Descriptions

Auto (lmo1076) is one of autolysins and is essential for listerial entry into numerous cell lines. The α helix in the N-terminal region (60-72) of Auto physically blocks the substrate-binding cleft of the protein.

Autoinhibitory domains (AIDs)

Target domain

89-243 (Peptidoglycan hydrolase domain)

Relief mechanism

Cleavage

Assay

Deletion assay, Structural analysis

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

3 structures for Q8Y842

Entry ID Method Resolution Chain Position Source
3FI7 X-ray 235 A A 52-243 PDB
5JQC X-ray 215 A A 233-491 PDB
AF-Q8Y842-F1 Predicted AlphaFoldDB

No variants for Q8Y842

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q8Y842

No associated diseases with Q8Y842

1 regional properties for Q8Y842

Type Name Position InterPro Accession
domain Mannosyl-glycoprotein endo-beta-N-acetylglucosamidase-like domain 79 - 243 IPR002901

Functions

Description
EC Number
Subcellular Localization
PANTHER Family PTHR33308 PEPTIDOGLYCAN HYDROLASE FLGJ
PANTHER Subfamily PTHR33308:SF9 PEPTIDOGLYCAN HYDROLASE FLGJ
PANTHER Protein Class metabolite interconversion enzyme
hydrolase
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
extracellular region The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite.

1 GO annotations of molecular function

Name Definition
amidase activity Catalysis of the reaction: a monocarboxylic acid amide + H2O = a monocarboxylate + NH3.

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
MIKKVFHFIL VLMLSVSIIP LFHAKAAETT NGVDSSEQED NTEVAREEMP PESEEPVFSL
70 80 90 100 110 120
EQNRDDAMAA LVVPQTRNSF LRAASTPTFQ QTFINSISTQ AMDLCKKYNL YPSVMIAQAA
130 140 150 160 170 180
LESNWGRSEL GKAPNYNLFG IKGSYNGKSV TMKTWEYSDS KGWYQINANF AKYPSHKESL
190 200 210 220 230 240
EDNAKKLRNG PSWDSSYYKG AWRENAKTYK DATAWLQGRY ATDNTYASKL NTLISSYNLT
250 260 270 280 290 300
QYDTLYDTIK QQKNVSEDAK VVKADGHGVY SGIYNTSAAS AKKLSTGAPY NNKDVKILKE
310 320 330 340 350 360
GTTSRGTWVQ FSLNNKVIGW MDKRAFVYYP KATNVKTLNL TGKITAGSTN GLWSEVPGTV
370 380 390 400 410 420
NAKKLATTAG AYQNKDAKII KQGQISGRTY YQFQVGGKTI GWLDARAFHV YDKIQSQSNV
430 440 450 460 470 480
NWNRTILNAD KHGVYSGVYN TSSSSMNKLS TGAKYNNKKV KVIKQAKTAR GTWYQFQVNG
490 500 510 520 530 540
KTVGWMDYRA FFDTITSQKT MNKTVTVGNA TNHGVFDGVY RTSPTVKRIS LGKPYNNKKV
550 560 570
KVLKEAVTDH ATWVQFKYGN TTAWMDKKAF KY