P43669

PR
Gene name
prc (STM1845)
Protein name
Tail-specific protease
Names
C-terminal-processing peptidase, PRC protein, Protease Re
Species
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
KEGG Pathway
stm:STM1845
EC number
3.4.21.102: Serine endopeptidases
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

3-82 (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 P43669

Entry ID Method Resolution Chain Position Source
AF-P43669-F1 Predicted AlphaFoldDB

No variants for P43669

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P43669

No associated diseases with P43669

4 regional properties for P43669

Type Name Position InterPro Accession
domain PDZ domain 238 - 323 IPR001478
domain Tail specific protease 326 - 531 IPR005151
domain Tail specific protease, C-terminal 536 - 667 IPR020992
domain Tail specific protease, N-terminal domain 49 - 232 IPR040573

Functions

Description
EC Number 3.4.21.102 Serine endopeptidases
Subcellular Localization
  • Cell inner membrane ; Peripheral membrane protein ; Periplasmic side
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
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.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.

2 GO annotations of molecular function

Name Definition
endopeptidase activity Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain.
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).

2 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.
signal transduction The cellular process in which a signal is conveyed to trigger a change in the activity or state of a cell. Signal transduction begins with reception of a signal (e.g. a ligand binding to a receptor or receptor activation by a stimulus such as light), or for signal transduction in the absence of ligand, signal-withdrawal or the activity of a constitutively active receptor. Signal transduction ends with regulation of a downstream cellular process, e.g. regulation of transcription or regulation of a metabolic process. Signal transduction covers signaling from receptors located on the surface of the cell and signaling via molecules located within the cell. For signaling between cells, signal transduction is restricted to events at and within the receiving cell.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MNTFFRLTAL AGLLALAGQS FAVEDITRAD QIPVLKEETQ HATVSERVTS RFTRSHYRQF
70 80 90 100 110 120
DLDEAFSAKI FDRYLNLLDY SHNVLLASDV EQFAKKKTVL GDELRTGKLD VFYDLYNLAQ
130 140 150 160 170 180
KRRFERYQYA LKVLERPMDF TGNDTFNLDR SKAPWPKDEA ELNALWDGKV KFDELSLKLT
190 200 210 220 230 240
GKSDKEIRET LTRRYKFAIR RLAQTNSEDV FSLAMTAFAR EIDPHTNYLS PRNTEQFNTE
250 260 270 280 290 300
MSLSLEGIGA VLQMDDDYTV INSLVAGGPA AKSKSISVGD RIVGVGQAGK PMVDVIGWRL
310 320 330 340 350 360
DDVVALIKGP KGSKVRLEIL PAGKGTKTRI ITLTRERIRL EDRAVKMSVK TVGKEKVGVL
370 380 390 400 410 420
DIPGFYVGLT DDVKVQLQKL EKQNVNSIVI DLRSNGGGAL TEAVSLSGLF IPSGPIVQVR
430 440 450 460 470 480
DNNGKVREDS DTDGVVYYKG PLVVLVDRFS ASASEIFAAA MQDYGRALIV GEPTFGKGTV
490 500 510 520 530 540
QQYRSLNRIY DQMLRPEWPA LGSVQYTIQK FYRVNGGSTQ RKGVTPDIIM PTGNEETETG
550 560 570 580 590 600
EKFEDNALPW DSIDAAKYVK SDDLAPFGPE LLKEHNARIA KDPEFQYIMK DIARFNAMKD
610 620 630 640 650 660
KRNIVSLNYA QREKENNEED ALRLARINDR FKREGKPLLK KLDDLPKDYQ EPDPYLDETV
670 680
KIALDLAHLE KEKPAEQAAA NK