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UniProtKB/Swiss-Prot entry Q9PK50

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name LON_CHLMU
Primary accession number Q9PK50
Secondary accession numbers None
Integrated into Swiss-Prot on June 1, 2001
Sequence was last modified on October 1, 2000 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 53)
Name and origin of the protein
Protein name ATP-dependent protease La
Synonym EC 3.4.21.53
Gene name
Name: lon
OrderedLocusNames: TC_0623
From
Chlamydia muridarum [TaxID: 83560] [HAMAP proteome]
Taxonomy Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae; Chlamydia.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=MoPn / Nigg;
DOI=10.1093/nar/28.6.1397; PubMed=10684935 [NCBI, ExPASy, EBI, Israel, Japan]
Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O., Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S., Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J., Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G., Salzberg S.L., Eisen J.A., Fraser C.M.;
"Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae AR39.";
Nucleic Acids Res. 28:1397-1406(2000).
Comments
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
AE002160; AAF39454.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR E81681; E81681.
RefSeq NP_296997.1; -.
3D structure databases
HSSP P43773; 1G3I. [HSSP ENTRY / PDB]
ModBase Q9PK50.
Protein family/group databases
MEROPS S16.002; -.
Enzyme and pathway databases
BioCyc CMUR243161:TC_0623-MON; -.
Ontologies
GO
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.
TIGRFAMs TIGR00763; lon; 1.
PROSITE PS01046; LON_SER; 1.
ProtoNet Q9PK50.
Genome annotation databases
GeneID 1245983; -.
GenomeReviews AE002160_GR; TC_0623.
KEGG cmu:TC0623; -.
TIGR TC_0623; -.
Phylogenomic databases
HOGENOM Q9PK50; -.
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
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   819  819     ATP-dependent protease La. PRO_0000076130
DOMAIN   41   237  197     Lon. 
NP_BIND   392   399  8     ATP (Potential). 
ACT_SITE   724   724        By similarity. 
ACT_SITE   767   767        By similarity. 
Sequence information
Length: 819 AA [This is the length of the unprocessed precursor] Molecular weight: 91844 Da [This is the MW of the unprocessed precursor] CRC64: DD87D5D701E1B063 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MNSTNNTDSQ NLDPNASEVE KLLDESAEAE EKTDDHTPPS ELFILPLNKR PFFPGMAAPL 

        70         80         90        100        110        120 
LIEAGPHYEV LTLLAKSSQK HIGLVLTKKE DANTLKIGFN QLHRVGVSAR ILRIMPIEGG 

       130        140        150        160        170        180 
SAQVLLSIED RIRIVKPVQD KYLKAKVAYH KENKELTEEL KAYSISIVSI IKDLLKLNPL 

       190        200        210        220        230        240 
FKEELQIFLG HSDFTEPGKL ADFSVALTTA TREELQEVLE TTDMHDRIDK ALVLLKKELD 

       250        260        270        280        290        300 
LSRLQSSINQ KIEATITKSQ KEFFLKEQLK TIKKELGLEK DDHAVDLEKF MERLNKRDVP 

       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 KLVQALKQSA IMNPVIMIDE VDKIGSSYHG DPASALLEVL 

       490        500        510        520        530        540 
DPEQNKDFLD HYLDVRVDLS NVLFILTANV LDSIPDPLLD RMEVLRLSGY ILEEKLQIAT 

       550        560        570        580        590        600 
KYLVPRARKE MGLSAQNVSF QPEALKHMIN NYAREAGVRT LNENIKKVLR KVALKIVQNQ 

       610        620        630        640        650        660 
EKNPSKKSRF TITPKNLQDY LGKPIFSSDR FYEKTPVGVA TGLAWTSLGG ATLYIESVQV 

       670        680        690        700        710        720 
PSSSGKADMH LTGQAGDVMK ESSQIAWTYL HSALERYAPG RPFFEKSQVH IHIPEGATPK 

       730        740        750        760        770        780 
DGPSAGITMV TSLLSLLLDV PVLNNLGMTG ELTLTGRVLG IGGIREKLIA ARRSKLNVLI 

       790        800        810 
FPEDNRRDYD ELPAYLKKGL KVHFVTHYDD VFKIAFPGV
Q9PK50 in FASTA format

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