NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Madrid E;
DOI=10.1038/24094; PubMed=9823893 [NCBI, ExPASy, EBI, Israel, Japan]
Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T., Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H., Kurland C.G.;
"The genome sequence of Rickettsia prowazekii and the origin of mitochondria.";
Nature 396:133-140(1998).

Comments

FUNCTION: Degrades short-lived regulatory and abnormal proteins in presence of ATP. 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 (By similarity).
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

AJ235271; CAA14907.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A71704; A71704.

RefSeq

NP_220831.1; -.

3D structure databases

ModBase

Q9ZD92.

Protein family/group databases

MEROPS

S16.001; -.

Enzyme and pathway databases

BioCyc

RPRO272947:RP450-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

883360; -.

GenomeReviews

AJ235269_GR; RP450.

KEGG

rpr:RP450; -.

Phylogenomic databases

HOGENOM

Q9ZD92; -.

Genome annotation databases

CMR

Q9ZD92; RP450.

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`	`1 784`	`784`	`ATP-dependent protease La.`	`PRO_0000076145`
`DOMAIN`	`5 205`	`201`	`Lon.`
`NP_BIND`	`356 363`	`8`	`ATP (Potential).`
`ACT_SITE`	`679 679`		`By similarity.`
`ACT_SITE`	`722 722`		`By similarity.`

Sequence information

Length: 784 AA [This is the length of the unprocessed precursor]

Molecular weight: 88071 Da [This is the MW of the unprocessed precursor]

CRC64: F38D1891B8ECA1F9 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MNKKSLPLMA LRDMVVFPGV IAPIFVGRKK SLQALSRTTI SEENNSKYIL VTLQKKFDQE 

        70         80         90        100        110        120 
NPSKHELYNT AILAKIIQIV KLPNNTAKIL IEAVARVKLS NIKDEEAFEA NYEIIPDEEI 

       130        140        150        160        170        180 
LDIHNMRSLV DNAVQLFSKY AMNDKKVNAE IIETINKEIS NRTNFINIIN ILSSHLITSL 

       190        200        210        220        230        240 
ETKQQLLEET NPVKRITTVI TTLTSNIVNS ETEHALQQRV RKQIEKTQRD YYLHEQMKAI 

       250        260        270        280        290        300 
QKELDEDKSE LADIEKKIKS LKLSKEAKEK AESEFKKLRA MNQMSAESGV TRNYLETLLS 

       310        320        330        340        350        360 
LPWGKYDNSK IDINQAEKIL NRDHFGLEKV KERIIEYLAV LQRSSKIRGP ILCLIGPPGV 

       370        380        390        400        410        420 
GKTSLVKSIA EGMGRKYTKF SLGGVRDEAE IRGHRKTYLG SMPGKILGQL KKIKTSNPVM 

       430        440        450        460        470        480 
LLDEIDKMSS DFRGDPASAL LEVLDPEQNS HFVDHYLEVE YDLSNVVFIA TANSHDLPRA 

       490        500        510        520        530        540 
LSDRMEKIYI SGYVEEEKLQ IAKNYLVPKQ FKMHKIKEDE ITISEAAILD LIRYYTKESG 

       550        560        570        580        590        600 
VRALEREICA LTRKALKQIL ANKTVKHISI DSNNLEEFLG AKKYNFGLAE KEDQIGSTTG 

       610        620        630        640        650        660 
LAYTEVGGEL LTIEALAFSG KGEIKTTGKL GDVMKESAMA AYSCFRSRAT NFGLKYDNYK 

       670        680        690        700        710        720 
DFDIHIHVPA GAIPKDGPSA GCALFTTIVS LMTKIPVHRT VAMTGEITLR GNVLPIGGLK 

       730        740        750        760        770        780 
EKLLAASRGG IKTVLIPEEN VKDLKDIPPN IKENLEIISV SNIDQVLKHA LVEMPINKGL 


SYDL

Q9ZD92 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