PEPX_LACLA
ID PEPX_LACLA Reviewed; 763 AA.
AC Q9CE01; Q93D09;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Xaa-Pro dipeptidyl-peptidase;
DE EC=3.4.14.11;
DE AltName: Full=X-Pro dipeptidyl-peptidase;
DE AltName: Full=X-prolyl-dipeptidyl aminopeptidase;
DE Short=X-PDAP;
GN Name=pepX; Synonyms=pepXP; OrderedLocusNames=LL2049; ORFNames=L118079;
OS Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=272623;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Ming X., Yang L., Liu J., Lin J., Ding M.;
RT "An X-prolyl dipeptidyl aminopeptidase from Lactococcus lactis: cloning,
RT expression in Escherichia coli and removal of N-terminal Pro-Pro from
RT recombinant proteins.";
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IL1403;
RX PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA Ehrlich S.D., Sorokin A.;
RT "The complete genome sequence of the lactic acid bacterium Lactococcus
RT lactis ssp. lactis IL1403.";
RL Genome Res. 11:731-753(2001).
CC -!- FUNCTION: Removes N-terminal dipeptides sequentially from polypeptides
CC having unsubstituted N-termini provided that the penultimate residue is
CC proline. {ECO:0000250}.
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 -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase S15 family. {ECO:0000305}.
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DR EMBL; AF401518; AAK96441.1; -; Genomic_DNA.
DR EMBL; AE005176; AAK06147.1; -; Genomic_DNA.
DR PIR; A86881; A86881.
DR RefSeq; NP_268206.1; NC_002662.1.
DR RefSeq; WP_004254450.1; NC_002662.1.
DR AlphaFoldDB; Q9CE01; -.
DR SMR; Q9CE01; -.
DR STRING; 272623.L118079; -.
DR ESTHER; lacla-pepx; Lactobacillus_peptidase.
DR MEROPS; S15.001; -.
DR PaxDb; Q9CE01; -.
DR EnsemblBacteria; AAK06147; AAK06147; L118079.
DR KEGG; lla:L118079; -.
DR PATRIC; fig|272623.7.peg.2206; -.
DR eggNOG; COG2936; Bacteria.
DR HOGENOM; CLU_011800_0_0_9; -.
DR OMA; LYTASPY; -.
DR Proteomes; UP000002196; 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..763
FT /note="Xaa-Pro dipeptidyl-peptidase"
FT /id="PRO_0000220220"
FT ACT_SITE 348
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 468
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 498
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CONFLICT 78
FT /note="T -> A (in Ref. 1; AAK96441)"
FT /evidence="ECO:0000305"
FT CONFLICT 205
FT /note="I -> M (in Ref. 1; AAK96441)"
FT /evidence="ECO:0000305"
FT CONFLICT 420
FT /note="D -> A (in Ref. 1; AAK96441)"
FT /evidence="ECO:0000305"
FT CONFLICT 457
FT /note="R -> K (in Ref. 1; AAK96441)"
FT /evidence="ECO:0000305"
FT CONFLICT 637
FT /note="L -> I (in Ref. 1; AAK96441)"
FT /evidence="ECO:0000305"
FT CONFLICT 763
FT /note="K -> N (in Ref. 1; AAK96441)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 763 AA; 87741 MW; D489B6BCBEBFB48E CRC64;
MRFNHFSIVD KNFDEQLAEL DQLGFRWSVF WDEKKILKDF LIQSPTDMTV LQANTELDVI
EFLKSSIELD WEIFWNITLQ LLDFVPNFDF EIGKATEFAK KLNLPQRDVE MTTETIISAF
YYLLCSRRKS GMILVEHWVS EGLLPLDNHY HFFNDKSLAT FDSSLLEREV VWVESPVDTE
QKGKNDLIKI QIIRPKSTEK LPVVITASPY HLGINEKAND LALHEMNVDL EKKDSHKIHV
QGKLPQKRPS ETKELPIVDK APYRFTHGWT YSLNDYFLTR GFASIYVAGV GTRGSNGFQT
SGDYQQIYSM TAVIDWLNGR TRAYTSRKKT HEIKATWANG KVAMTGKSYL GTMAYGAATT
GVDGLEVILA EAGISSWYNY YRENGLVRSP GGFPGEDLDV LAALTYSRNL DGADYLKGND
EYEKRLAEMT TALDRKSGDY NQFWHDRNYL INSDQVRADV LIVHGLQDWN VTPEQAYNFW
QALPEGHAKH AFLHRGAHIY MNSWQSIDFS ETINAYFSAK LLDRDLNLNL PPVILQENSK
EQVWSAVSKF GGDDQLKLPL GKTAVSFAQF DNHYDDESFK KYSKDFNVFK KDLFENKANE
AVIDLELPSE LTINGPIELE IRLKLNDSKG LLSAQILDFG PKKRLEDKAR VKDFKVLDRG
RNFMLDDLVE LPLVESPYQL VTKGFTNLQN KDLLTVSDLK ADEWFTLKFE LQPTIYHLEK
ADKLRVILYS TDFEHTVRDN RKVTYEIDLS QSKLIIPIES VKK
