O84348

PR
Gene name
lon
Protein name
Lon protease
Names
ATP-dependent protease La
Species
Chlamydia trachomatis (strain D/UW-3/Cx)
KEGG Pathway
ctr:CT_344
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)

1-67 (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 O84348

Entry ID Method Resolution Chain Position Source
AF-O84348-F1 Predicted AlphaFoldDB

No variants for O84348

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for O84348

No associated diseases with O84348

5 regional properties for O84348

Type Name Position InterPro Accession
domain Lon protease, N-terminal domain 41 - 237 IPR003111
domain AAA+ ATPase domain 384 - 529 IPR003593
domain ATPase, AAA-type, core 388 - 524 IPR003959
active_site Peptidase S16, active site 721 - 729 IPR008268
domain Peptidase S16, Lon proteolytic domain 612 - 818 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
MNSTNNTDSQ NLDPNASEVE KLLDESAEAE EKVDDHTPPS ELFILPLNKR PFFPGMAAPL
70 80 90 100 110 120
LIEAGPHYEV LTLLAKSSQK HIGLVLTKKE DANTLKVGFN QLHRVGVSAR ILRIMPIEGG
130 140 150 160 170 180
SAQVLLSIED RIRIVKPIQD KYLKAKVSYH KENKELTEEL KAYSISIVSI IKDLLKLNPL
190 200 210 220 230 240
FKEELQIFLG HSDFTEPGKL ADFSVALTTA TREELQEILE TTDMHDRIDK ALVLLKKELD
250 260 270 280 290 300
LSRLQSSINQ KIEATITKSQ KEFFLKEQLK TIKKELGLEK DDHAVDLEKF MERFNKRDVP
310 320 330 340 350 360
QYAMDVIQDE MDKLQTLETS SAEYAVCRNY LDWLTIVPWG IQTKEYHDLK KAESILNKDH
370 380 390 400 410 420
YGLEDIKQRI LELISVGKLA NGMKGSIICL VGPPGVGKTS IGRSIAKVLH RKFFRFSVGG
430 440 450 460 470 480
MRDEAEIKGH RRTYIGAMPG KLVQALKQSQ IMNPVIMIDE VDKIGSSYHG DPASALLEVL
490 500 510 520 530 540
DPEQNKDFLD HYLDVRVDLS NVLFILTANV LDSIPDPLLD RMEVLRLSGY ILEEKLQIAT
550 560 570 580 590 600
KYLVPRARKE MGLSAQNVTF QPEALKHMIN NYAREAGVRT LNENIKKVLR KVALKIVQNQ
610 620 630 640 650 660
EKNLSKKSRF TITPKNLQDY LGKPVFSSDR FYEKTPVGVA TGLAWTSLGG ATLYIESVQV
670 680 690 700 710 720
PSSSGKADMH LTGQAGDVMK ESSQIAWTYL HSALERYAPG QPFFEKSQVH IHIPEGATPK
730 740 750 760 770 780
DGPSAGITMV TSLLSLLLDV PVLNNLGMTG ELTLTGRVLG IGGIREKLIA ARRSKLNILI
790 800 810
FPEDNRRDYD ELPAYLKKGL KVHFVTHYDD VFKIAFPGV