P69965

PR
Gene name
psaB (YPO1304, y2881, YP_1288)
Protein name
Chaperone protein PsaB
Names
Species
Yersinia pestis
KEGG Pathway
ypm:YP_1288
EC number
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

42-180 (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 P69965

Entry ID Method Resolution Chain Position Source
AF-P69965-F1 Predicted AlphaFoldDB

No variants for P69965

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P69965

No associated diseases with P69965

3 regional properties for P69965

Type Name Position InterPro Accession
domain Pili assembly chaperone, N-terminal 45 - 173 IPR016147
domain Pili assembly chaperone, C-terminal 195 - 265 IPR016148
conserved_site Pili assembly chaperone, conserved site 117 - 134 IPR018046

Functions

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

1 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.

No GO annotations of molecular function

Name Definition
No GO annotations for molecular function

2 GO annotations of biological process

Name Definition
cell wall organization A process that results in the assembly, arrangement of constituent parts, or disassembly of the cell wall, the rigid or semi-rigid envelope lying outside the cell membrane of plant, fungal and most prokaryotic cells, maintaining their shape and protecting them from osmotic lysis.
chaperone-mediated protein folding The process of inhibiting aggregation and assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure that is dependent on interaction with a chaperone.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MKNLFFSAYK KVFSYITSIV IFMVSLPYAY SQDVVVNTTK HLFTVKIGTT RVIYPSSSTK
70 80 90 100 110 120
GVSVSVANPQ DYPILVQTQV KDEDKTSPAP FIVTPPLFRL DAGLQGRVRI IRTGGKFPED
130 140 150 160 170 180
RETLQWLCLT GIPPKNGDAW GNTQNNPKNS SPTMDIQMSI STCIKLLFRP DKVKGDPTDS
190 200 210 220 230 240
ADSLTWRYKG NYLEVNNPTP FYMNFYSLRI GDEKINLSDL GSKDEIKNGS YVPPFSSRDF
250 260 270
IIPVKNKGKA TEVFWQVIND NGGVSREFKS TVQ