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Reviewed, UniProtKB/Swiss-Prot Q43880 (THER_ALIAC)

Last modified June 16, 2009. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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

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Names and origin

Protein namesRecommended name:
    Thermolysin
    EC=3.4.24.27
Alternative name(s):
    Thermostable neutral proteinase
OrganismAlicyclobacillus acidocaldarius (Bacillus acidocaldarius)
Taxonomic identifier1388 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Alicyclobacillaceae › Alicyclobacillus

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Protein attributes

Sequence length546 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Extracellular zinc metalloprotease.

Catalytic activity

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

Cofactor

Binds 4 calcium ions per subunit.

Binds 1 zinc ion per subunit.

Subcellular location

Secreted.

Sequence similarities

Belongs to the peptidase M4 family.

biophysicochemical properties

Temperature dependence:

Thermostable.

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Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   LigandCalcium
Metal-binding
Zinc
   Molecular functionHydrolase
Metalloprotease
Protease
   PTMZymogen
Gene Ontology (GO)
   Biological processproteolysis

Inferred from electronic annotation. Source: InterPro

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncalcium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

metalloendopeptidase activity

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Potential
Propeptide26 – 228203Activation peptide
PRO_0000028584
Chain229 – 546318Thermolysin
PRO_0000028585

Sites

Active site3731 By similarity
Active site4611Proton donor By similarity
Metal binding2871Calcium 1 By similarity
Metal binding2891Calcium 1 By similarity
Metal binding2911Calcium 1; via carbonyl oxygen By similarity
Metal binding3681Calcium 2 By similarity
Metal binding3721Zinc; catalytic By similarity
Metal binding3761Zinc; catalytic By similarity
Metal binding3961Zinc; catalytic By similarity
Metal binding4071Calcium 2 By similarity
Metal binding4071Calcium 3 By similarity
Metal binding4131Calcium 3; via carbonyl oxygen By similarity
Metal binding4151Calcium 2 By similarity
Metal binding4151Calcium 3 By similarity
Metal binding4171Calcium 2; via carbonyl oxygen By similarity
Metal binding4201Calcium 2 By similarity
Metal binding4201Calcium 3 By similarity
Metal binding4231Calcium 4; via carbonyl oxygen By similarity
Metal binding4241Calcium 4 By similarity
Metal binding4271Calcium 4; via carbonyl oxygen By similarity
Metal binding4301Calcium 4 By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q43880-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 3AC33A611BD2B071

FASTA54659,770
        10         20         30         40         50         60 
MNKRAMLGAI GLAFGLMAWP FGASAKEKSM VWNEQWKTPS FVSGSLLKGE DAPEELVYRY 

        70         80         90        100        110        120 
LDQEKNTFQL GGQARERLSL IGKQTDELGH TVMRFEQRYR GIPVYGAVLV AHVNDGELSS 

       130        140        150        160        170        180 
LSGTLIPNLD KRTLKTEAAI SIQQAEMIAK QDVADAVTKE RPAAEEGKPT RLVIYPDGET 

       190        200        210        220        230        240 
PRLAYEVNVR FLTPVPGNWI YMIDAADGKV LNKWNQMDEA KPGGGQPVAG TSTVGVGRGV 

       250        260        270        280        290        300 
LGDQKYINTT YSSYYGYYYL QDNTRGSGIF TYDGRNRTVL PGSLWADGDN QFFASYDAAA 

       310        320        330        340        350        360 
VDAHYYAGVV YDYYKNVHGR LSYDGSNAAI RSTVHYGRGY NNAFWNGSQM VYGDGDGQTF 

       370        380        390        400        410        420 
LPFSGGIDVV GHELTHAVTD YTAGLVYQNE SGAINEAMSD IFGTLVEFYA NRNPDWEIGE 

       430        440        450        460        470        480 
DIYTPGIAGD ALRSMSDPAK YGDPDHYSKR YTGTQDNGGV HTNSGIINKA AYLLSQGGVH 

       490        500        510        520        530        540 
YGVSVTGIGR DKMGKIFYRA LVYYLTPTSN FSQLRAACVQ AAADLYGSTS QEVNSVKQAF 


NAVGVY

« Hide

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References

[1]"Cloning and sequencing of the neutral protease-encoding gene from a thermophilic strain of Bacillus sp."
Vecerek B., Kyslik P.
Gene 158:147-148(1995) [PubMed: 7789802] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: BT1.

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Cross-references

Sequence databases

U07824 Genomic DNA. Translation: AAC43402.1.

3D structure databases

HSSPHSSP built from PDB template 1HYT based on UniProtKB P00800.
SMRQ43880. Positions 228-545.
ModBaseSearch...

Protein family/group databases

MEROPSM04.001.

Enzyme and pathway databases

BRENDA3.4.24.27. 97623.

Family and domain databases

InterProIPR005075. Pept_M4_propep_PepSY.
IPR006025. Pept_M_Zn_BS.
IPR013856. Peptidase_M4.
IPR001570. Peptidase_M4_C.
IPR011096. Propep_M4_M36.
[Graphical view]
Gene3DG3DSA:3.10.170.10. Peptidase_M4. 1 hit.
G3DSA:1.10.390.10. Peptidase_M4/M36. 1 hit.
PfamPF07504. FTP. 1 hit.
PF03413. PepSY. 1 hit.
PF01447. Peptidase_M4. 1 hit.
PF02868. Peptidase_M4_C. 1 hit.
[Graphical view]
PRINTSPR00730. THERMOLYSIN.
PROSITEPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameTHER_ALIAC
AccessionPrimary (citable) accession number: Q43880
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2003
Last sequence update: November 1, 1996
Last modified: June 16, 2009
This is version 55 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)

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Relevant documents

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