PEPX_LACLC
ID PEPX_LACLC Reviewed; 763 AA.
AC P22346; P22093;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 03-AUG-2022, entry version 127.
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;
OS Lactococcus lactis subsp. cremoris (Streptococcus cremoris).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=1359;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NCDO 763 / ML3;
RX PubMed=1674656; DOI=10.1128/aem.57.1.45-50.1991;
RA Nardi M., Chopin M.-C., Chopin A., Cals M.M., Gripon J.-C.;
RT "Cloning and DNA sequence analysis of an X-prolyl dipeptidyl aminopeptidase
RT gene from Lactococcus lactis subsp. lactis NCDO 763.";
RL Appl. Environ. Microbiol. 57:45-50(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-25.
RC STRAIN=P8-2-47;
RX PubMed=1674655; DOI=10.1128/aem.57.1.38-44.1991;
RA Mayo B., Kok J., Venema K., Bockelmann W., Teuber M., Reinke H., Venema G.;
RT "Molecular cloning and sequence analysis of the X-prolyl dipeptidyl
RT aminopeptidase gene from Lactococcus lactis subsp. cremoris.";
RL Appl. Environ. Microbiol. 57:38-44(1991).
RN [3]
RP ACTIVE SITE SER-348.
RX PubMed=1459244; DOI=10.1016/0014-5793(92)80960-o;
RA Chich J.-F., Chapot-Chartier M.P., Ribadeau-Dumas B., Gripon J.-C.;
RT "Identification of the active site serine of the X-prolyl dipeptidyl
RT aminopeptidase from Lactococcus lactis.";
RL FEBS Lett. 314:139-142(1992).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RX PubMed=12377124; DOI=10.1016/s0969-2126(02)00851-1;
RA Rigolet P., Mechin I., Delage M.-M., Chich J.-F.;
RT "The structural basis for catalysis and specificity of the X-prolyl
RT dipeptidyl aminopeptidase from Lactococcus lactis.";
RL Structure 10:1383-1394(2002).
CC -!- FUNCTION: Removes N-terminal dipeptides sequentially from polypeptides
CC having unsubstituted N-termini provided that the penultimate residue is
CC proline.
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.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the peptidase S15 family. {ECO:0000305}.
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DR EMBL; M35865; AAA25207.1; -; Genomic_DNA.
DR EMBL; M58315; AAA25232.1; -; Genomic_DNA.
DR PIR; A43747; A43747.
DR PIR; A43748; A43748.
DR RefSeq; WP_011835997.1; NZ_LITG01000138.1.
DR RefSeq; WP_021165010.1; NZ_WJUX01000052.1.
DR PDB; 1LNS; X-ray; 2.20 A; A=1-763.
DR PDBsum; 1LNS; -.
DR AlphaFoldDB; P22346; -.
DR SMR; P22346; -.
DR ESTHER; lacla-pepx; Lactobacillus_peptidase.
DR MEROPS; S15.001; -.
DR OMA; LYTASPY; -.
DR BRENDA; 3.4.14.11; 2903.
DR BRENDA; 3.4.14.5; 2903.
DR EvolutionaryTrace; P22346; -.
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 1: Evidence at protein level;
KW 3D-structure; Aminopeptidase; Cytoplasm; Direct protein sequencing;
KW Hydrolase; Protease; Serine protease.
