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Reviewed, UniProtKB/Swiss-Prot P37945 (LON1_BACSU)

Last modified June 16, 2009. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    ATP-dependent protease La 1
    EC=3.4.21.53
Gene names
Name: lonA
Synonyms: lon
Ordered Locus Names: BSU28200
OrganismBacillus subtilis [Complete proteome] [HAMAP]
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillus

Protein attributes

Sequence length774 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Degrades short-lived regulatory and abnormal proteins in the presence of ATP. Hydrolyzes two ATP for each peptide bond cleaved in the protein substrate By similarity. Has been implicated in preventing sigma(G) activity under non-sporulation conditions.

Catalytic activity

Hydrolysis of proteins in presence of ATP.

Subcellular location

Cytoplasm.

Induction

By heat shock.

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 term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological processproteolysis

Inferred from electronic annotation. Source: InterPro

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 – 774774ATP-dependent protease La 1
PRO_0000076116

Regions

Domain8 – 200193Lon
Nucleotide binding354 – 3618ATP Potential

Sites

Active site6771 By similarity
Active site7201 By similarity

Secondary structure

............... 774
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P37945-1 [UniParc].

Last modified October 1, 1994. Version 1.
Checksum: BE339D896FCEF533

FASTA77486,607
        10         20         30         40         50         60 
MAEELKRSIP LLPLRGLLVY PTMVLHLDVG RDKSVQALEQ AMMHDHMIFL ATQQDISIDE 

        70         80         90        100        110        120 
PGEDEIFTVG TYTKIKQMLK LPNGTIRVLV EGLKRAHIVK YNEHEDYTSV DIQLIHEDDS 

       130        140        150        160        170        180 
KDTEDEALMR TLLDHFDQYI KISKKISAET YAAVTDIEEP GRMADIVASH LPLKLKDKQD 

       190        200        210        220        230        240 
ILETADVKDR LNKVIDFINN EKEVLEIEKK IGQRVKRSME RTQKEYYLRE QMKAIQKELG 

       250        260        270        280        290        300 
DKEGKTGEVQ TLTEKIEEAG MPDHVKETAL KELNRYEKIP SSSAESSVIR NYIDWLVALP 

       310        320        330        340        350        360 
WTDETDDKLD LKEAGRLLDE EHHGLEKVKE RILEYLAVQK LTKSLKGPIL CLAGPPGVGK 

       370        380        390        400        410        420 
TSLAKSIAKS LGRKFVRISL GGVRDESEIR GHRRTYVGAM PGRIIQGMKK AGKLNPVFLL 

       430        440        450        460        470        480 
DEIDKMSSDF RGDPSSAMLE VLDPEQNSSF SDHYIEETFD LSKVLFIATA NNLATIPGPL 

       490        500        510        520        530        540 
RDRMEIINIA GYTEIEKLEI VKDHLLPKQI KEHGLKKSNL QLRDQAILDI IRYYTREAGV 

       550        560        570        580        590        600 
RSLERQLAAI CRKAAKAIVA EERKRITVTE KNLQDFIGKR IFRYGQAETE DQVGVVTGLA 

       610        620        630        640        650        660 
YTTVGGDTLS IEVSLSPGKG KLILTGKLGD VMRESAQAAF SYVRSKTEEL GIEPDFHEKY 

       670        680        690        700        710        720 
DIHIHVPEGA VPKDGPSAGI TMATALVSAL TGRAVSREVG MTGEITLRGR VLPIGGLKEK 

       730        740        750        760        770 
ALGAHRAGLT TIIAPKDNEK DIEDIPESVR EGLTFILASH LDEVLEHALV GEKK 

« Hide

References

« Hide 'large scale' references
[1]"Cloning, nucleotide sequence, and expression of the Bacillus subtilis lon gene."
Riethdorf S., Voelker U., Gerth U., Winkler A., Engelmann S., Hecker M.
J. Bacteriol. 176:6518-6527(1994) [PubMed: 7961402] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168 / IS58.
[2]"The dnaB-pheA (256 degrees-240 degrees) region of the Bacillus subtilis chromosome containing genes responsible for stress responses, the utilization of plant cell walls and primary metabolism."
Wipat A., Carter N., Brignell C.S., Guy J.B., Piper K., Sanders J., Emmerson P.T., Harwood C.R.
Microbiology 142:3067-3078(1996) [PubMed: 8969504] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[3]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed: 9384377] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.

Cross-references

Sequence databases

X76424 Genomic DNA. Translation: CAA53984.1.
Z75208 Genomic DNA. Translation: CAA99540.1.
AL009126 Genomic DNA. Translation: CAB14780.1.
PIRI40421.
RefSeqNP_390698.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1X37NMR-A490-604[»]
ModBaseSearch...

Protein family/group databases

MEROPSS16.001.

Genome annotation databases

GeneID937486.
GenomeReviewsGene locus BSU28200 in contig AL009126_GR.
KEGGbsu:BSU28200.
NMPDRfig|224308.1.peg.2823.

Organism-specific databases

SubtiListBG10338. lonA. [Micado]
CMRSearch...

Phylogenomic databases

HOGENOMP37945.
OMAP37945. VMKESIQ.

Enzyme and pathway databases

BioCycBSUB224308:BSU2816-MON.
BRENDA3.4.21.53. 150.

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.
IPR001984. Peptidase_S16_C.
[Graphical view]
PfamPF00004. AAA. 1 hit.
PF02190. LON. 1 hit.
PF05362. Lon_C. 1 hit.
[Graphical view]
PRINTSPR00830. ENDOLAPTASE.
SMARTSM00382. AAA. 1 hit.
SM00464. LON. 1 hit.
[Graphical view]
TIGRFAMsTIGR00763. lon. 1 hit.
PROSITEPS01046. LON_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLON1_BACSU
AccessionPrimary (citable) accession number: P37945
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: June 16, 2009
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents