A9R289

PR
Gene name
eco
Protein name
Ecotin
Names
Species
Yersinia pestis bv Antiqua (strain Angola)
KEGG Pathway
ypg:YpAngola_A1316
EC number
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

1-154 (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 A9R289

Entry ID Method Resolution Chain Position Source
AF-A9R289-F1 Predicted AlphaFoldDB

No variants for A9R289

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A9R289

No associated diseases with A9R289

No regional properties for A9R289

Type Name Position InterPro Accession
No domain, repeats, and functional sites for A9R289

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
periplasmic space The region between the inner (cytoplasmic) and outer membrane (Gram-negative Bacteria) or cytoplasmic membrane and cell wall (Fungi and Gram-positive Bacteria).

1 GO annotations of molecular function

Name Definition
serine-type endopeptidase inhibitor activity Binds to and stops, prevents or reduces the activity of serine-type endopeptidases, enzymes that catalyze the hydrolysis of nonterminal peptide bonds in a polypeptide chain; a serine residue (and a histidine residue) are at the active center of the enzyme.

No GO annotations of biological process

Name Definition
No GO annotations for biological process

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MKKCSIILAS VLLATSINAI ADTPTPLNQQ QPLEKIAPYP QAEKGMSRQV IFLEPQKDES
70 80 90 100 110 120
RFKVELLIGK TLNVDCNRHM LGGNLETRTL SGWGFDYLVM DKISQPASTM MACPEDSKPQ
130 140 150 160
VKFVTANLGD AAMQRYNSRL PIVVYVPQGV EVKYRIWEAG EDIRSAQVK