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Protein

Pseudomonalisin

Gene

pcp

Organism
Pseudomonas sp. (strain 101) (Achromobacter parvulus T1)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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.

Cofactori

Ca2+Note: Binds 1 Ca2+ ion per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei295 – 2951Charge relay system1 Publication
Active sitei299 – 2991Charge relay system1 Publication
Active sitei502 – 5021Charge relay system1 Publication
Metal bindingi543 – 5431Calcium
Metal bindingi544 – 5441Calcium; via carbonyl oxygen
Metal bindingi559 – 5591Calcium; via carbonyl oxygen
Metal bindingi561 – 5611Calcium; via carbonyl oxygen
Metal bindingi563 – 5631Calcium

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. serine-type endopeptidase activity Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BRENDAi3.4.21.100. 5085.

Protein family/group databases

MEROPSiS53.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Pseudomonalisin (EC:3.4.21.100)
Alternative name(s):
Pepstatin-insensitive carboxyl proteinase
Pseudomonapepsin
Gene namesi
Name:pcp
OrganismiPseudomonas sp. (strain 101) (Achromobacter parvulus T1)
Taxonomic identifieri33067 [NCBI]
Taxonomic lineageiBacteriaProteobacteria

Subcellular locationi

GO - Cellular componenti

  1. periplasmic space Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei? – 215Removed in mature formPRO_0000027362
Signal peptidei1 – ?Sequence Analysis
Chaini216 – 585370PseudomonalisinPRO_0000027363Add
BLAST
Propeptidei586 – 5872Removed in mature formPRO_0000027364

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi352 ↔ 391

Post-translational modificationi

Autocatalytically processed.

Keywords - PTMi

Disulfide bond, Zymogen

Structurei

Secondary structure

1
587
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi225 – 2273Combined sources
Helixi228 – 2314Combined sources
Beta strandi240 – 25213Combined sources
Helixi254 – 26613Combined sources
Beta strandi274 – 2785Combined sources
Helixi290 – 30617Combined sources
Beta strandi311 – 3199Combined sources
Beta strandi321 – 3244Combined sources
Helixi327 – 33913Combined sources
Beta strandi343 – 3475Combined sources
Helixi353 – 3586Combined sources
Helixi361 – 37414Combined sources
Beta strandi378 – 3825Combined sources
Turni390 – 3956Combined sources
Turni407 – 4093Combined sources
Beta strandi413 – 42311Combined sources
Beta strandi429 – 4346Combined sources
Beta strandi436 – 4394Combined sources
Beta strandi445 – 4473Combined sources
Beta strandi451 – 4577Combined sources
Helixi460 – 4645Combined sources
Beta strandi470 – 4745Combined sources
Beta strandi476 – 4805Combined sources
Helixi483 – 4853Combined sources
Beta strandi487 – 4915Combined sources
Beta strandi494 – 4985Combined sources
Helixi501 – 51818Combined sources
Turni519 – 5213Combined sources
Helixi527 – 53610Combined sources
Helixi538 – 5403Combined sources
Beta strandi548 – 5514Combined sources
Beta strandi560 – 5634Combined sources
Turni564 – 5663Combined sources
Helixi573 – 58311Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GA1X-ray1.40A216-587[»]
1GA4X-ray1.40A216-587[»]
1GA6X-ray1.00A216-587[»]
1KDVX-ray1.10A216-585[»]
1KDYX-ray1.10A216-585[»]
1KDZX-ray1.40A216-585[»]
1KE1X-ray1.80A216-585[»]
1KE2X-ray2.00A216-585[»]
1NLUX-ray1.30A216-585[»]
ProteinModelPortaliP42790.
SMRiP42790. Positions 218-587.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP42790.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini219 – 583365Peptidase S53Add
BLAST

Sequence similaritiesi

Contains 1 peptidase S53 domain.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.40.50.200. 1 hit.
InterProiIPR015366. Peptidase_S53_propep.
IPR000209. Peptidase_S8/S53_dom.
IPR023828. Peptidase_S8_Ser-AS.
IPR009020. Prot_inh_propept.
IPR030400. Sedolisin_dom.
[Graphical view]
PfamiPF00082. Peptidase_S8. 1 hit.
PF09286. Pro-kuma_activ. 1 hit.
[Graphical view]
SMARTiSM00944. Pro-kuma_activ. 1 hit.
[Graphical view]
SUPFAMiSSF52743. SSF52743. 1 hit.
SSF54897. SSF54897. 1 hit.
PROSITEiPS51695. SEDOLISIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P42790-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKSSAAKQTV LCLNRYAVVA LPLAIASFAA FGASPASTLW APTDTKAFVT
60 70 80 90 100
PAQVEARSAA PLLELAAGET AHIVVSLKLR DEAQLKQLAQ AVNQPGNAQF
110 120 130 140 150
GKFLKRRQFL SQFAPTEAQV QAVVAHLRKN GFVNIHVVPN RLLISADGSA
160 170 180 190 200
GAVKAAFNTP LVRYQLNGKA GYANTAPAQV PQDLGEIVGS VLGLQNVTRA
210 220 230 240 250
HPMLKVGERS AAKTLAAGTA KGHNPTEFPT IYDASSAPTA ANTTVGIITI
260 270 280 290 300
GGVSQTLQDL QQFTSANGLA SVNTQTIQTG SSNGDYSDDQ QGQGEWDLDS
310 320 330 340 350
QSIVGSAGGA VQQLLFYMAD QSASGNTGLT QAFNQAVSDN VAKVINVSLG
360 370 380 390 400
WCEADANADG TLQAEDRIFA TAAAQGQTFS VSSGDEGVYE CNNRGYPDGS
410 420 430 440 450
TYSVSWPASS PNVIAVGGTT LYTTSAGAYS NETVWNEGLD SNGKLWATGG
460 470 480 490 500
GYSVYESKPS WQSVVSGTPG RRLLPDISFD AAQGTGALIY NYGQLQQIGG
510 520 530 540 550
TSLASPIFVG LWARLQSANS NSLGFPAASF YSAISSTPSL VHDVKSGNNG
560 570 580
YGGYGYNAGT GWDYPTGWGS LDIAKLSAYI RSNGFGH
Length:587
Mass (Da):61,073
Last modified:October 31, 1995 - v1
Checksum:iE193D8B2C225829A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D37970 Genomic DNA. Translation: BAA07188.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D37970 Genomic DNA. Translation: BAA07188.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GA1X-ray1.40A216-587[»]
1GA4X-ray1.40A216-587[»]
1GA6X-ray1.00A216-587[»]
1KDVX-ray1.10A216-585[»]
1KDYX-ray1.10A216-585[»]
1KDZX-ray1.40A216-585[»]
1KE1X-ray1.80A216-585[»]
1KE2X-ray2.00A216-585[»]
1NLUX-ray1.30A216-585[»]
ProteinModelPortaliP42790.
SMRiP42790. Positions 218-587.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiS53.001.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.4.21.100. 5085.

Miscellaneous databases

EvolutionaryTraceiP42790.

Family and domain databases

Gene3Di3.40.50.200. 1 hit.
InterProiIPR015366. Peptidase_S53_propep.
IPR000209. Peptidase_S8/S53_dom.
IPR023828. Peptidase_S8_Ser-AS.
IPR009020. Prot_inh_propept.
IPR030400. Sedolisin_dom.
[Graphical view]
PfamiPF00082. Peptidase_S8. 1 hit.
PF09286. Pro-kuma_activ. 1 hit.
[Graphical view]
SMARTiSM00944. Pro-kuma_activ. 1 hit.
[Graphical view]
SUPFAMiSSF52743. SSF52743. 1 hit.
SSF54897. SSF54897. 1 hit.
PROSITEiPS51695. SEDOLISIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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(1993) [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(1994) [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(1998) [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(2000) [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(2000) [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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 216-585 IN COMPLEX WITH INHIBITOR, CALCIUM-BINDING SITES.

Entry informationi

Entry nameiPICP_PSESR
AccessioniPrimary (citable) accession number: P42790
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 1995
Last sequence update: October 31, 1995
Last modified: March 31, 2015
This is version 90 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

External Data

Dasty 3

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 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.