P21165

PR
Gene name
pepQ (b3847, JW3823)
Protein name
Xaa-Pro dipeptidase
Names
X-Pro dipeptidase, Imidodipeptidase, Proline dipeptidase, Prolidase
Species
Escherichia coli (strain K12)
KEGG Pathway
eco:b3847
EC number
3.4.13.9: Dipeptidases
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

1-44 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

2 structures for P21165

Entry ID Method Resolution Chain Position Source
4QR8 X-ray 200 A A/B 1-443 PDB
AF-P21165-F1 Predicted AlphaFoldDB

No variants for P21165

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P21165

No associated diseases with P21165

3 regional properties for P21165

Type Name Position InterPro Accession
domain Peptidase M1, membrane alanine aminopeptidase 216 - 434 IPR014782
domain ERAP1-like C-terminal domain 507 - 813 IPR024571
domain Aminopeptidase N-like, N-terminal domain 11 - 180 IPR045357

Functions

Description
EC Number 3.4.13.9 Dipeptidases
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.

7 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.
dipeptidase activity Catalysis of the hydrolysis of a dipeptide.
manganese ion binding Binding to a manganese ion (Mn).
metallodipeptidase activity Catalysis of the hydrolysis of a dipeptide by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions.
peptidase activity Catalysis of the hydrolysis of a peptide bond. A peptide bond is a covalent bond formed when the carbon atom from the carboxyl group of one amino acid shares electrons with the nitrogen atom from the amino group of a second amino acid.
phosphoric triester hydrolase activity Catalysis of the hydrolysis of a phosphoric triester.
proline dipeptidase activity Catalysis of the reaction: H2O + a dipeptide with proline at the C-terminal <=> L-proline + a standard alpha amino acid.

2 GO annotations of biological process

Name Definition
peptide catabolic process The chemical reactions and pathways resulting in the breakdown of peptides, compounds of 2 or more (but usually less than 100) amino acids where the alpha carboxyl group of one is bound to the alpha amino group of another.
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
MESLASLYKN HIATLQERTR DALARFKLDA LLIHSGELFN VFLDDHPYPF KVNPQFKAWV
70 80 90 100 110 120
PVTQVPNCWL LVDGVNKPKL WFYLPVDYWH NVEPLPTSFW TEDVEVIALP KADGIGSLLP
130 140 150 160 170 180
AARGNIGYIG PVPERALQLG IEASNINPKG VIDYLHYYRS FKTEYELACM REAQKMAVNG
190 200 210 220 230 240
HRAAEEAFRS GMSEFDINIA YLTATGHRDT DVPYSNIVAL NEHAAVLHYT KLDHQAPEEM
250 260 270 280 290 300
RSFLLDAGAE YNGYAADLTR TWSAKSDNDY AQLVKDVNDE QLALIATMKA GVSYVDYHIQ
310 320 330 340 350 360
FHQRIAKLLR KHQIITDMSE EAMVENDLTG PFMPHGIGHP LGLQVHDVAG FMQDDSGTHL
370 380 390 400 410 420
AAPAKYPYLR CTRILQPGMV LTIEPGIYFI ESLLAPWREG QFSKHFNWQK IEALKPFGGI
430 440
RIEDNVVIHE NNVENMTRDL KLA