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UniProtKB/Swiss-Prot entry Q89A99

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

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Entry information
Entry name LON_BUCBP
Primary accession number Q89A99
Secondary accession numbers None
Integrated into Swiss-Prot on April 13, 2004
Sequence was last modified on June 1, 2003 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 41)
Name and origin of the protein
Protein name ATP-dependent protease La
Synonym EC 3.4.21.53
Gene name
Name: lon
OrderedLocusNames: bbp_421
From
Buchnera aphidicola subsp. Baizongia pistaciae [TaxID: 135842] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Buchnera.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1073/pnas.0235981100; PubMed=12522265 [NCBI, ExPASy, EBI, Israel, Japan]
van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F., Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J., Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
"Reductive genome evolution in Buchnera aphidicola.";
Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
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
AE016826; AAO27131.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_778026.1; -.
3D structure databases
SMR Q89A99; 491-584, 594-775.
ModBase Q89A99.
Protein family/group databases
MEROPS S16.001; -.
Enzyme and pathway databases
BioCyc BAPH224915:BBP_421-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.
BLOCKS Q89A99.
ProtoNet Q89A99.
Genome annotation databases
GeneID 1058354; -.
GenomeReviews AE016826_GR; bbp_421.
KEGG bab:bbp421; -.
Phylogenomic databases
HOGENOM Q89A99; -.
Genome annotation databases
CMR Q89A99; bbp_421.
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   780  780     ATP-dependent protease La. PRO_0000076127
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: 780 AA [This is the length of the unprocessed precursor] Molecular weight: 88203 Da [This is the MW of the unprocessed precursor] CRC64: 2C0AF017E21E6EAA [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MNPERSEYIE IPVLPLRDVV IYPYMVIPLF VGRDKSIKCI EASMNKNKKI MLVTQKEAEI 

        70         80         90        100        110        120 
DEPTDNDLFT IGTTASILQM LKLPDGTVKV LVEGLQRAKV KKINNENGYF TAQIQLICTP 

       130        140        150        160        170        180 
EITEKEQSIL IRTTLNQFEN YVKFNKKISP EILNSLNNIT NASQLSDMIA IHMPLKLSEK 

       190        200        210        220        230        240 
QSILETYNTN ERLERLMAIM ESEIDLLQVE KRIRNRVKKQ MEKSQREYYL NEQMKAIQKE 

       250        260        270        280        290        300 
LGEMDETLDE HEILKRKITT IKMPKEAQEK MASELHKLKM MSPMSAEATV VRSYIDWMIQ 

       310        320        330        340        350        360 
IPWNIRSKVK KNLTQAQKIL DSDHFGLDKV KERILEYLAV QSRINTVKGP ILCLVGPPGV 

       370        380        390        400        410        420 
GKTSLGQSIA RATGRKYIRM ALGGIRDEAE IRGHRRTYIG SMPGKIIQKM AKVGVKNPLF 

       430        440        450        460        470        480 
LLDEIDKMSC DIRVDPASAL LEVLDPEQNV AFNDHYLEVD YDLSNVMFIA TSNSTNIPAP 

       490        500        510        520        530        540 
LLDRMEIIRI SGYTEFEKLN IAKSYLKPKQ IKRNALKSNE LTIEDSVVTN IIRYYTREAG 

       550        560        570        580        590        600 
VRNLERELSK ICRKCVKNLI LNKSLKKIKI TTDNLHDYLG IKKYDFGKTN YKNQIGQVIG 

       610        620        630        640        650        660 
LAWTEVGGEL LTIEAACISG KGKLIYTGSL GEVMQESIQA ALTVVRSQAN KLGIKKNFYE 

       670        680        690        700        710        720 
KNDIHVHVPE GATPKDGPSA GIAMCTAIVS CLTGIPVKSD IAMTGEITLR GQILTIGGLK 

       730        740        750        760        770        780 
EKLLAAHRGG IKKVLIPYDN EKDLQEIPKT ILKGLFVHPV KHIKEVLNLS LENTPYFSSK
Q89A99 in FASTA format

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