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Q01693 (AMPX_VIBPR) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Bacterial leucyl aminopeptidase

EC=3.4.11.10
OrganismVibrio proteolyticus (Aeromonas proteolytica)
Taxonomic identifier671 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio

Protein attributes

Sequence length504 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids.

Cofactor

Binds 2 zinc ions per subunit.

Subcellular location

Secreted.

Sequence similarities

Belongs to the peptidase M28 family. M28E subfamily.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   LigandMetal-binding
Zinc
   Molecular functionAminopeptidase
Hydrolase
Protease
   PTMDisulfide bond
Zymogen
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionaminopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Propeptide22 – 10685 Potential
PRO_0000026849
Chain107 – 405299Bacterial leucyl aminopeptidase
PRO_0000026850
Propeptide406 – 50499Removed in mature form Potential
PRO_0000026851

Sites

Metal binding2031Zinc 1
Metal binding2231Zinc 1
Metal binding2231Zinc 2; catalytic
Metal binding2581Zinc 2; catalytic
Metal binding2851Zinc 1
Metal binding3621Zinc 2; catalytic

Amino acid modifications

Disulfide bond329 ↔ 333

Experimental info

Sequence conflict303 – 3042TD → DT AA sequence Ref.1
Sequence conflict3061N → D AA sequence Ref.1
Sequence conflict312 – 3143TQL → QT AA sequence Ref.1

Secondary structure

.............................................. 504
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q01693 [UniParc].

Last modified July 1, 1993. Version 1.
Checksum: 7B33317EF6153B48

FASTA50454,232
        10         20         30         40         50         60 
MKYTKTLLAM VLSATFCQAY AEDKVWISIG ADANQTVMKS GAESILPNSV ASSGQVWVGQ 

        70         80         90        100        110        120 
VDVAQLAELS HNMHEEHNRC GGYMVHPSAQ SAMAASAMPT TLASFVMPPI TQQATVTAWL 

       130        140        150        160        170        180 
PQVDASQITG TISSLESFTN RFYTTTSGAQ ASDWIASEWQ ALSASLPNAS VKQVSHSGYN 

       190        200        210        220        230        240 
QKSVVMTITG SEAPDEWIVI GGHLDSTIGS HTNEQSVAPG ADDDASGIAA VTEVIRVLSE 

       250        260        270        280        290        300 
NNFQPKRSIA FMAYAAEEVG LRGSQDLANQ YKSEGKNVVS ALQLDMTNYK GSAQDVVFIT 

       310        320        330        340        350        360 
DYTDSNFTQY LTQLMDEYLP SLTYGFDTCG YACSDHASWH NAGYPAAMPF ESKFNDYNPR 

       370        380        390        400        410        420 
IHTTQDTLAN SDPTGSHAKK FTQLGLAYAI EMGSATGDTP TPGNQLEDGV PVTDLSGSRG 

       430        440        450        460        470        480 
SNVWYTFELE TQKNLQITTS GGYGDLDLYV KFGSKASKQN WDCRPYLSGN NEVCTFNNAS 

       490        500 
PGTYSVMLTG YSNYSGASLK ASTF 

« Hide

References

[1]"Cloning and nucleotide sequence of the Vibrio proteolyticus aminopeptidase gene."
van Heeke G., Denslow S., Watkins J., Wilson K., Wagner F.
Biochim. Biophys. Acta 1131:337-340(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 107-136 AND 233-405.
Strain: ATCC 15338 / DSM 30189 / JCM 21193 / LMG 3772 / NBRC 13287 / NCIMB 1326.
[2]"Isolation of the leucine aminopeptidase gene from Aeromonas proteolytica. Evidence for an enzyme precursor."
Guenet C., Lepage P., Harris B.A.
J. Biol. Chem. 267:8390-8395(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 73-504.
[3]"Rapid purification of the Aeromonas proteolytica aminopeptidase: crystallization and preliminary X-ray data."
Schalk C., Remy J.M., Chevrier B., Moras D., Tarnus C.
Arch. Biochem. Biophys. 294:91-97(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION, CRYSTALLIZATION.
[4]"Crystal structure of Aeromonas proteolytica aminopeptidase: a prototypical member of the co-catalytic zinc enzyme family."
Chevrier B., Schalk C., D'Orchymont H., Rondeau J.-M., Moras D., Tarnus C.
Structure 2:283-290(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 107-396.
[5]"The structure of the Aeromonas proteolytica aminopeptidase complexed with a hydroxamate inhibitor. Involvement in catalysis of Glu151 and two zinc ions of the co-catalytic unit."
Chevrier B., D'Orchymont H., Schalk C., Tarnus C., Moras D.
Eur. J. Biochem. 237:393-398(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH INHIBITOR.
[6]"1-butaneboronic acid binding to Aeromonas proteolytica aminopeptidase: a case of arrested development."
De Paola C.C., Bennett B., Holz R.C., Ringe D., Petsko G.A.
Biochemistry 38:9048-9053(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF INHIBITOR COMPLEX.
[7]"Inhibition of the aminopeptidase from Aeromonas proteolytica by L-leucinephosphonic acid. Spectroscopic and crystallographic characterization of the transition state of peptide hydrolysis."
Stamper C., Bennett B., Edwards T., Holz R.C., Ringe D., Petsko G.A.
Biochemistry 40:7035-7046(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF INHIBITOR COMPLEX.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z11993 Genomic DNA. Translation: CAA78039.1.
M85159 Genomic DNA. Translation: AAA21940.1.
PIRS24314.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AMPX-ray1.80A107-397[»]
1CP6X-ray1.90A107-397[»]
1FT7X-ray2.20A107-397[»]
1IGBX-ray2.30A107-397[»]
1LOKX-ray1.20A107-397[»]
1RTQX-ray0.95A107-405[»]
1TXRX-ray2.00A107-405[»]
1XRYX-ray2.10A107-405[»]
2ANPX-ray1.90A107-397[»]
2DEAX-ray1.24A107-405[»]
2IQ6X-ray2.00A107-397[»]
2NYQX-ray2.50A107-405[»]
2PRQX-ray2.15A107-397[»]
3B35X-ray1.10A107-397[»]
3B3CX-ray1.46A107-397[»]
3B3SX-ray1.18A107-397[»]
3B3TX-ray1.17A107-397[»]
3B3VX-ray1.22A107-397[»]
3B3WX-ray1.75A107-397[»]
3B7IX-ray1.75A107-397[»]
3FH4X-ray1.95A107-405[»]
3VH9X-ray1.29A107-405[»]
ProteinModelPortalQ01693.
SMRQ01693. Positions 107-397.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBQ01693.
ChEMBLCHEMBL3750.

Protein family/group databases

MEROPSM28.002.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKQ01693.

Family and domain databases

InterProIPR012189. Pept_M28E_Ap1.
IPR007280. Peptidase_C_arc/bac.
IPR007484. Peptidase_M28.
[Graphical view]
PfamPF04389. Peptidase_M28. 1 hit.
PF04151. PPC. 1 hit.
[Graphical view]
PIRSFPIRSF036685. BacLeuNPeptidase. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ01693.
PMAP-CutDBQ01693.

Entry information

Entry nameAMPX_VIBPR
AccessionPrimary (citable) accession number: Q01693
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: May 14, 2014
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references