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O69177 (LON_RHIME) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Lon protease
EC=3.4.21.53
Alternative name(s):
ATP-dependent protease La
Gene names
Name:lon
Ordered Locus Names:R01257
ORF Names:SMc01905
OrganismRhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti) [Complete proteome] [HAMAP]
Taxonomic identifier266834 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Rhizobiaceae › Sinorhizobium/Ensifer group › Sinorhizobium

Protein attributes

Sequence length806 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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. In R.meliloti it is important for controlling the turnover of a constitutively expressed protein(s) that, when unregulated, disrupts normal nodule formation and normal growth.

Catalytic activity

Hydrolysis of proteins in presence of ATP.

Subunit structure

Homohexamer. Organized in a ring with a central cavity By similarity.

Subcellular location

Cytoplasm By similarity.

Induction

By heat shock By similarity.

Sequence similarities

Belongs to the peptidase S16 family.

Contains 1 Lon domain.

Ontologies

Keywords
   Biological processStress response
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionHydrolase
Protease
Serine protease
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processproteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

response to stress

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP 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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 806806Lon protease
PRO_0000076144

Regions

Domain14 – 204191Lon
Nucleotide binding359 – 3668ATP By similarity

Sites

Active site6811 By similarity
Active site7241 By similarity

Experimental info

Sequence conflict103 – 12624IERYT…EPDED → TNAIRRVTIFTRPWPMHCPN RTRY Ref.4
Sequence conflict2661L → F in AAF05300. Ref.1
Sequence conflict353 – 3597PILCLVG → RSLLVVS in AAC17128. Ref.4
Sequence conflict3571L → F in AAF05300. Ref.1
Sequence conflict4911I → F in AAF05300. Ref.1
Sequence conflict4991D → E in AAF05300. Ref.1
Sequence conflict5021R → L in AAF05300. Ref.1
Sequence conflict5211P → T in AAF05300. Ref.1
Sequence conflict532 – 5343MAV → TAI in AAF05300. Ref.1
Sequence conflict5731T → S in AAF05300. Ref.1
Sequence conflict5781H → N in AAF05300. Ref.1
Sequence conflict7461L → I in AAF05300. Ref.1
Sequence conflict7571L → F in AAF05300. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O69177 [UniParc].

Last modified May 30, 2000. Version 2.
Checksum: 4A984D1676072A00

FASTA80689,458
        10         20         30         40         50         60 
MTNKTSPATE SATYPVLPLR DIVVFPHMIV PLFVGREKSI RALEEVMGTD KQIMLVTQIN 

        70         80         90        100        110        120 
ATDDDPEPSA IYKVGTIANV LQLLKLPDGT VKVLVEGRSR AEIERYTPRD DFYEAMAHAL 

       130        140        150        160        170        180 
PEPDEDPVEI EALSRSVVSE FESYVKLNKK ISPEVVGVAS QIEDYSKLAD TVASHLSIKI 

       190        200        210        220        230        240 
VEKQEMLETT SVKMRLEKAL GFMEGEISVL QVEKRIRSRV KRQMEKTQRE YYLNEQMKAI 

       250        260        270        280        290        300 
QKELGDSEDG RDEMAELEER ISKTKLSKEA REKADAELKK LRQMSPMSAE ATVVRNYLDW 

       310        320        330        340        350        360 
LLGLPWGKKS KIKTDLNHAE KVLDTDHFGL DKVKERIVEY LAVQARSSKI KGPILCLVGP 

       370        380        390        400        410        420 
PGVGKTSLAK SIAKATGREY IRMALGGVRD EAEIRGHRRT YIGSMPGKVV QSMKKAKKSN 

       430        440        450        460        470        480 
PLFLLDEIDK MGQDFRGDPS SALLEVLDPE QNSTFMDHYL EVEYDLSNVM FITTANTLNI 

       490        500        510        520        530        540 
PPPLMDRMEV IRIAGYTEDE KREIAKRHLL PKAIRDHALQ PNEFSVTDGA LMAVIQNYTR 

       550        560        570        580        590        600 
EAGVRNFERE LMKLARKAVT EILKGKTKKV EVTAENIHDY LGVPRFRHGE AERDDQVGVV 

       610        620        630        640        650        660 
TGLAWTEVGG ELLTIEGVMM PGKGRMTVTG NLRDVMKESI SAAASYVRSR AIDFGIEPPL 

       670        680        690        700        710        720 
FDKRDIHVHV PEGATPKDGP SAGVAMATAI VSVMTGIPIS KDVAMTGEIT LRGRVLPIGG 

       730        740        750        760        770        780 
LKEKLLAALR GGIKKVLIPE ENAKDLADIP DNVKNSLEII PVSRMGEVIA HALLRLPEPI 

       790        800 
EWDPASQPAA LPSVDSQDEA GTSIAH

« Hide

References

« Hide 'large scale' references
[1]"The Sinorhizobium meliloti lon protease is involved in regulating exopolysaccharide synthesis and is required for nodulation of alfalfa."
Summers M.L., Botero L.M., Busse S.C., McDermott T.R.
J. Bacteriol. 182:2551-2558(2000) [PubMed: 10762258] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Analysis of the chromosome sequence of the legume symbiont Sinorhizobium meliloti strain 1021."
Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J., Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S., Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D. expand/collapse author list , Pohl T., Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C., Thebault P., Vandenbol M., Weidner S., Galibert F.
Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001) [PubMed: 11481430] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 1021.
[3]"The composite genome of the legume symbiont Sinorhizobium meliloti."
Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F., Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G., Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P., Cowie A. expand/collapse author list , Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S., Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I., Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S., Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C., Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R., Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H., Wong K., Yeh K.-C., Batut J.
Science 293:668-672(2001) [PubMed: 11474104] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 1021.
[4]"Partial coding sequence of Sinorhizobium meliloti lon gene."
Biondi E., Fancelli S., Bazzicalupo M.
Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 103-359.
Strain: CL375B.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF167159 Genomic DNA. Translation: AAF05300.1.
AL591688 Genomic DNA. Translation: CAC45836.1.
AF065445 Genomic DNA. Translation: AAC17128.1.
RefSeqNP_385363.1. NC_003047.1.

3D structure databases

ProteinModelPortalO69177.
SMRO69177. Positions 595-773.
ModBaseSearch...

Protein family/group databases

MEROPSS16.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1232902.
GenomeReviewsGene locus R01257 in contig AL591688_GR.
KEGGsme:SMc01905.
NMPDRfig|266834.1.peg.2551.
PATRIC23631823. VBISinMel96828_2671.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG566281.
OMAFMEGEIS.
ProtClustDBCLSK864999.

Enzyme and pathway databases

BioCycSMEL266834:SMC01905-MONOMER.

Family and domain databases

InterProIPR003593. 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]
KOK01338.
PfamPF00004. AAA. 1 hit.
PF02190. LON. 1 hit.
PF05362. Lon_C. 1 hit.
[Graphical view]
PIRSFPIRSF001174. Lon_proteas. 1 hit.
SMARTSM00382. AAA. 1 hit.
SM00464. LON. 1 hit.
[Graphical view]
SUPFAMSSF88697. PUA-like. 1 hit.
SSF54211. Ribosomal_S5_D2-typ_fold. 1 hit.
TIGRFAMsTIGR00763. Lon. 1 hit.
PROSITEPS01046. LON_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLON_RHIME
AccessionPrimary (citable) accession number: O69177
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 30, 2000
Last modified: January 25, 2012
This is version 86 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

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