Q6ME13

PR
Gene name
lon
Protein name
Lon protease
Names
ATP-dependent protease La
Species
Protochlamydia amoebophila (strain UWE25)
KEGG Pathway
pcu:PC_RS02245
EC number
3.4.21.53: Serine endopeptidases
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

1-57 (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 Q6ME13

Entry ID Method Resolution Chain Position Source
AF-Q6ME13-F1 Predicted AlphaFoldDB

No variants for Q6ME13

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q6ME13

No associated diseases with Q6ME13

5 regional properties for Q6ME13

Type Name Position InterPro Accession
domain Lon protease, N-terminal domain 35 - 232 IPR003111
domain AAA+ ATPase domain 379 - 523 IPR003593
domain ATPase, AAA-type, core 383 - 519 IPR003959
active_site Peptidase S16, active site 731 - 739 IPR008268
domain Peptidase S16, Lon proteolytic domain 624 - 828 IPR008269

Functions

Description
EC Number 3.4.21.53 Serine endopeptidases
Subcellular Localization
  • Cytoplasm
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.

5 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
ATP hydrolysis activity Catalysis of the reaction: ATP + H2O = ADP + H+ phosphate. ATP hydrolysis is used in some reactions as an energy source, for example to catalyze a reaction or drive transport against a concentration gradient.
ATP-dependent peptidase activity Catalysis of the hydrolysis of peptide bonds, driven by ATP hydrolysis.
sequence-specific DNA binding Binding to DNA of a specific nucleotide composition, e.g. GC-rich DNA binding, or with a specific sequence motif or type of DNA e.g. promotor binding or rDNA binding.
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).

2 GO annotations of biological process

Name Definition
cellular response to heat Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a heat stimulus, a temperature stimulus above the optimal temperature for that organism.
protein quality control for misfolded or incompletely synthesized proteins The chemical reactions and pathways resulting in the breakdown of misfolded or attenuated proteins.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MLEEPIDALE TEFENALNSL EDNQLSKING QLPEQVHVFP LLRRPFFPGM AAPLVIEPGP
70 80 90 100 110 120
FYEVLKVVAK SDHKCVGLVL TRSEQAEIYK VGFSDLYQIG VLARVLRIIP MEQGGAQVIL
130 140 150 160 170 180
NMERRIKIEK PTSETKTLKA NVSYIEDDPI LTTELKAYAI SILSTIKELL KLNPLFKEEL
190 200 210 220 230 240
QIFLGHSDFT EPGKLADFAV ALTTASREEL QDVLETFDIR KRIDKALILL KKELDISILQ
250 260 270 280 290 300
HNINQKIEAT INKSQKDFFL REQLKTIKKE LGIERDDKSL DREKFEARLK ERVVPSDVMK
310 320 330 340 350 360
VITEELEKLS VLDMQSAEYS VVRGYLDWLT TIPWGIYSQE NHNLEEAEKI LAHDHYGLED
370 380 390 400 410 420
IKQRILEFIG VGKLAKGVRG SIICLVGPPG VGKTSIGKSI ARALNRKFYR FSVGGMRDEA
430 440 450 460 470 480
EIKGHRRTYV GAMPGKMIQA LKYCQTMNPV IMLDEVDKMG KSFQGDPASA LLEVLDPEQN
490 500 510 520 530 540
AEFLDHYLDV RCNLSEVLFI VTANVLDTIP EPLKDRMDIL RLSGYIMQEK LEIAKKYLIP
550 560 570 580 590 600
RNRKEMGLKA LEVSFTQEAL RSIINGYARE SGVRNLENLL KKILRKLAVN IVREQEEHDK
610 620 630 640 650 660
EQAKKKKSSR SKKPIAFVPT KHSITPSNLK DFLGKPVFTS DRFYERTPVG VCMGLAWTAM
670 680 690 700 710 720
GGATLYIESI KVAGEKTVMK LTGQAGDVMK ESAEIAWSYV HSSIHKYAPG YTFFEKSQVH
730 740 750 760 770 780
IHIPEGATPK DGPSAGITMV TSLLSLILDT PVLDNLGMTG ELTLTGRVLP IGGVKEKLVA
790 800 810 820 830
ARRSGLKVLI FPKDNLRDYE ELPEYIRKGI TVHFVDHYDQ VFKISFPNKH QMKLC