FT CHAIN 1..763
FT /note="Xaa-Pro dipeptidyl-peptidase"
FT /id="PRO_0000220221"
FT ACT_SITE 348
FT /note="Charge relay system"
FT /evidence="ECO:0000269|PubMed:1459244"
FT ACT_SITE 468
FT /note="Charge relay system"
FT ACT_SITE 498
FT /note="Charge relay system"
FT CONFLICT 50
FT /note="A -> D (in Ref. 2; AAA25232)"
FT /evidence="ECO:0000305"
FT CONFLICT 130
FT /note="T -> N (in Ref. 2; AAA25232)"
FT /evidence="ECO:0000305"
FT CONFLICT 367
FT /note="L -> V (in Ref. 2; AAA25232)"
FT /evidence="ECO:0000305"
FT CONFLICT 573
FT /note="N -> H (in Ref. 2; AAA25232)"
FT /evidence="ECO:0000305"
FT CONFLICT 649
FT /note="V -> A (in Ref. 2; AAA25232)"
FT /evidence="ECO:0000305"
FT CONFLICT 681
FT /note="V -> I (in Ref. 2; AAA25232)"
FT /evidence="ECO:0000305"
FT CONFLICT 692
FT /note="S -> N (in Ref. 2; AAA25232)"
FT /evidence="ECO:0000305"
FT HELIX 13..22
FT /evidence="ECO:0007829|PDB:1LNS"
FT HELIX 33..42
FT /evidence="ECO:0007829|PDB:1LNS"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:1LNS"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:1LNS"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:1LNS"
FT HELIX 59..64
FT /evidence="ECO:0007829|PDB:1LNS"
FT HELIX 71..81
FT /evidence="ECO:0007829|PDB:1LNS"
FT TURN 86..88
FT /evidence="ECO:0007829|PDB:1LNS"
FT HELIX 95..101
FT /evidence="ECO:0007829|PDB:1LNS"
FT HELIX 113..125
FT /evidence="ECO:0007829|PDB:1LNS"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:1LNS"
FT HELIX 134..140
FT /evidence="ECO:0007829|PDB:1LNS"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:1LNS"
FT STRAND 167..174
FT /evidence="ECO:0007829|PDB:1LNS"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:1LNS"
FT STRAND 187..194
FT /evidence="ECO:0007829|PDB:1LNS"
FT STRAND 201..207
FT /evidence="ECO:0007829|PDB:1LNS"
FT HELIX 216..222
FT /evidence="ECO:0007829|PDB:1LNS"
FT STRAND 235..237
FT /evidence="ECO:0007829|PDB:1LNS"
FT HELIX 272..278
FT /evidence="ECO:0007829|PDB:1LNS"
FT TURN 279..281
FT /evidence="ECO:0007829|PDB:1LNS"
FT STRAND 283..287
FT /evidence="ECO:0007829|PDB:1LNS"
FT HELIX 304..317
FT /evidence="ECO:0007829|PDB:1LNS"
FT STRAND 323..326
FT /evidence="ECO:0007829|PDB:1LNS"
FT STRAND 338..347
FT /evidence="ECO:0007829|PDB:1LNS"
FT HELIX 349..358
FT /evidence="ECO:0007829|PDB:1LNS"
FT TURN 359..361
FT /evidence="ECO:0007829|PDB:1LNS"
FT STRAND 365..372
FT /evidence="ECO:0007829|PDB:1LNS"
FT HELIX 377..381
FT /evidence="ECO:0007829|PDB:1LNS"
FT STRAND 382..387
FT /evidence="ECO:0007829|PDB:1LNS"
FT HELIX 398..405
FT /evidence="ECO:0007829|PDB:1LNS"
FT HELIX 407..410
FT /evidence="ECO:0007829|PDB:1LNS"
FT HELIX 412..433
FT /evidence="ECO:0007829|PDB:1LNS"
