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Reviewed, UniProtKB/Swiss-Prot Q10744 (PEPC_LACHE)

Last modified June 16, 2009. Version 59. 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:
    Aminopeptidase C
    EC=3.4.22.40
Alternative name(s):
    Bleomycin hydrolase
Gene names
Name: pepC
OrganismLactobacillus helveticus
Taxonomic identifier1587 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Lactobacillales › Lactobacillaceae › Lactobacillus

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Protein attributes

Sequence length449 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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General annotation (Comments)

Catalytic activity

Inactivates bleomycin B2 (a cytotoxic glycometallopeptide) by hydrolysis of a carboxyamide bond of beta-aminoalanine, but also shows general aminopeptidase activity. The specificity varies somewhat with source, but amino acid arylamides of Met, Leu and Ala are preferred.

Subunit structure

Homohexamer By similarity.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the peptidase C1 family.

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Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionAminopeptidase
Hydrolase
Protease
Thiol protease
Gene Ontology (GO)
   Biological processproteolysis

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionaminopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

cysteine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 449449Aminopeptidase C
PRO_0000050591

Sites

Active site701 By similarity
Active site3641 By similarity
Active site3851 By similarity

Natural variations

Natural variant71N → T
Natural variant631D → N
Natural variant1791L → V
Natural variant2341N → D
Natural variant310 – 3112NN → KS
Natural variant3331A → D

Experimental info

Sequence conflict373 – 3742IV → NG in AAA25250. Ref.2
Sequence conflict435 – 44915QLLPW…LAFKY → NYCHGIQWVL Ref.2

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Sequences

Sequence LengthMass (Da)Tools
Q10744-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: B0E5C687691B96A3

FASTA44951,400
        10         20         30         40         50         60 
MAKEINNDTI AKFENDLNNH PVFNVASHAA QENGIYKASQ NLQTKIDLDP IFSIEIDTGK 

        70         80         90        100        110        120 
PADQKQSGRC WMFSALNTMR HPLQKKFKLQ DFELSQNYTN FWDKFEKSNW FFENVIATAD 

       130        140        150        160        170        180 
KDLGDRKVSF LFATPQQDGG QWDMLCGIIE KYGIVPKSVY PETANATNSS ALNDTLNTLL 

       190        200        210        220        230        240 
RKDGLELRRL VNAGKSEDEV QARKEEMLND VFRVLAISTC VPPKKFNFEY RDDNHNYHID 

       250        260        270        280        290        300 
KDITPKEFFD KYVGMDLANH ISTINAPTSD KPFHKVFSVE YLGNVEGGRQ VRHLNLKVDE 

       310        320        330        340        350        360 
MKDLIIKQLN NGEVVWFGSN VVKDSERRAG LLATNLYRRD QLFDVDFSMS KADKLDSGES 

       370        380        390        400        410        420 
MMDHAMVITG VDIVDGKPTK WKIENSWGEK PGFKGYFVMS DSWFDSFVYQ AVINKDILPE 

       430        440 
DLKKAYDEGK DNPIQLLPWD PMGALAFKY

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References

[1]"Characterization and expression of the Lactobacillus helveticus pepC gene encoding a general aminopeptidase."
Vesanto E., Varmanen P., Steele J.L., Palva A.
Eur. J. Biochem. 224:991-997(1994) [PubMed: 7925424] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 53/7 and CNRZ 32.
[2]"Characterization of the Lactobacillus helveticus CNRZ32 pepC gene."
Fernandez L., Bhowmik T., Steele J.L.
Appl. Environ. Microbiol. 60:333-336(1994) [PubMed: 8117086] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: CNRZ 32.

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Cross-references

Sequence databases

Z30340 Genomic DNA. Translation: CAA82997.1.
L26223 Genomic DNA. Translation: AAA25250.1.
PIRS48200.

3D structure databases

HSSPHSSP built from PDB template 2CB5 based on UniProtKB Q13867.
ModBaseSearch...

Protein family/group databases

MEROPSC01.086.

Enzyme and pathway databases

BRENDA3.4.22.40. 39238.

Family and domain databases

InterProIPR000169. Pept_cys_AS.
IPR004134. Peptidase_C1B.
[Graphical view]
PANTHERPTHR10363. Peptidase_C1B. 1 hit.
PfamPF03051. Peptidase_C1_2. 1 hit.
[Graphical view]
PIRSFPIRSF005700. PepC. 1 hit.
PROSITEPS00640. THIOL_PROTEASE_ASN. False negative.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry namePEPC_LACHE
AccessionPrimary (citable) accession number: Q10744
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: June 16, 2009
This is version 59 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