O31147 (LON_MYCSM) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Lon protease
EC=3.4.21.53

Alternative name(s):
ATP-dependent protease La

Gene names

Name:

lon

Organism

Mycobacterium smegmatis

Taxonomic identifier

1772 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium

Protein attributes

Sequence length	779 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner By similarity. Ref.1
Catalytic activity	Hydrolysis of proteins in presence of ATP.
Enzyme regulation	Stimulated by unfolded protein. Ref.1
Subunit structure	Homohexamer. Organized in a ring with a central cavity By similarity. Oligomerization is Mg2+-dependent. Ref.2
Subcellular location	Cytoplasm.
Induction	By heat shock By similarity. Ref.1
Sequence similarities	Belongs to the peptidase S16 family. Contains 1 Lon domain.

Ontologies

Keywords
Biological process	Stress response
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Hydrolase Protease Serine protease
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: UniProtKB-KW response to stress Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATP-dependent peptidase activity Inferred from electronic annotation. Source: InterPro serine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 779	779	Lon protease		PRO_0000076141
Regions
	Domain	6 – 185	180	Lon
	Nucleotide binding	352 – 359	8	ATP By similarity
Sites
	Active site	675	1
	Active site	718	1	By similarity
Experimental info
	Mutagenesis	675	1	S → A or T: Loss of activity. Ref.1
	Mutagenesis	675	1	S → C: Retains some activity. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	O31147 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: EA063D92BD26CD9F	FASTA	779	83,676
	10 20 30 40 50 60 MAEAKTVPVL FLNDSIVLPG MVVPIELDDA ARAAVDAARA SESGELLIAP RLEDRYPAYG 70 80 90 100 110 120 VLASIVQIGR LPNGDAAAVV RGERRAHIGS GTSGPGAALW VQVEEVTDPE PTDETKKLAG 130 140 150 160 170 180 EYKKLLLAML QRRDAWQIVD MVNKITDPSA LADTAGYASY LTGTQKRELL ETTDVDRRLS 190 200 210 220 230 240 LLIGWTGDHL AETEVNDKIA EDVRTGMEKQ QKEFLLRQQL AAIRKELGEL DDNGDGSSDD 250 260 270 280 290 300 YRARIEQADL PEKVREAALR EVGKLERASD QSPEGGWIRT WLDTVLDLPW NVRTEDSTDL 310 320 330 340 350 360 ARAREILDTD HHGLSDVKDR IVEYLAVRGA APQRGMAVVG GRGSGAVMVL AGPPGVGKTS 370 380 390 400 410 420 LGESVARALD RKFVRVALGG VRDEAEIRGH RRTYVGALPG RIVRAIGEAG SMNPVVLLDE 430 440 450 460 470 480 IDKVGSDYRG DPAAALLEVL DPAQNHTFRD HYLDLDLDLS DVVFLVTANV IENIPSALLD 490 500 510 520 530 540 RMELVEIDGY TADDKLAIAQ GFLLPRQRER GGLTSDEVTV TEAALRKIAA DYTREPGVRQ 550 560 570 580 590 600 FERLLAKAMR KAATKLADHP QAAPITIDEP DLVEYLGRPR FLPESAERTA VPGVATGLAV 610 620 630 640 650 660 TGLGGDVLYI EANSTEGEPG LQLTGQLGDV MKESAQIAMS YVRAHAKQLG VDPEALNRRI 670 680 690 700 710 720 HIHVPAGAVP KDGPSAGVTM VTALVSMATG RKVRGDVGMT GEVTLNGRVL PIGGVKQKLL 730 740 750 760 770 AAQRAGLSTV FIPQRNQPDL DDVPADVLDA LDVRPMTDVA DIIAAALEPA HEASTAAAA

References

[1]	"The lon protease from Mycobacterium smegmatis: molecular cloning, sequence analysis, functional expression, and enzymatic characterization." Roudiak S.G., Seth A., Knipfer N., Shrader T.E. Biochemistry 37:377-386(1998) [PubMed: 9425059] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, ENZYME REGULATION, MUTAGENESIS OF SER-675.
[2]	"Mg2+-linked oligomerization modulates the catalytic activity of the Lon (La) protease from Mycobacterium smegmatis." Rudyak S.G., Brenowitz M., Shrader T.E. Biochemistry 40:9317-9323(2001) [PubMed: 11478899] [Abstract] Cited for: SUBUNIT.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF030688 Genomic DNA. Translation: AAB86425.1.
3D structure databases
ProteinModelPortal	O31147.
SMR	O31147. Positions 592-769.
ModBase	Search...
Protein family/group databases
MEROPS	S16.001.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR003593. ATPase_AAA+_core. IPR003959. ATPase_AAA_core. IPR008269. Pept_S16_C. IPR004815. Pept_S16_lon. IPR003111. Pept_S16_N. IPR008268. Peptidase_S16_AS. IPR015947. PUA-like_domain. IPR020568. Ribosomal_S5_D2-typ_fold. [Graphical view]
Pfam	PF00004. AAA. 1 hit. PF02190. LON. 1 hit. PF05362. Lon_C. 1 hit. [Graphical view]
PIRSF	PIRSF001174. Lon_proteas. 1 hit.
SMART	SM00382. AAA. 1 hit. SM00464. LON. 1 hit. [Graphical view]
SUPFAM	SSF88697. PUA-like. 1 hit. SSF54211. Ribosomal_S5_D2-typ_fold. 1 hit.
TIGRFAMs	TIGR00763. Lon. 1 hit.
PROSITE	PS01046. LON_SER. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

LON_MYCSM

Accession

Primary (citable) accession number: O31147

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	January 1, 1998
Last modified:	January 25, 2012
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program