P24555

PR
Gene name
ptrB (tlp, b1845, JW1834)
Protein name
Protease 2
Names
Oligopeptidase B, Protease II
Species
Escherichia coli (strain K12)
KEGG Pathway
eco:b1845
EC number
3.4.21.83: Serine endopeptidases
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

91-162 (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 P24555

Entry ID Method Resolution Chain Position Source
AF-P24555-F1 Predicted AlphaFoldDB

No variants for P24555

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P24555

No associated diseases with P24555

3 regional properties for P24555

Type Name Position InterPro Accession
domain Peptidase S9, prolyl oligopeptidase, catalytic domain 463 - 676 IPR001375
active_site Peptidase S9, serine active site 507 - 537 IPR002471
domain Peptidase S9A, N-terminal domain 3 - 403 IPR023302

Functions

Description
EC Number 3.4.21.83 Serine endopeptidases
Subcellular Localization
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.

2 GO annotations of molecular function

Name Definition
oligopeptidase activity Catalysis of the hydrolysis of a peptide bond in an oligopeptide, i.e. a molecule containing a small number (2 to 20) of amino acid residues connected by peptide bonds.
serine-type endopeptidase activity Catalysis of the hydrolysis of internal, alpha-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
MLPKAARIPH AMTLHGDTRI DNYYWLRDDT RSQPEVLDYL QQENSYGHRV MASQQALQDR
70 80 90 100 110 120
ILKEIIDRIP QREVSAPYIK NGYRYRHIYE PGCEYAIYQR QSAFSEEWDE WETLLDANKR
130 140 150 160 170 180
AAHSEFYSMG GMAITPDNTI MALAEDFLSR RQYGIRFRNL ETGNWYPELL DNVEPSFVWA
190 200 210 220 230 240
NDSWIFYYVR KHPVTLLPYQ VWRHAIGTPA SQDKLIYEEK DDTYYVSLHK TTSKHYVVIH
250 260 270 280 290 300
LASATTSEVR LLDAEMADAE PFVFLPRRKD HEYSLDHYQH RFYLRSNRHG KNFGLYRTRM
310 320 330 340 350 360
RDEQQWEELI PPRENIMLEG FTLFTDWLVV EERQRGLTSL RQINRKTREV IGIAFDDPAY
370 380 390 400 410 420
VTWIAYNPEP ETARLRYGYS SMTTPDTLFE LDMDTGERRV LKQTEVPGFY AANYRSEHLW
430 440 450 460 470 480
IVARDGVEVP VSLVYHRKHF RKGHNPLLVY GYGSYGASID ADFSFSRLSL LDRGFVYAIV
490 500 510 520 530 540
HVRGGGELGQ QWYEDGKFLK KKNTFNDYLD ACDALLKLGY GSPSLCYAMG GSAGGMLMGV
550 560 570 580 590 600
AINQRPELFH GVIAQVPFVD VVTTMLDESI PLTTGEFEEW GNPQDPQYYE YMKSYSPYDN
610 620 630 640 650 660
VTAQAYPHLL VTTGLHDSQV QYWEPAKWVA KLRELKTDDH LLLLCTDMDS GHGGKSGRFK
670 680
SYEGVAMEYA FLVALAQGTL PATPAD