P24171

PR
Gene name
dcp
Protein name
Dipeptidyl carboxypeptidase
Names
Peptidyl-dipeptidase Dcp
Species
Escherichia coli (strain K12)
KEGG Pathway
eco:b1538
EC number
3.4.15.5: Peptidyl-dipeptidases
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

1-67 (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 P24171

Entry ID Method Resolution Chain Position Source
1Y79 X-ray 200 A 1 2-681 PDB
AF-P24171-F1 Predicted AlphaFoldDB

No variants for P24171

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P24171

No associated diseases with P24171

1 regional properties for P24171

Type Name Position InterPro Accession
domain Peptidase M3A/M3B catalytic domain 230 - 678 IPR001567

Functions

Description
EC Number 3.4.15.5 Peptidyl-dipeptidases
Subcellular Localization
  • Cytoplasm
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
outer membrane-bounded periplasmic space The region between the inner (cytoplasmic or plasma) membrane and outer membrane of organisms with two membranes such as Gram negative bacteria. These periplasmic spaces are relatively thick and contain a thin peptidoglycan layer (PGL), also referred to as a thin cell wall.

4 GO annotations of molecular function

Name Definition
carboxypeptidase activity Catalysis of the hydrolysis of a single C-terminal amino acid residue from a polypeptide chain.
metal ion binding Binding to a metal ion.
metalloendopeptidase activity Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain 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.
metallopeptidase activity Catalysis of the hydrolysis of peptide bonds 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.

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
MTTMNPFLVQ STLPYLAPHF DQIANHHYRP AFDEGMQQKR AEIAAIALNP QMPDFNNTIL
70 80 90 100 110 120
ALEQSGELLT RVTSVFFAMT AAHTNDELQR LDEQFSAELA ELANDIYLNG ELFARVDAVW
130 140 150 160 170 180
QRRESLGLDS ESIRLVEVIH QRFVLAGAKL AQADKAKLKV LNTEAATLTS QFNQRLLAAN
190 200 210 220 230 240
KSGGLVVNDI AQLAGMSEQE IALAAEAARE KGLDNKWLIP LLNTTQQPAL AEMRDRATRE
250 260 270 280 290 300
KLFIAGWTRA EKNDANDTRA IIQRLVEIRA QQATLLGFPH YAAWKIADQM AKTPEAALNF
310 320 330 340 350 360
MREIVPAARQ RASDELASIQ AVIDKQQGGF SAQPWDWAFY AEQVRREKFD LDEAQLKPYF
370 380 390 400 410 420
ELNTVLNEGV FWTANQLFGI KFVERFDIPV YHPDVRVWEI FDHNGVGLAL FYGDFFARDS
430 440 450 460 470 480
KSGGAWMGNF VEQSTLNKTH PVIYNVCNYQ KPAAGEPALL LWDDVITLFH EFGHTLHGLF
490 500 510 520 530 540
ARQRYATLSG TNTPRDFVEF PSQINEHWAT HPQVFARYAR HYQSGAAMPD ELQQKMRNAS
550 560 570 580 590 600
LFNKGYEMSE LLSAALLDMR WHCLEENEAM QDVDDFELRA LVAENMDLPA IPPRYRSSYF
610 620 630 640 650 660
AHIFGGGYAA GYYAYLWTQM LADDGYQWFV EQGGLTRENG LRFREAILSR GNSEDLERLY
670 680
RQWRGKAPKI MPMLQHRGLN I