P42790 (PICP_PSESR) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Pseudomonalisin
EC=3.4.21.100

Alternative name(s):
Pepstatin-insensitive carboxyl proteinase
Pseudomonapepsin

Gene names

Name:

pcp

Organism

Pseudomonas sp. (strain 101) (Achromobacter parvulus T1)

Taxonomic identifier

33067 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › unclassified Proteobacteria › unclassified pseudomonads

Protein attributes

Sequence length	587 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	Hydrolysis of the B chain of insulin at 13-Glu-|-Ala-14, 15-Leu-|-Tyr-16 and 25-Phe-|-Tyr-26 and angiotensin I at 4-Tyr-|-Ile-5. A good synthetic substrate is Lys-Pro-Ile-Glu-Phe-|-Phe(NO2)-Arg-Leu.
Cofactor	Binds 1 calcium ion per subunit.
Subcellular location	Periplasm.
Post-translational modification	Autocatalytically processed.
Sequence similarities	Belongs to the peptidase S53 family.

Ontologies

Keywords
Cellular component	Periplasm
Domain	Signal
Ligand	Calcium Metal-binding
Molecular function	Hydrolase Protease Serine 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	periplasmic space Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW serine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – ?

Potential

Propeptide

? – 215

Removed in mature form

PRO_0000027362

Chain

216 – 585

370

Pseudomonalisin

PRO_0000027363

Propeptide

586 – 587

2

Removed in mature form

PRO_0000027364

Sites

Active site

295

1

Charge relay system Ref.3

Active site

299

1

Charge relay system Ref.3

Active site

502

1

Charge relay system Ref.3

Metal binding

543

1

Calcium

Metal binding

544

1

Calcium; via carbonyl oxygen

Metal binding

559

1

Calcium; via carbonyl oxygen

Metal binding

561

1

Calcium; via carbonyl oxygen

Metal binding

563

1

Calcium

Amino acid modifications

Disulfide bond

352 ↔ 391

Secondary structure

1

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587

Helix Strand Turn

Details...

Helix

225 – 227

3

Helix

228 – 231

4

Beta strand

240 – 252

13

Helix

254 – 266

13

Beta strand

274 – 278

5

Helix

290 – 306

17

Beta strand

311 – 319

9

Beta strand

321 – 324

4

Helix

327 – 339

13

Beta strand

343 – 347

5

Helix

353 – 358

6

Helix

361 – 374

14

Beta strand

378 – 382

5

Turn

390 – 395

6

Turn

407 – 409

3

Beta strand

413 – 423

11

Beta strand

429 – 434

6

Beta strand

436 – 439

4

Beta strand

445 – 447

3

Beta strand

451 – 457

7

Helix

460 – 464

5

Beta strand

470 – 474

5

Beta strand

476 – 480

5

Helix

483 – 485

3

Beta strand

487 – 491

5

Beta strand

494 – 498

5

Helix

501 – 518

18

Turn

519 – 521

3

Helix

527 – 536

10

Helix

538 – 540

3

Beta strand

548 – 551

4

Beta strand

560 – 563

4

Turn

564 – 566

3

Helix

573 – 583

11

Sequences

	Sequence		Length	Mass (Da)
	P42790 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: E193D8B2C225829A	FASTA	587	61,073
	10 20 30 40 50 60 MKSSAAKQTV LCLNRYAVVA LPLAIASFAA FGASPASTLW APTDTKAFVT PAQVEARSAA 70 80 90 100 110 120 PLLELAAGET AHIVVSLKLR DEAQLKQLAQ AVNQPGNAQF GKFLKRRQFL SQFAPTEAQV 130 140 150 160 170 180 QAVVAHLRKN GFVNIHVVPN RLLISADGSA GAVKAAFNTP LVRYQLNGKA GYANTAPAQV 190 200 210 220 230 240 PQDLGEIVGS VLGLQNVTRA HPMLKVGERS AAKTLAAGTA KGHNPTEFPT IYDASSAPTA 250 260 270 280 290 300 ANTTVGIITI GGVSQTLQDL QQFTSANGLA SVNTQTIQTG SSNGDYSDDQ QGQGEWDLDS 310 320 330 340 350 360 QSIVGSAGGA VQQLLFYMAD QSASGNTGLT QAFNQAVSDN VAKVINVSLG WCEADANADG 370 380 390 400 410 420 TLQAEDRIFA TAAAQGQTFS VSSGDEGVYE CNNRGYPDGS TYSVSWPASS PNVIAVGGTT 430 440 450 460 470 480 LYTTSAGAYS NETVWNEGLD SNGKLWATGG GYSVYESKPS WQSVVSGTPG RRLLPDISFD 490 500 510 520 530 540 AAQGTGALIY NYGQLQQIGG TSLASPIFVG LWARLQSANS NSLGFPAASF YSAISSTPSL 550 560 570 580 VHDVKSGNNG YGGYGYNAGT GWDYPTGWGS LDIAKLSAYI RSNGFGH

