; T46737; T46737.
DR   AlphaFoldDB; Q9RDW6; -.
DR   SMR; Q9RDW6; -.
DR   STRING; 568703.LGG_01695; -.
DR   ESTHER; lacrh-pepx; Lactobacillus_peptidase.
DR   eggNOG; COG2936; Bacteria.
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_0000220223"
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;  87981 MW;  9E14407E740B96E4 CRC64;
     MKLNQFARLT PDIDQQLKEL ARIGLPADPQ APFADTAAAM YAAFFPEAYQ PAAQQDKFAQ
     VAVNSHQNLA EWLATKPTHM KRADFYNVAL QLLGFEAFSD FDLSDPISFM TVTKLPSVAH
     DLLHTADLLQ ASYLLLTTRT KHLVSFLDDL ANRGFFKDFQ AQSSQPAHLL FNGKVQQVFD
     ARQAVREVVW IESDVDSDHD GQRDLLEATI YRPKATDRGL KVPVLFTANP YFHGTNDVTA
     ATHVPETVLA VKPHGASKAE VTAAPASKPK LPARPVTGET KQAAAYAEEN SPYAFNDYFL
     ARGFAVVYSA GVGTRYSDGF RTIGGPEETD GAVAVIEWLT GKRRAFTNRT DGVAIKAWWS
     SGKVAMTGKS YLATLAIAGA TTGVEGLKTI VADAGISSWY DYYRENGLVV APGGYQGEDA
     DVLAVDTFSR QKSGGDMIRL KKAWEQHLAQ MTRDQDRTTG AYTAWWDARN YRKNAANVKA
     DVVLIHGLND WNVKPKNAIR FWQAIADLPI QKKLILHQGQ HVYVHNVRSL DFLDMMNLWL
     THELLGVANQ AEQVLPNVLV QDNVTPQTWS AYSDFANPAA EHVTTTANLK TDFESATDQF
     SDHATATFTA QHDTSASFEK AIITPNSAYV NSRLWLTQPV LEHDRVLEGI PHLELTLAVD
     APTGILSVRL VDLGKAKRFE ENAATVGASG LQLGFDFKTT DIVEFKPANK ETPSKLITLG
     HINLQNPKNA YEVQTITPGQ FFHVSLDLQP THYHLPAGRQ LALIIHGADM AQTIRPTKVT
     HYQLDLAKST LTLPFRI