FT TURN 435..437
FT /evidence="ECO:0007829|PDB:1LNS"
FT HELIX 442..445
FT /evidence="ECO:0007829|PDB:1LNS"
FT HELIX 449..455
FT /evidence="ECO:0007829|PDB:1LNS"
FT STRAND 458..465
FT /evidence="ECO:0007829|PDB:1LNS"
FT HELIX 474..482
FT /evidence="ECO:0007829|PDB:1LNS"
FT STRAND 489..495
FT /evidence="ECO:0007829|PDB:1LNS"
FT STRAND 504..506
FT /evidence="ECO:0007829|PDB:1LNS"
FT HELIX 509..521
FT /evidence="ECO:0007829|PDB:1LNS"
FT STRAND 532..536
FT /evidence="ECO:0007829|PDB:1LNS"
FT STRAND 540..542
FT /evidence="ECO:0007829|PDB:1LNS"
FT STRAND 544..548
FT /evidence="ECO:0007829|PDB:1LNS"
FT STRAND 555..560
FT /evidence="ECO:0007829|PDB:1LNS"
FT STRAND 562..565
FT /evidence="ECO:0007829|PDB:1LNS"
FT STRAND 567..572
FT /evidence="ECO:0007829|PDB:1LNS"
FT HELIX 576..584
FT /evidence="ECO:0007829|PDB:1LNS"
FT HELIX 586..594
FT /evidence="ECO:0007829|PDB:1LNS"
FT STRAND 601..606
FT /evidence="ECO:0007829|PDB:1LNS"
FT STRAND 611..615
FT /evidence="ECO:0007829|PDB:1LNS"
FT STRAND 618..628
FT /evidence="ECO:0007829|PDB:1LNS"
FT STRAND 631..645
FT /evidence="ECO:0007829|PDB:1LNS"
FT STRAND 650..657
FT /evidence="ECO:0007829|PDB:1LNS"
FT STRAND 659..662
FT /evidence="ECO:0007829|PDB:1LNS"
FT STRAND 666..670
FT /evidence="ECO:0007829|PDB:1LNS"
FT STRAND 673..687
FT /evidence="ECO:0007829|PDB:1LNS"
FT STRAND 690..692
FT /evidence="ECO:0007829|PDB:1LNS"
FT STRAND 705..710
FT /evidence="ECO:0007829|PDB:1LNS"
FT STRAND 714..718
FT /evidence="ECO:0007829|PDB:1LNS"
FT STRAND 723..730
FT /evidence="ECO:0007829|PDB:1LNS"
FT TURN 733..735
FT /evidence="ECO:0007829|PDB:1LNS"
FT STRAND 744..748
FT /evidence="ECO:0007829|PDB:1LNS"
FT HELIX 749..751
FT /evidence="ECO:0007829|PDB:1LNS"
FT STRAND 753..758
FT /evidence="ECO:0007829|PDB:1LNS"
SQ SEQUENCE 763 AA; 87697 MW; F89D81F88BDD7BEE CRC64;
MRFNHFSIVD KNFDEQLAEL DQLGFRWSVF WDEKKILKDF LIQSPSDMTA LQATAELDVI
EFLKSSIELD WEIFWNIALQ LLDFVPNFDF EIGKAFEYAK NSNLPQIEAE MTTENIISAF
YYLLCTRRKT GMILVEHWVS EGLLPLDNHY HFFNDKSLAT FDSSLLEREV LWVESPVDSE
QRGENDLIKI QIIRPKSTEK LPVVMTASPY HLGINDKAND LALHDMNVEL EEKTSHEIHV
EQKLPQKLSA KAKELPIVDK APYRFTHGWT YSLNDYFLTR GFASIYVAGV GTRSSDGFQT
SGDYQQIYSM TAVIDWLNGR ARAYTSRKKT HEIKASWANG KVAMTGKSYL GTMAYGAATT
GVEGLELILA EAGISSWYNY YRENGLVRSP GGFPGEDLDV LAALTYSRNL DGADFLKGNA
EYEKRLAEMT AALDRKSGDY NQFWHDRNYL INTDKVKADV LIVHGLQDWN VTPEQAYNFW
KALPEGHAKH AFLHRGAHIY MNSWQSIDFS ETINAYFVAK LLDRDLNLNL PPVILQENSK
DQVWTMMNDF GANTQIKLPL GKTAVSFAQF DNNYDDETFK KYSKDFNVFK KDLFENKANE
AVIDLELPSM LTINGPVELE LRLKLNDTKG FLSAQILDFG QKKRLEDKVR VKDFKVLDRG
RNFMLDDLVE LPLVESPYQL VTKGFTNLQN QSLLTVSDLK ADEWFTIKFE LQPTIYHLEK
ADKLRVILYS TDFEHTVRDN RKVTYEIDLS QSKLIIPIES VKN
