Descriptions

Mycosin-1 protease (MycP1) is a serine protease anchored to the inner membrane of Mycobacterium smegmatis, and is essential in virulence factor secretion through the ESX-1 type VII secretion system (T7SS). MycP1's autoinhibition involves a putative propeptide that wraps around the protease domain in a non-classical manner. Although not directly inhibiting proteolytic activity, the propeptide contributes to conformational stability of the active site, influencing MycP1's function.

Autoinhibitory domains (AIDs)

Target domain

66-389 (Protease domain)

Relief mechanism

Assay

Structural analysis, Deletion assay

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

5 structures for A0QNL1

Entry ID Method Resolution Chain Position Source
4J94 X-ray 186 A A 24-407 PDB
4KB5 X-ray 215 A A 24-422 PDB
4KPG X-ray 215 A A 24-407 PDB
4M1Z X-ray 225 A PDB
AF-A0QNL1-F1 Predicted AlphaFoldDB

No variants for A0QNL1

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A0QNL1

No associated diseases with A0QNL1

1 regional properties for A0QNL1

Type Name Position InterPro Accession
domain Peptidase S8/S53 domain 83 - 381 IPR000209

Functions

Description
EC Number 3.4.21.- Serine endopeptidases
Subcellular Localization
  • Cell membrane ; Single-pass membrane protein
  • Cell wall-associated
PANTHER Family PTHR42884 PROPROTEIN CONVERTASE SUBTILISIN/KEXIN-RELATED
PANTHER Subfamily PTHR42884:SF14 NEUROENDOCRINE CONVERTASE 1
PANTHER Protein Class serine protease
protein modifying enzyme
PANTHER Pathway Category Endothelin signaling pathway
furin
Alzheimer disease-presenilin pathway
Furin
Alzheimer disease-amyloid secretase pathway
Furin

1 GO annotations of cellular component

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

1 GO annotations of molecular function

Name Definition
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
MQRVAVMVLA VLLALFSAPP AWAIDPPVID AGAVPPDETG PDQPTEQRKI CATPTVMPNS
70 80 90 100 110 120
NFADRPWAND YLRIQEAQKF ATGAGVTVAV IDTGVNGSPR VPAEPGGDFV DAAGNGMSDC
130 140 150 160 170 180
DAHGTMTAAI IGGRPSPTDG FVGMAPDVRL LSLRQTSVAF QPKGARQDPN DPNTTQTAGS
190 200 210 220 230 240
IRSLARSVVH AANLGAQVIN ISEAACYKVT RRIDETSLGA AINYAVNVKG AVIVVAAGNT
250 260 270 280 290 300
GQDCSQNPPP DPSVPSDPRG WREVQTIVSP AWYDPLVLTV GSIGQNGQPS NFSMSGPWVG
310 320 330 340 350 360
AAAPGENLTS LGYDGQPVNA TPGEDGPVPL NGTSFSAAYV SGLAALVKQR FPDLTPAQII
370 380 390 400 410 420
NRITATARHP GGGVDNYVGA GVIDPVAALT WEIPDGPEKA PFRVKEVPPP VYIPPPDRGP
430 440
ITAVVIAGAT LAFALGIGAL ARRALRRKQ