B3WEZ5

PR
Gene name
pepX
Protein name
Xaa-Pro dipeptidyl-peptidase
Names
X-Pro dipeptidyl-peptidase, X-prolyl-dipeptidyl aminopeptidase, X-PDAP
Species
Lacticaseibacillus casei (strain BL23) (Lactobacillus casei)
KEGG Pathway
lcb:LCABL_18670
EC number
3.4.14.11: Dipeptidyl-peptidases and tripeptidyl-peptidases
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

224-305 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for B3WEZ5

Entry ID Method Resolution Chain Position Source
AF-B3WEZ5-F1 Predicted AlphaFoldDB

No variants for B3WEZ5

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for B3WEZ5

No associated diseases with B3WEZ5

3 regional properties for B3WEZ5

Type Name Position InterPro Accession
domain Xaa-Pro dipeptidyl-peptidase-like domain 200 - 523 IPR000383
domain Xaa-Pro dipeptidyl-peptidase, C-terminal 537 - 792 IPR013736
domain X-Prolyl dipeptidyl aminopeptidase PepX, N-terminal domain 1 - 155 IPR015251

Functions

Description
EC Number 3.4.14.11 Dipeptidyl-peptidases and tripeptidyl-peptidases
Subcellular Localization
  • Cytoplasm
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.

3 GO annotations of molecular function

Name Definition
aminopeptidase activity Catalysis of the hydrolysis of a single N-terminal amino acid residue from a polypeptide chain.
dipeptidyl-peptidase activity Catalysis of the hydrolysis of N-terminal dipeptides from a polypeptide chain.
serine-type peptidase activity Catalysis of the hydrolysis of peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine).

1 GO annotations of biological process

Name Definition
proteolysis The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MKLNQFARLT PDFKVQVAEL KQIGLQADPD DAFSQSATDL FNAFFPEAYT LAAKEDKLAQ
70 80 90 100 110 120
VAVNMDQTLA AWLAKKPSKM TRRDFYNVAL QLLGFEAFTD FDLNDPFKMM TATKLPSLDH
130 140 150 160 170 180
DLTSTADLLK AVYLLLNTRT KHLVSYLDDL ANRGFLKDFQ KKQKKPTHLL FNGKVQQVFD
190 200 210 220 230 240
ARQAVREVVW IESDMDTDHD GQRDLLEATI YRPKATDQGL KVPVLFTANP YFHGTNDVTA
250 260 270 280 290 300
VTHVPETTLA VKTHGASKAE VTANPEEPAN LPHHPVNGEA TQAEAYAEEN SMYAFNDYFL
310 320 330 340 350 360
ARGFAVVYSA GVGTRYSDGF RTTGGPEETD GAVAVIEWLT GKRRAFTNRT DGITIKAWWS
370 380 390 400 410 420
TGLVAMTGKS YLATLAMAAA TTGVDGLKTI VADAGISSWY DYYRENGLVV APGGFQGEDA
430 440 450 460 470 480
DVLAVDTFSR QKSGGDLINI KQAWEKHLAT ITHDQDRTTG AYNTWWDARN YRKNANKVKA
490 500 510 520 530 540
DVVLIHGLND WNVKPTNAIK FWEAIADLPI QKKLVLHQGQ HVYVHNVRSL DFLDMMNLWL
550 560 570 580 590 600
THELLGEANG AEDVLPNVVV QDNVAVQTWS AYQNFASPAA EHVTNTRNLK TDFEAATDQF
610 620 630 640 650 660
TDHATATFNA QHDTSASFET AIITPNSAYA NSRLWLTQPP LERDQTLEGI PHLELTLAID
670 680 690 700 710 720
APTGILSVRL IDLGMAKRFG ETAATVALNG LQLGFDYKTT DILEFKPTAK PTPSKLISLG
730 740 750 760 770 780
HINLQNPKNA YEVQRITPGQ PFHISLDLQP THYHLPAGRQ LALVIHGADM AQTIRPIKTT
790
HYQIDLANSS ITLPYRI