Q01693 (AMPX_VIBPR) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Bacterial leucyl aminopeptidase EC=3.4.11.10
Organism	Vibrio proteolyticus (Aeromonas proteolytica)
Taxonomic identifier	671 [NCBI]
Taxonomic lineage	cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Vibrionales › Vibrionaceae › Vibrio

Protein attributes

Sequence length	504 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 component	Secreted
Domain	Signal
Ligand	Metal-binding Zinc
Molecular function	Aminopeptidase Hydrolase Protease
PTM	Disulfide bond Zymogen
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological_process	proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	aminopeptidase 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 21

21

Potential

Propeptide

22 – 106

85

Potential

PRO_0000026849

Chain

107 – 405

299

Bacterial leucyl aminopeptidase

PRO_0000026850

Propeptide

406 – 504

99

Removed in mature form Potential

PRO_0000026851

Sites

Metal binding

203

1

Zinc 1

Metal binding

223

1

Zinc 1

Metal binding

223

1

Zinc 2; catalytic

Metal binding

258

1

Zinc 2; catalytic

Metal binding

285

1

Zinc 1

Metal binding

362

1

Zinc 2; catalytic

Amino acid modifications

Disulfide bond

329 ↔ 333

Experimental info

Sequence conflict

303 – 304

2

TD → DT AA sequence Ref.1

Sequence conflict

306

1

N → D AA sequence Ref.1

Sequence conflict

312 – 314

3

TQL → QT AA sequence Ref.1

Secondary structure

1

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504

Helix Strand Turn

Details...

Helix

113 – 119

7

Helix

120 – 122

3

Helix

125 – 136

12

Helix

146 – 163

18

Beta strand

164 – 166

3

Beta strand

169 – 176

8

Beta strand

179 – 188

10

Beta strand

191 – 203

13

Turn

221 – 224

4

Helix

225 – 240

16

Beta strand

246 – 255

10

Helix

257 – 259

3

Helix

262 – 273

12

Beta strand

277 – 283

7

Beta strand

292 – 299

8

Beta strand

301 – 303

3

Helix

305 – 318

14

Beta strand

324 – 327

4

Helix

336 – 341

6

Beta strand

349 – 352

4

Helix

354 – 356

3

Turn

359 – 362

4

Helix

368 – 370

3

Helix

376 – 394

19

Sequences

	Sequence		Length	Mass (Da)
	Q01693 [UniParc]. Last modified July 1, 1993. Version 1. Checksum: 7B33317EF6153B48	FASTA	504	54,232
	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

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.

PIR

S24314.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AMP	X-ray	1.80	A	107-397	[»]
1CP6	X-ray	1.90	A	107-397	[»]
1FT7	X-ray	2.20	A	107-397	[»]
1IGB	X-ray	2.30	A	107-397	[»]
1LOK	X-ray	1.20	A	107-397	[»]
1RTQ	X-ray	0.95	A	107-405	[»]
1TXR	X-ray	2.00	A	107-405	[»]
1XRY	X-ray	2.10	A	107-405	[»]
2ANP	X-ray	1.90	A	107-397	[»]
2DEA	X-ray	1.24	A	107-405	[»]
2IQ6	X-ray	2.00	A	107-397	[»]
2NYQ	X-ray	2.50	A	107-405	[»]
2PRQ	X-ray	2.15	A	107-397	[»]
3B35	X-ray	1.10	A	107-397	[»]
3B3C	X-ray	1.46	A	107-397	[»]
3B3S	X-ray	1.18	A	107-397	[»]
3B3T	X-ray	1.17	A	107-397	[»]
3B3V	X-ray	1.22	A	107-397	[»]
3B3W	X-ray	1.75	A	107-397	[»]
3B7I	X-ray	1.75	A	107-397	[»]
3FH4	X-ray	1.95	A	107-405	[»]
3VH9	X-ray	1.29	A	107-405	[»]

ProteinModelPortal

Q01693.

SMR

Q01693. Positions 107-397.

ModBase

Search...

Protein family/group databases

MEROPS

M28.002.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

SABIO-RK

Q01693.

Family and domain databases

InterPro

IPR012189. Pept_M28E_Ap1.
IPR007280. Peptidase_C_arc/bac.
IPR007484. Peptidase_M28.
[Graphical view]

Pfam

PF04389. Peptidase_M28. 1 hit.
PF04151. PPC. 1 hit.
[Graphical view]

PIRSF

PIRSF036685. BacLeuNPeptidase. 1 hit.

ProtoNet

Search...

Other

BindingDB

Q01693.

ChEMBL

CHEMBL3750.

EvolutionaryTrace

Q01693.

PMAP-CutDB

Q01693.

Entry information

Entry name

AMPX_VIBPR

Accession

Primary (citable) accession number: Q01693

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	July 1, 1993
Last modified:	April 3, 2013
This is version 99 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program