References

[1]	"Cloning, nucleotide sequence, and expression of an isovaleryl pepstatin-insensitive carboxyl proteinase gene from Pseudomonas sp. 101." Oda K., Takahashi T., Tokuda Y., Shibano Y., Takahashi S. J. Biol. Chem. 269:26518-26524(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 216-224.
[2]	"The primary structure of pepstatin-insensitive carboxyl proteinase produced by Pseudomonas sp. No. 101." Hayashi K., Izu H., Oda K., Fukuhara K., Matsuo M., Takano R., Hara S. J. Biochem. 118:738-744(1995) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 216-585.
[3]	"Identification of catalytic residues of pepstatin-insensitive carboxyl proteinases from prokaryotes by site-directed mutagenesis." Oyama H., Abe S., Ushiyama S., Takahashi S., Oda K. J. Biol. Chem. 274:27815-27822(1999) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF ASPARTIC ACID AND GLUTAMIC ACID RESIDUES, ACTIVE SITES.
[4]	"Inhibitor complexes of the Pseudomonas serine-carboxyl proteinase." Wlodawer A., Li M., Gustchina A., Dauter Z., Uchida K., Oyama H., Goldfarb N.E., Dunn B.M., Oda K. Biochemistry 40:15602-15611(2001) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.1 ANGSTROMS) OF 216-585.
[5]	"Carboxyl proteinase from Pseudomonas defines a novel family of subtilisin-like enzymes." Wlodawer A., Li M., Dauter Z., Gustchina A., Uchida K., Oyama H., Dunn B.M., Oda K. Nat. Struct. Biol. 8:442-446(2001) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.0 ANGSTROMS) OF 216-587.
[6]	"Two inhibitor molecules bound in the active site of Pseudomonas sedolisin: a model for the bi-product complex following cleavage of a peptide substrate." Wlodawer A., Li M., Gustchina A., Oyama H., Oda K., Beyer B.B., Clemente J., Dunn B.M. Biochem. Biophys. Res. Commun. 314:638-645(2004) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 216-585 IN COMPLEX WITH INHIBITOR, CALCIUM-BINDING SITES.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D37970 Genomic DNA. Translation: BAA07188.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GA1	X-ray	1.40	A	216-587	[»]
1GA4	X-ray	1.40	A	216-587	[»]
1GA6	X-ray	1.00	A	216-587	[»]
1KDV	X-ray	1.10	A	216-585	[»]
1KDY	X-ray	1.10	A	216-585	[»]
1KDZ	X-ray	1.40	A	216-585	[»]
1KE1	X-ray	1.80	A	216-585	[»]
1KE2	X-ray	2.00	A	216-585	[»]
1NLU	X-ray	1.30	A	216-585	[»]

ProteinModelPortal

P42790.

SMR

P42790. Positions 218-587.

ModBase

Search...

Protein family/group databases

MEROPS

S53.001.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

Gene3D

3.40.50.200. 1 hit.

InterPro

IPR015366. Peptidase_S53_propep.
IPR000209. Peptidase_S8/S53_dom.
IPR023828. Peptidase_S8_Ser-AS.
IPR009020. Prot_inh_propept.
[Graphical view]

Pfam

PF00082. Peptidase_S8. 1 hit.
PF09286. Pro-kuma_activ. 1 hit.
[Graphical view]

SMART

SM00944. Pro-kuma_activ. 1 hit.
[Graphical view]

SUPFAM

SSF52743. Pept_S8_S53. 1 hit.
SSF54897. Prot_inh_propept. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P42790.

Entry information

Entry name

PICP_PSESR

Accession

Primary (citable) accession number: P42790

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	April 3, 2013
This is version 82 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program