Lon protease 1 - Borrelia burgdorferi (strain ATCC 35210 / B31 / CIP 102532 / DSM 4680)

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Q59185 (LON1_BORBU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 98. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Lon protease 1
EC=3.4.21.53

Alternative name(s):
ATP-dependent protease La 1

Gene names

Name:	lon1
Ordered Locus Names:	BB_0253

Organism

Borrelia burgdorferi (strain ATCC 35210 / B31 / CIP 102532 / DSM 4680) [Reference proteome] [HAMAP]

Taxonomic identifier

224326 [NCBI]

Taxonomic lineage

Bacteria › Spirochaetes › Spirochaetales › Spirochaetaceae › Borrelia › Borrelia burgdorferi group ›

Protein attributes

Sequence length	806 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

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. HAMAP-Rule MF_01973
Catalytic activity	Hydrolysis of proteins in presence of ATP. HAMAP-Rule MF_01973
Subunit structure	Homohexamer. Organized in a ring with a central cavity By similarity.
Subcellular location	Cytoplasm HAMAP-Rule MF_01973.
Induction	By heat shock By similarity.
Sequence similarities	Belongs to the peptidase S16 family. Contains 1 Lon domain.

Ontologies

Keywords
Biological process	Stress response
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Hydrolase Protease Serine protease
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	misfolded or incompletely synthesized protein catabolic process Inferred from electronic annotation. Source: InterPro response to stress Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 806

806

Lon protease 1 HAMAP-Rule MF_01973

PRO_0000076118

Regions

Domain

31 – 231

201

Lon

Nucleotide binding

389 – 396

ATP By similarity

Sites

Active site

714

By similarity

Active site

757

By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q59185 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: 71F488D719B1424E
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FASTA

806

90,710

        10         20         30         40         50         60 
MDESKKARSG DKKKEKAVAG ILPHSNKPAR VPLIAVPSHP VFPGMFIPIV LISDSDMKAI 

        70         80         90        100        110        120 
DYAMKGNGII ALFVLNDKFL EKNNNNAQQK LIIDYSKDIY SVGVTGKIIK KINLPDGGYN 

       130        140        150        160        170        180 
IFVSTFDRIK FVKVVLNDKF PIIEIDYLKQ IPVRKDDIQS KAVYGSILLR TKEIFAHRKM 

       190        200        210        220        230        240 
PEVQLNMVNI EDKGKLCDIV ASTISSSKND HQIVLETLNV KDRLKKVLEL IYEELNLIEI 

       250        260        270        280        290        300 
QNKIAKGIQE RLEKQQKEFF LKEQLKAIKA ELGIGDKKSS DLEKLKTKLK ALELKGEPLE 

       310        320        330        340        350        360 
VVEKELEKFS LLETSSAEYI VVRNYLELIT ELPWRDFKIN FDKLDLQKSK KILDKTHYGM 

       370        380        390        400        410        420 
NEVKDRIIEY ISVLKLRKTQ KGAIILLVGP PGVGKTSIGA AIAKVLRTKF FRFSVGGMRD 

       430        440        450        460        470        480 
ESEIKGHRRT YVGALPGKII QGLRITKTNS PVFLIDEVDK ISASSYGDPF SVLLEVLDPE 

       490        500        510        520        530        540 
QNVRFRDHYL DLPFDISNVF FILTANSVET IPRPLLNRME IIEISGYIDN EKIEIARKYL 

       550        560        570        580        590        600 
IPKVLSENGV DKDSLKFQSS SLVQIAQEYA RDNGVRNFEK YLNKIVRKVA RKLIENTEVK 

       610        620        630        640        650        660 
SYQISNDNLE EYVGVPVFRK ESMPNAMYSG MVMGLAWTNY GGSTLMIETV KTESKVGGIK 

       670        680        690        700        710        720 
LTGRLGDVMK ESANIAYTYV NSIKGDLSIS KSFFEKNIIH LHIPEGATPK DGPSAGITIA 

       730        740        750        760        770        780 
SAFISLALNK VVRPHLAMTG ELSLTGNVMM IGGLKEKIIA AKRSGVEHII VPKANRVDLE 

       790        800 
EIPTNIKSGI NFYLVDNMRE VIKLLF

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and expression of the Borrelia burgdorferi lon gene." Cloud J.L., Marconi R.T., Eggers C.H., Garon C.F., Tilly K., Samuels D.S. Gene 194:137-141(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 35210 / B31 / CIP 102532 / DSM 4680.
[2]	"Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi." Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A., Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L., Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L., Peterson J.D., Kerlavage A.R., Quackenbush J. Venter J.C. Nature 390:580-586(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 35210 / B31 / CIP 102532 / DSM 4680.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L77216 Genomic DNA. Translation: AAB72011.1. AE000783 Genomic DNA. Translation: AAB91493.1.
PIR	E70131.
RefSeq	NP_212387.1. NC_001318.1.
3D structure databases
ProteinModelPortal	Q59185.
ModBase	Search...
Protein-protein interaction databases
STRING	224326.BB0253.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAB91493; AAB91493; BB_0253.
GeneID	1195090.
KEGG	bbu:BB_0253.
PATRIC	20557124. VBIBorBur75917_0652.
Phylogenomic databases
eggNOG	COG0466.
KO	K01338.
OMA	FFILTAN.
ProtClustDB	CLSK544900.
Enzyme and pathway databases
BioCyc	BBUR224326:BB_0253-MONOMER.
Family and domain databases
Gene3D	3.30.230.10. 1 hit.
HAMAP	MF_01973. lon_bact.
InterPro	IPR003593. AAA+_ATPase. IPR003959. ATPase_AAA_core. IPR027065. Lon_Prtase. 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. IPR014721. Ribosomal_S5_D2-typ_fold_subgr. [Graphical view]
PANTHER	PTHR10046. PTHR10046. 1 hit.
Pfam	PF00004. AAA. 1 hit. PF02190. LON. 1 hit. PF05362. Lon_C. 1 hit. [Graphical view]
PIRSF	PIRSF001174. Lon_proteas. 1 hit.
SMART	SM00382. AAA. 1 hit. SM00464. LON. 1 hit. [Graphical view]
SUPFAM	SSF88697. PUA-like. 1 hit. SSF54211. Ribosomal_S5_D2-typ_fold. 1 hit.
TIGRFAMs	TIGR00763. lon. 1 hit.
PROSITE	PS01046. LON_SER. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

LON1_BORBU

Accession

Primary (citable) accession number: Q59185

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	May 1, 2013
This is version 98 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents