Descriptions

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

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for Q0HS08

Entry ID Method Resolution Chain Position Source
AF-Q0HS08-F1 Predicted AlphaFoldDB

No variants for Q0HS08

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q0HS08

No associated diseases with Q0HS08

4 regional properties for Q0HS08

Type Name Position InterPro Accession
domain Peptidyl-prolyl cis-trans isomerase, PpiC-type 173 - 274 IPR000297-1
domain Peptidyl-prolyl cis-trans isomerase, PpiC-type 283 - 383 IPR000297-2
domain SurA N-terminal 27 - 143 IPR015391
conserved_site Peptidyl-prolyl cis-trans isomerase, PpiC-type, conserved site 322 - 343 IPR023058

Functions

Description
EC Number 5.2.1.8 Cis-trans isomerases
Subcellular Localization
  • Periplasm
  • Is capable of associating with the outer membrane
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.

3 GO annotations of molecular function

Name Definition
peptide binding Binding to a peptide, an organic compound comprising two or more amino acids linked by peptide bonds.
peptidyl-prolyl cis-trans isomerase activity Catalysis of the reaction: peptidyl-proline (omega=180) = peptidyl-proline (omega=0).
unfolded protein binding Binding to an unfolded protein.

3 GO annotations of biological process

Name Definition
Gram-negative-bacterium-type cell outer membrane assembly The assembly of an outer membrane of the type formed in Gram-negative bacteria. This membrane is enriched in polysaccharide and protein, and the outer leaflet of the membrane contains specific lipopolysaccharide structures.
protein folding The process of assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure.
protein stabilization Any process involved in maintaining the structure and integrity of a protein and preventing it from degradation or aggregation.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MKPSKHLIFA LFALAISQPT MAAPQPIDRV AVQINDGIVL ESEITNMIDT VKANARAANQ
70 80 90 100 110 120
SLPSDSALRT QVIERLILTR LQLQMADRIG LHIGDLQLDQ AIENIAREQK MTVAQMQQKI
130 140 150 160 170 180
ESEGLSFGQY REQLREEITL GEIQRIQVQR RIQVSPQEIT GLVKLIQEQG MKDVEYQIGH
190 200 210 220 230 240
ILIDVPNNPN SEQLEASSKR ANAVLERLKS GEDFRRTAIA SSSGPKALEG GIWDYMNINE
250 260 270 280 290 300
MPTLFAEVIN GAKKGDIIGP IKSGAGFHII KIMDARGLQT KEIEEVRARH ILLKPSPILS
310 320 330 340 350 360
EDRAKAMLEQ FLKQIRSGEA KFEDLARQYS EDPGSATKGG ELGWAEPSIY VPEFAQTLNS
370 380 390 400 410 420
LSPDQISEPF RTTHGWHITQ LEERRKTDAT DQFNTNRAHQ LIFRRKFNEE LQNWLDEMRA
430
DAYIEVFQPE SNRG