P80561 (APX_STRGR) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Aminopeptidase S EC=3.4.11.24 Alternative name(s): SGAP
Organism	Streptomyces griseus
Taxonomic identifier	1911 [NCBI]
Taxonomic lineage	cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptomycineae › Streptomycetaceae › Streptomyces › Streptomyces griseus group

Protein attributes

Sequence length	284 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Specific for larger hydrophobic acids, especially leucine. No cleavage occurs if the next residue is proline.
Catalytic activity	Release of an N-terminal amino acid with a preference for large hydrophobic amino-terminus residues. Ref.3
Cofactor	Binds 2 zinc ions per subunit.
Enzyme regulation	Binds a calcium ion which modulates the activity of the enzyme.
Subunit structure	Monomer.
Subcellular location	Secreted.
Sequence similarities	Belongs to the peptidase M28 family. M28A subfamily.
Biophysicochemical properties	Kinetic parameters: KM=0.59 mM for Leu-NH-Np (with zinc as cofactor) Ref.3 KM=0.13 mM for Leu-NH-Np (with manganese as cofactor) KM=0.046 mM for Leu-NH-Np (with cobalt as cofactor) KM=4.1 mM for Ala-NH-Np (with zinc as cofactor) KM=1.74 mM for Ala-NH-Np (with cobalt as cofactor)
Mass spectrometry	Molecular mass is 29728±1.0 Da from positions 1 - 284. Determined by ESI. Ref.1

Ontologies

Keywords
Cellular component	Secreted
Ligand	Calcium 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

Chain

1 – 284

284

Aminopeptidase S

PRO_0000174143

Sites

Metal binding

85

1

Zinc 1

Metal binding

97

1

Zinc 1

Metal binding

97

1

Zinc 2

Metal binding

132

1

Zinc 2

Metal binding

160

1

Zinc 1

Metal binding

247

1

Zinc 2

Amino acid modifications

Disulfide bond

245 ↔ 250

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

284

Helix Strand Turn

Details...

Helix

6 – 21

16

Turn

22 – 25

4

Helix

32 – 48

17

Beta strand

51 – 59

9

Beta strand

62 – 70

9

Beta strand

74 – 85

12

Turn

95 – 98

4

Helix

99 – 114

16

Beta strand

120 – 129

10

Helix

131 – 133

3

Helix

136 – 144

9

Helix

147 – 150

4

Beta strand

153 – 159

7

Beta strand

170 – 172

3

Helix

176 – 188

13

Beta strand

194 – 196

3

Helix

205 – 210

6

Beta strand

215 – 219

5

Beta strand

223 – 225

3

Helix

228 – 234

7

Beta strand

240 – 242

3

Turn

244 – 247

4

Helix

258 – 276

19

Sequences

	Sequence		Length	Mass (Da)
	P80561 [UniParc]. Last modified February 1, 1996. Version 1. Checksum: 67F1B80F8CA5C4CC	FASTA	284	29,723
	10 20 30 40 50 60 APDIPLANVK AHLTQLSTIA ANNGGNRAHG RPGYKASVDY VKAKLDAAGY TTTLQQFTSG 70 80 90 100 110 120 GATGYNLIAN WPGGDPNKVL MAGAHLDSVS SGAGINDNGS GSAAVLETAL AVSRAGYQPD 130 140 150 160 170 180 KHLRFAWWGA EELGLIGSKF YVNNLPSADR SKLAGYLNFD MIGSPNPGYF VYDDDPVIEK 190 200 210 220 230 240 TFKNYFAGLN VPTEIETEGD GRSDHAPFKN VGVPVGGLFT GAGYTKSAAQ AQKWGGTAGQ 250 260 270 280 AFDRCYHSSC DSLSNINDTA LDRNSDAAAH AIWTLSSGTG EPPT

References

[1]	"Aminopeptidase from Streptomyces griseus: primary structure and comparison with other zinc-containing aminopeptidases." Maras B., Greenblatt H.M., Shoham G., Spungin-Bialik A., Blumberg S., Barra D. Eur. J. Biochem. 236:843-846(1996) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE, MASS SPECTROMETRY.
[2]	"Streptomyces griseus aminopeptidase is a calcium-activated zinc metalloprotein. Purification and properties of the enzyme." Spungin A., Blumberg S. Eur. J. Biochem. 183:471-477(1989) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-6.
[3]	"Specificity of Streptomyces griseus aminopeptidase and modulation of activity by divalent metal ion binding and substitution." Ben-Meir D., Spungin A., Ashkenazi R., Blumberg S. Eur. J. Biochem. 212:107-112(1993) [PubMed] [Europe PMC] [Abstract] Cited for: CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES.
[4]	"Streptomyces griseus aminopeptidase: X-ray crystallographic structure at 1.75-A resolution." Greenblatt H.M., Almog O., Maras B., Spungin-Bialik A., Barra D., Blumberg S., Shoham G. J. Mol. Biol. 265:620-636(1997) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

PIR

S66427.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1CP7	X-ray	1.58	A	1-284	[»]
1F2O	X-ray	1.70	A	1-284	[»]
1F2P	X-ray	1.80	A	1-284	[»]
1QQ9	X-ray	1.53	A	1-284	[»]
1TF8	X-ray	1.30	A	1-284	[»]
1TF9	X-ray	1.30	A	1-284	[»]
1TKF	X-ray	1.20	A	1-284	[»]
1TKH	X-ray	1.25	A	1-284	[»]
1TKJ	X-ray	1.15	A	1-284	[»]
1XBU	X-ray	1.20	A	1-277	[»]
1XJO	X-ray	1.75	A	1-284	[»]

ProteinModelPortal

P80561.

SMR

P80561. Positions 1-277.

ModBase

Search...

Protein family/group databases

MEROPS

M28.003.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

BRENDA

3.4.11.24. 6035.

SABIO-RK

P80561.

Family and domain databases

InterPro

IPR007484. Peptidase_M28.
[Graphical view]

Pfam

PF04389. Peptidase_M28. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P80561.

Entry information

Entry name

APX_STRGR

Accession

Primary (citable) accession number: P80561

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	February 1, 1996
Last modified:	April 3, 2013
This is version 77 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program