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Protein

Bacterial leucyl aminopeptidase

Gene
N/A
Organism
Vibrio proteolyticus (Aeromonas proteolytica)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

Zn2+4 PublicationsNote: Binds 2 Zn2+ ions per subunit.4 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi203Zinc 1Combined sources4 Publications1
Metal bindingi223Zinc 1Combined sources4 Publications1
Metal bindingi223Zinc 2; catalyticCombined sources4 Publications1
Metal bindingi258Zinc 2; catalyticCombined sources4 Publications1
Metal bindingi285Zinc 1Combined sources4 Publications1
Metal bindingi362Zinc 2; via tele nitrogen; catalyticCombined sources4 Publications1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Protease

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.4.11.10. 167.
SABIO-RKQ01693.

Protein family/group databases

MEROPSiM28.002.

Names & Taxonomyi

Protein namesi
Recommended name:
Bacterial leucyl aminopeptidase (EC:3.4.11.10)
OrganismiVibrio proteolyticus (Aeromonas proteolytica)
Taxonomic identifieri671 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio

Subcellular locationi

  • Secreted 1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL3750.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 21Sequence analysisAdd BLAST21
PropeptideiPRO_000002684922 – 1062 PublicationsAdd BLAST85
ChainiPRO_0000026850107 – 405Bacterial leucyl aminopeptidaseAdd BLAST299
PropeptideiPRO_0000026851406 – 504Removed in mature form1 PublicationAdd BLAST99

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi329 ↔ 333Combined sources4 Publications

Keywords - PTMi

Disulfide bond, Zymogen

Miscellaneous databases

PMAP-CutDBQ01693.

Interactioni

Chemistry databases

BindingDBiQ01693.

Structurei

Secondary structure

1504
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi113 – 119Combined sources7
Helixi120 – 122Combined sources3
Helixi125 – 136Combined sources12
Helixi146 – 163Combined sources18
Beta strandi164 – 166Combined sources3
Beta strandi169 – 176Combined sources8
Beta strandi179 – 188Combined sources10
Beta strandi191 – 203Combined sources13
Turni221 – 224Combined sources4
Helixi225 – 240Combined sources16
Beta strandi246 – 255Combined sources10
Helixi257 – 259Combined sources3
Helixi262 – 273Combined sources12
Beta strandi277 – 283Combined sources7
Beta strandi292 – 299Combined sources8
Beta strandi301 – 303Combined sources3
Helixi305 – 318Combined sources14
Beta strandi324 – 327Combined sources4
Helixi336 – 341Combined sources6
Beta strandi349 – 352Combined sources4
Helixi354 – 356Combined sources3
Turni359 – 362Combined sources4
Helixi368 – 370Combined sources3
Helixi376 – 394Combined sources19

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
ProteinModelPortaliQ01693.
SMRiQ01693.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ01693.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M28 family. M28E subfamily.Curated

Keywords - Domaini

Signal

Family and domain databases

InterProiIPR012189. Pept_M28E_Ap1.
IPR007280. Peptidase_C_arc/bac.
IPR007484. Peptidase_M28.
[Graphical view]
PfamiPF04389. Peptidase_M28. 1 hit.
PF04151. PPC. 1 hit.
[Graphical view]
PIRSFiPIRSF036685. BacLeuNPeptidase. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q01693-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKYTKTLLAM VLSATFCQAY AEDKVWISIG ADANQTVMKS GAESILPNSV
60 70 80 90 100
ASSGQVWVGQ VDVAQLAELS HNMHEEHNRC GGYMVHPSAQ SAMAASAMPT
110 120 130 140 150
TLASFVMPPI TQQATVTAWL PQVDASQITG TISSLESFTN RFYTTTSGAQ
160 170 180 190 200
ASDWIASEWQ ALSASLPNAS VKQVSHSGYN QKSVVMTITG SEAPDEWIVI
210 220 230 240 250
GGHLDSTIGS HTNEQSVAPG ADDDASGIAA VTEVIRVLSE NNFQPKRSIA
260 270 280 290 300
FMAYAAEEVG LRGSQDLANQ YKSEGKNVVS ALQLDMTNYK GSAQDVVFIT
310 320 330 340 350
DYTDSNFTQY LTQLMDEYLP SLTYGFDTCG YACSDHASWH NAGYPAAMPF
360 370 380 390 400
ESKFNDYNPR IHTTQDTLAN SDPTGSHAKK FTQLGLAYAI EMGSATGDTP
410 420 430 440 450
TPGNQLEDGV PVTDLSGSRG SNVWYTFELE TQKNLQITTS GGYGDLDLYV
460 470 480 490 500
KFGSKASKQN WDCRPYLSGN NEVCTFNNAS PGTYSVMLTG YSNYSGASLK

ASTF
Length:504
Mass (Da):54,232
Last modified:July 1, 1993 - v1
Checksum:i7B33317EF6153B48
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti303 – 304TD → DT AA sequence (PubMed:1627651).Curated2
Sequence conflicti306N → D AA sequence (PubMed:1627651).Curated1
Sequence conflicti312 – 314TQL → QT AA sequence (PubMed:1627651).Curated3

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z11993 Genomic DNA. Translation: CAA78039.1.
M85159 Genomic DNA. Translation: AAA21940.1.
PIRiS24314.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z11993 Genomic DNA. Translation: CAA78039.1.
M85159 Genomic DNA. Translation: AAA21940.1.
PIRiS24314.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
ProteinModelPortaliQ01693.
SMRiQ01693.
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

BindingDBiQ01693.
ChEMBLiCHEMBL3750.

Protein family/group databases

MEROPSiM28.002.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.4.11.10. 167.
SABIO-RKQ01693.

Miscellaneous databases

EvolutionaryTraceiQ01693.
PMAP-CutDBQ01693.

Family and domain databases

InterProiIPR012189. Pept_M28E_Ap1.
IPR007280. Peptidase_C_arc/bac.
IPR007484. Peptidase_M28.
[Graphical view]
PfamiPF04389. Peptidase_M28. 1 hit.
PF04151. PPC. 1 hit.
[Graphical view]
PIRSFiPIRSF036685. BacLeuNPeptidase. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiAMPX_VIBPR
AccessioniPrimary (citable) accession number: Q01693
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: November 2, 2016
This is version 112 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

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.