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Protein

Lon protease 2

Gene

lon2

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

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).By similarity

Catalytic activityi

Hydrolysis of proteins in presence of ATP.PROSITE-ProRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei445 – 4451PROSITE-ProRule annotation
Active sitei488 – 4881PROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi97 – 1048ATPBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Stress response

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciBSUB:BSU28210-MONOMER.

Protein family/group databases

MEROPSiS16.005.

Names & Taxonomyi

Protein namesi
Recommended name:
Lon protease 2 (EC:3.4.21.53)
Alternative name(s):
ATP-dependent protease La 2
Gene namesi
Name:lon2
Synonyms:lonB, ysxF
Ordered Locus Names:BSU28210
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 552552Lon protease 2PRO_0000076117Add
BLAST

Proteomic databases

PaxDbiP42425.

Expressioni

Developmental stagei

Restricted to the prespore compartment of sporulating cells.1 Publication

Inductioni

By heat shock.By similarity

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100015411.

Structurei

3D structure databases

ProteinModelPortaliP42425.
SMRiP42425. Positions 65-539.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini349 – 535187Lon proteolyticPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase S16 family.PROSITE-ProRule annotation
Contains 1 Lon proteolytic domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4108IUQ. Bacteria.
COG1067. LUCA.
HOGENOMiHOG000054711.
InParanoidiP42425.
KOiK04076.
OMAiTRTPNEI.
OrthoDBiEOG6BW4V4.
PhylomeDBiP42425.

Family and domain databases

Gene3Di3.30.230.10. 1 hit.
3.40.50.300. 1 hit.
InterProiIPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR027065. Lon_Prtase.
IPR033141. LonB/LonC.
IPR027417. P-loop_NTPase.
IPR008269. Pept_S16_C.
IPR008268. Peptidase_S16_AS.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
IPR014251. Spore_LonB.
[Graphical view]
PANTHERiPTHR10046. PTHR10046. 1 hit.
PTHR10046:SF53. PTHR10046:SF53. 1 hit.
PfamiPF00004. AAA. 1 hit.
PF05362. Lon_C. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
SSF54211. SSF54211. 1 hit.
TIGRFAMsiTIGR02902. spore_lonB. 1 hit.
PROSITEiPS51786. LON_PROTEOLYTIC. 1 hit.
PS01046. LON_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P42425-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSWTGIALFI QLFFGIIIGL YFWNLLKNQR TQKVTIDKES KKEMEQLRKM
60 70 80 90 100
RAISLSEPLS EKVRPKSFKD IVGQEDGIKA LKAALCGPNP QHVIVYGPPG
110 120 130 140 150
VGKTAAARLV LEEAKKHKQS PFKEQAVFVE LDATTARFDE RGIADPLIGS
160 170 180 190 200
VHDPIYQGAG AMGQAGIPQP KQGAVTHAHG GVLFIDEIGE LHPIQMNKML
210 220 230 240 250
KVLEDRKVFL DSAYYSEENT QIPNHIHDIF QNGLPADFRL IGATTRMPNE
260 270 280 290 300
IPPAIRSRCL EVFFRELEKD ELKTVAKTAA DKIEKNISEE GLDLLTSYTR
310 320 330 340 350
NGREAVNMIQ IAAGMAVTEN RKDITIEDIE WVIHSSQLTP KHEQKIGVEP
360 370 380 390 400
QVGIVNGLAV YGPNSGSLLE IEVSVTAAQD KGSINITGIA EEESIGSQSK
410 420 430 440 450
SIRRKSMAKG SVENVLTVLR TMGMKPSDYD IHINFPGGIP IDGPSAGIAM
460 470 480 490 500
AAGIFSAIHK IPIDNTVAMT GEISLNGLVK PIGGVIPKIK AAKQSGAKKV
510 520 530 540 550
IIPYENQQAI LKQIDGIEII AVKTFQEVLD EILVNPPTEQ KPFHIEINKE

SV
Length:552
Mass (Da):60,429
Last modified:October 1, 1996 - v2
Checksum:i313AAF539662A0B5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti500 – 5001V → G in CAA53987 (PubMed:7961402).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U18229 Genomic DNA. Translation: AAA84744.1.
Z75208 Genomic DNA. Translation: CAA99539.1.
AL009126 Genomic DNA. Translation: CAB14781.1.
X76424 Genomic DNA. Translation: CAA53987.1.
PIRiG69652.
RefSeqiNP_390699.1. NC_000964.3.
WP_004398923.1. NZ_JNCM01000036.1.

Genome annotation databases

EnsemblBacteriaiCAB14781; CAB14781; BSU28210.
GeneIDi937484.
KEGGibsu:BSU28210.
PATRICi18977518. VBIBacSub10457_2948.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U18229 Genomic DNA. Translation: AAA84744.1.
Z75208 Genomic DNA. Translation: CAA99539.1.
AL009126 Genomic DNA. Translation: CAB14781.1.
X76424 Genomic DNA. Translation: CAA53987.1.
PIRiG69652.
RefSeqiNP_390699.1. NC_000964.3.
WP_004398923.1. NZ_JNCM01000036.1.

3D structure databases

ProteinModelPortaliP42425.
SMRiP42425. Positions 65-539.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100015411.

Protein family/group databases

MEROPSiS16.005.

Proteomic databases

PaxDbiP42425.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB14781; CAB14781; BSU28210.
GeneIDi937484.
KEGGibsu:BSU28210.
PATRICi18977518. VBIBacSub10457_2948.

Phylogenomic databases

eggNOGiENOG4108IUQ. Bacteria.
COG1067. LUCA.
HOGENOMiHOG000054711.
InParanoidiP42425.
KOiK04076.
OMAiTRTPNEI.
OrthoDBiEOG6BW4V4.
PhylomeDBiP42425.

Enzyme and pathway databases

BioCyciBSUB:BSU28210-MONOMER.

Family and domain databases

Gene3Di3.30.230.10. 1 hit.
3.40.50.300. 1 hit.
InterProiIPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR027065. Lon_Prtase.
IPR033141. LonB/LonC.
IPR027417. P-loop_NTPase.
IPR008269. Pept_S16_C.
IPR008268. Peptidase_S16_AS.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
IPR014251. Spore_LonB.
[Graphical view]
PANTHERiPTHR10046. PTHR10046. 1 hit.
PTHR10046:SF53. PTHR10046:SF53. 1 hit.
PfamiPF00004. AAA. 1 hit.
PF05362. Lon_C. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
SSF54211. SSF54211. 1 hit.
TIGRFAMsiTIGR02902. spore_lonB. 1 hit.
PROSITEiPS51786. LON_PROTEOLYTIC. 1 hit.
PS01046. LON_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Ye R., Wong S.L.
    Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 168.
  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] [Europe PMC] [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.
    , 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 168.
  4. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 499-552.
    Strain: 168 / IS58.
  5. "Forespore-specific transcription of the lonB gene during sporulation in Bacillus subtilis."
    Serrano M., Hoevel S., Moran C.P. Jr., Henriques A.O., Voelker U.
    J. Bacteriol. 183:2995-3003(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEVELOPMENTAL STAGE.

Entry informationi

Entry nameiLON2_BACSU
AccessioniPrimary (citable) accession number: P42425
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: October 1, 1996
Last modified: April 13, 2016
This is version 120 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.