FUNCTION: Degrades short-lived regulatory and abnormal proteins in presence of ATP. Degrades the regulatory proteins rcsA and sulA. Hydrolyzes two ATPs for each peptide bond cleaved in the protein substrate (By similarity).
CATALYTIC ACTIVITY: Hydrolysis of proteins in presence of ATP.
SUBUNIT: Homotetramer (By similarity).
SUBCELLULAR LOCATION: Cytoplasm.
SIMILARITY: Belongs to the peptidase S16 family [view classification].
SIMILARITY: Contains 1 Lon domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AE013218; AAM68004.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_660793.1; -.

3D structure databases

SMR

Q8K988; 8-117, 491-584, 594-775.

ModBase

Q8K988.

Protein family/group databases

MEROPS

S16.001; -.

Enzyme and pathway databases

BioCyc

BAPH198804:BUSG461-MON; -.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0005524;	Molecular function: ATP binding (inferred from electronic annotation from InterPro).
GO:0004176;	Molecular function: ATP-dependent peptidase activity (inferred from electronic annotation from InterPro).
GO:0017111;	Molecular function: nucleoside-triphosphatase activity (inferred from electronic annotation from InterPro).
GO:0004252;	Molecular function: serine-type endopeptidase activity (inferred from electronic annotation from InterPro).
GO:0006510;	Biological process: ATP-dependent proteolysis (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR003593; AAA+_ATPase_core.
IPR003959; AAA_ATPase_core.
IPR001270; Chaprnin_clpA/B.
IPR008269; Pept_S16_C.
IPR004815; Pept_S16_lon.
IPR003111; Pept_S16_N.
IPR001984; Peptidase_S16.
IPR008268; Peptidase_S16_AS.
Graphical view of domain structure.

Pfam

PF00004; AAA; 1.
PF02190; LON; 1.
PF05362; Lon_C; 1.
Pfam graphical view of domain structure.

PRINTS

PR00300; CLPPROTEASEA.
PR00830; ENDOLAPTASE.

SMART

SM00382; AAA; 1.
SM00464; LON; 1.
SMART graphical view of domain structure.

TIGR00763; lon; 1.

PS01046; LON_SER; 1.

Genome annotation databases

GeneID

1005704; -.

GenomeReviews

AE013218_GR; BUsg_461.

KEGG

bas:BUsg461; -.

Phylogenomic databases

HOGENOM

Q8K988; -.

Genome annotation databases

CMR

Q8K988; BUsg_461.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

ATP-binding; Complete proteome; Cytoplasm; Hydrolase; Nucleotide-binding; Protease; Serine protease.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 777`	`777`	`ATP-dependent protease La.`	`PRO_0000076126`
`DOMAIN`	`10 202`	`193`	`Lon.`
`NP_BIND`	`356 363`	`8`	`ATP (Potential).`
`ACT_SITE`	`679 679`		`By similarity.`
`ACT_SITE`	`722 722`		`By similarity.`

Sequence information

Length: 777 AA [This is the length of the unprocessed precursor]

Molecular weight: 87755 Da [This is the MW of the unprocessed precursor]

CRC64: 768ACD8B06713DD2 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MNSERSERIK IPVLPLRDVV VYPHMVIPLF VGRKKSIHCI ETSMNNDKKI MLIAQKEASK 

        70         80         90        100        110        120 
DEPSTNDLFN IGTISSILQM LKLPDGTVKV LVEGLQRACI KNIESNGEHL VAEVELIISP 

       130        140        150        160        170        180 
TVIDKEQEVL IRTTVNQFES YIKLNKKIPS EILNTLSQTK NAEKLADTIA AHMPLKLADK 

       190        200        210        220        230        240 
QSVLEIYNVN ERLEFLMAIM ETEIDLLKVE KRIRNRVKKQ MEKSQREYYL NEQIKAIQKE 

       250        260        270        280        290        300 
LGDMDEIPDE NKILKRKIKS LKMPKEAKEK TESELQKLKM MSPMSAEATV VRSYIDWMIQ 

       310        320        330        340        350        360 
VPWNIKTKIK KDIQEAKKIL DIDHFGLEKV KERILEYLAV QSRTNKVKGP ILCLIGPPGV 

       370        380        390        400        410        420 
GKTSLGKSIA KSTGRKYVRM ALGGIRDEAE IRGHRRTYIG SMPGKLMQKM VKAKVKNPLF 

       430        440        450        460        470        480 
LLDEIDKMSC DIRVDPASAL LEVLDPEQNI NFNDHYLEVD YDLSDVMFVA TSNSMNIPAP 

       490        500        510        520        530        540 
LLDRMEIIRL SGYTENEKLN IAKCYLYPKQ MERNALKRNE LIITDCAIIS IIQYYTREAG 

       550        560        570        580        590        600 
VRSLEREISK ICRKVVKLLI LNKSLKKIEI NSKNLKKFLG IKRFDYGKTN NLNQIGQVVG 

       610        620        630        640        650        660 
LAWTEVGGEL LTIETACVSG KGKLTYTGSL GEVMQESIQA ALTVVRSQAK KLGIKKDFHE 

       670        680        690        700        710        720 
KHDIHVHVPE GATPKDGPSA GIAMCTAIVS SLTKNPVKSN IAMTGEITLQ GRVLTIGGLK 

       730        740        750        760        770 
EKLLAAHRGG VKTVLIPYEN KRNLEEIPKN IIEGLTIYPV KNIEEVLKIA LENTPYV

Q8K988 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools