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P43133

- THER_GEOSE

UniProt

P43133 - THER_GEOSE

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Protein
Thermolysin
Gene
nprS, nprM
Organism
Geobacillus stearothermophilus (Bacillus stearothermophilus)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Extracellular zinc metalloprotease.1 Publication

Catalytic activityi

Preferential cleavage: Xaa-|-Leu > Xaa-|-Phe.

Cofactori

Binds 4 calcium ions per subunit By similarity.
Binds 1 zinc ion per subunit By similarity.

Temperature dependencei

Thermostable. Retains about 45% of its activity after treatment of 90 degrees Celsius for 30 minutes.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi292 – 2921Calcium 1 By similarity
Metal bindingi294 – 2941Calcium 1 By similarity
Metal bindingi296 – 2961Calcium 1; via carbonyl oxygen By similarity
Metal bindingi373 – 3731Calcium 2 By similarity
Metal bindingi377 – 3771Zinc; catalytic By similarity
Active sitei378 – 3781 By similarity
Metal bindingi381 – 3811Zinc; catalytic By similarity
Metal bindingi401 – 4011Zinc; catalytic By similarity
Metal bindingi412 – 4121Calcium 2 By similarity
Metal bindingi412 – 4121Calcium 3 By similarity
Metal bindingi418 – 4181Calcium 3; via carbonyl oxygen By similarity
Metal bindingi420 – 4201Calcium 2 By similarity
Metal bindingi420 – 4201Calcium 3 By similarity
Metal bindingi422 – 4221Calcium 2; via carbonyl oxygen By similarity
Metal bindingi425 – 4251Calcium 2 By similarity
Metal bindingi425 – 4251Calcium 3 By similarity
Metal bindingi429 – 4291Calcium 4 By similarity
Metal bindingi432 – 4321Calcium 4; via carbonyl oxygen By similarity
Metal bindingi435 – 4351Calcium 4 By similarity
Active sitei466 – 4661Proton donor By similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. metalloendopeptidase activity Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Protein family/group databases

MEROPSiM04.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Thermolysin (EC:3.4.24.27)
Alternative name(s):
Neutral protease
Gene namesi
Name:nprS
Synonyms:nprM
OrganismiGeobacillus stearothermophilus (Bacillus stearothermophilus)
Taxonomic identifieri1422 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

Subcellular locationi

Secreted 1 Publication

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3131 Reviewed prediction
Add
BLAST
Propeptidei32 – 235204Activation peptide
PRO_0000028612Add
BLAST
Chaini236 – 551316Thermolysin
PRO_0000028613Add
BLAST

Keywords - PTMi

Zymogen

Expressioni

Inductioni

Is expressed in the stationary phase. Up-regulated by NprA.1 Publication

Structurei

3D structure databases

ProteinModelPortaliP43133.
SMRiP43133. Positions 236-551.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M4 family.

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.10.170.10. 1 hit.
InterProiIPR011096. FTP_domain.
IPR025711. PepSY.
IPR023612. Peptidase_M4.
IPR001570. Peptidase_M4_C_domain.
IPR013856. Peptidase_M4_domain.
[Graphical view]
PfamiPF07504. FTP. 1 hit.
PF03413. PepSY. 1 hit.
PF01447. Peptidase_M4. 1 hit.
PF02868. Peptidase_M4_C. 1 hit.
[Graphical view]
PRINTSiPR00730. THERMOLYSIN.
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P43133-1 [UniParc]FASTAAdd to Basket

« Hide

MKRKMKMKLV RFGLAAGLAA QVFFLPYNAL ASTEHVTWNQ QFQTPQFISG    50
DLLKVNGTSP EELVYQYVEK NENKFKFHEN AKDTLQLKEK KNDNLGFTFM 100
RFQQTYKGIP VFGAVVTAHV KDGTLTALSG TLIPNLDTKG SLKSGKKLSE 150
KQARDIAEKD LVANVTKEVP EYEQGKDTEF VVYVNGDEAS LAYVVNLNFL 200
TPEPGNWLYI IDAVDGKILN KFNQLDAAKP GDVKSITGTS TVGVGRGVLG 250
DQKNINTTYS TYYYLQDNTR GNGIFTYDAK YRTTLPGSLW ADADNQFFAS 300
YDAPAVDAHY YAGVTYDYYK NVHNRLSYDG NNAAIRSSVH YSQGYNNAFW 350
NGSQMVYGDG DGQTFIPLSG GIDVVAHELT HAVTDYTAGL IYQNESGAIN 400
EAISDIFGTL VEFYANKNPD WEIGEDVYTP GISGDSLRSM SDPAKYGDPD 450
HYSKRYTGTQ DNGGVHINSG IINKAAYLIS QGGTHYGVSV VGIGRDKLGK 500
IFYRALTQYL TPTSNFSQLR AAAVQSATDL YGSTSQEVAS VKQAFDAVGV 550
K 551
Length:551
Mass (Da):60,617
Last modified:November 1, 1995 - v1
Checksum:iFCF4B2B5A7870129
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti10 – 145VRFGL → RSFGV AA sequence 1 Publication
Sequence conflicti24 – 241Missing in AAB02774. 1 Publication
Sequence conflicti29 – 335ALAST → RLASS AA sequence 1 Publication
Sequence conflicti114 – 1141A → Q in AAB02774. 1 Publication
Sequence conflicti124 – 1241T → S in AAB02774. 1 Publication
Sequence conflicti134 – 1341P → PIP AA sequence 1 Publication
Sequence conflicti261 – 2611T → S in AAB02774. 1 Publication
Sequence conflicti463 – 4631G → A in AAB02774. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M21663 Genomic DNA. Translation: AAB02774.1.
M34237 Genomic DNA. Translation: AAA22625.1.
PIRiA46564.
B36706.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M21663 Genomic DNA. Translation: AAB02774.1 .
M34237 Genomic DNA. Translation: AAA22625.1 .
PIRi A46564.
B36706.

3D structure databases

ProteinModelPortali P43133.
SMRi P43133. Positions 236-551.
ModBasei Search...
MobiDBi Search...

Chemistry

DrugBanki DB01093. Dimethyl sulfoxide.

Protein family/group databases

MEROPSi M04.001.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 3.10.170.10. 1 hit.
InterProi IPR011096. FTP_domain.
IPR025711. PepSY.
IPR023612. Peptidase_M4.
IPR001570. Peptidase_M4_C_domain.
IPR013856. Peptidase_M4_domain.
[Graphical view ]
Pfami PF07504. FTP. 1 hit.
PF03413. PepSY. 1 hit.
PF01447. Peptidase_M4. 1 hit.
PF02868. Peptidase_M4_C. 1 hit.
[Graphical view ]
PRINTSi PR00730. THERMOLYSIN.
PROSITEi PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Cloning and nucleotide sequence of the highly thermostable neutral protease gene from Bacillus stearothermophilus."
    Kubo M., Imanaka T.
    J. Gen. Microbiol. 134:1883-1892(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 236-240, FUNCTION AS A PROTEASE, TEMPERATURE DEPENDENCE, SUBCELLULAR LOCATION.
    Strain: MK232.
  2. "Cloning and nucleotide sequences of the Bacillus stearothermophilus neutral protease gene and its transcriptional activator gene."
    Nishiya Y., Imanaka T.
    J. Bacteriol. 172:4861-4869(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 236-239, INDUCTION.
    Strain: TELNE.

Entry informationi

Entry nameiTHER_GEOSE
AccessioniPrimary (citable) accession number: P43133
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: May 14, 2014
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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