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Protein

Membrane-bound protease PH1510

Gene

PH1510

Organism
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Protease that cleaves its substrates preferentially near hydrophobic or aromatic amino acid residues. Can degrade casein and the stomatin homolog PH1511 (in vitro).3 Publications

Enzyme regulationi

Inhibited by divalent metal cations, including Mg2+, Mn2+, Ca2+ and Zn2+. Mildly inhibited by 0.01 % SDS and 0.1% dodecyl-beta-D-maltoside. Activity is nearly abolished by 1 % SDS.1 Publication

pH dependencei

Optimum pH is 5-6.1 Publication

Temperature dependencei

Optimum temperature is above 90 degrees Celsius.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei97 – 971Nucleophile
Active sitei138 – 1381Proton donor/acceptor

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Enzyme and pathway databases

BioCyciPHOR70601:GJWR-1510-MONOMER.
BRENDAi3.4.21.B56. 5244.

Protein family/group databases

MEROPSiS49.005.
TCDBi8.A.21.2.1. the stomatin/podocin/band 7/nephrosis.2/spfh (stomatin) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Membrane-bound protease PH1510 (EC:3.4.21.-)
Alternative name(s):
NfeD homolog
Stomatin operon partner protein
Short name:
STOPP
Gene namesi
Ordered Locus Names:PH1510
OrganismiPyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Taxonomic identifieri70601 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus
Proteomesi
  • UP000000752 Componenti: Chromosome

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei239 – 25921HelicalSequence analysisAdd
BLAST
Transmembranei271 – 29121HelicalSequence analysisAdd
BLAST
Transmembranei307 – 32721HelicalSequence analysisAdd
BLAST
Transmembranei344 – 36421HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi62 – 621T → A: Reduces enzyme activity by over 90%. 1 Publication
Mutagenesisi97 – 971S → A: Abolishes enzyme activity. 1 Publication
Mutagenesisi138 – 1381K → A: Reduces enzyme activity by 99%. 1 Publication
Mutagenesisi168 – 1681D → A: Reduces enzyme activity by 97%. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence analysisAdd
BLAST
Chaini21 – 441421Membrane-bound protease PH1510PRO_0000429022Add
BLAST

Interactioni

Subunit structurei

Homodimer.4 Publications

Protein-protein interaction databases

STRINGi70601.PH1510.

Structurei

Secondary structure

1
441
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi23 – 319Combined sources
Helixi35 – 5016Combined sources
Beta strandi54 – 6310Combined sources
Helixi67 – 7812Combined sources
Beta strandi84 – 885Combined sources
Beta strandi94 – 963Combined sources
Helixi98 – 1047Combined sources
Beta strandi106 – 1116Combined sources
Beta strandi116 – 1183Combined sources
Beta strandi122 – 1265Combined sources
Beta strandi128 – 1303Combined sources
Beta strandi132 – 1343Combined sources
Helixi137 – 15317Combined sources
Helixi158 – 1669Combined sources
Helixi173 – 1786Combined sources
Beta strandi183 – 1853Combined sources
Helixi189 – 1968Combined sources
Beta strandi218 – 2214Combined sources
Helixi226 – 23611Combined sources
Helixi376 – 3794Combined sources
Beta strandi383 – 3886Combined sources
Beta strandi390 – 3989Combined sources
Beta strandi401 – 4099Combined sources
Beta strandi418 – 4258Combined sources
Beta strandi428 – 4336Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DEOX-ray3.00A/B16-236[»]
3BPPX-ray2.30A16-236[»]
3VIVX-ray2.25A/B16-236[»]
3WG5X-ray2.40A/B16-236[»]
3WWVX-ray2.40A371-441[»]
ProteinModelPortaliO59179.
SMRiO59179. Positions 20-235.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO59179.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni64 – 674Substrate binding
Regioni119 – 1246Substrate binding

Sequence similaritiesi

Belongs to the peptidase S14 family.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiarCOG01910. Archaea.
COG1030. LUCA.
HOGENOMiHOG000217027.
KOiK07403.
OMAiILYASHV.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
3.90.226.10. 2 hits.
InterProiIPR029045. ClpP/crotonase-like_dom.
IPR023562. ClpP/TepA.
IPR012340. NA-bd_OB-fold.
IPR002810. NfeD-like_C.
[Graphical view]
PfamiPF00574. CLP_protease. 1 hit.
PF01957. NfeD. 1 hit.
[Graphical view]
SUPFAMiSSF52096. SSF52096. 1 hit.

Sequencei

Sequence statusi: Complete.

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

O59179-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRRILLSMIV LIFLASPILA KNIVYVAQIK GQITSYTYDQ FDRYITIAEQ
60 70 80 90 100
DNAEAIIIEL DTPGGRADAM MNIVQRIQQS KIPVIIYVYP PGASAASAGT
110 120 130 140 150
YIALGSHLIA MAPGTSIGAC RPILGYSQNG SIIEAPPKIT NYFIAYIKSL
160 170 180 190 200
AQESGRNATI AEEFITKDLS LTPEEALKYG VIEVVARDIN ELLKKSNGMK
210 220 230 240 250
TKIPVNGRYV TLNFTNVEVR YLAPSFKDKL ISYITDPNVA YLLLTLGIWA
260 270 280 290 300
LIIGFLTPGW HVPETVGAIM IILAIIGFGY FGYNSAGILL IIVAMLFFIA
310 320 330 340 350
EALTPTFGLF TVAGLITFII GGILLFGGGE EYLVRKEVFS QLRILIITVG
360 370 380 390 400
AILAAFFAFG MAAVIRAHKK KARTGKEEMI GLIGTVVEEL NPEGMIKVRG
410 420 430 440
ELWKARSKFN GKIEKGEKVR VVDMDGLTLI VVRERKEGGE K
Length:441
Mass (Da):48,281
Last modified:August 1, 1998 - v1
Checksum:i2E16ECFC4529C4E6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000001 Genomic DNA. Translation: BAA30618.1.
PIRiB71027.
RefSeqiWP_010885587.1. NC_000961.1.

Genome annotation databases

EnsemblBacteriaiBAA30618; BAA30618; BAA30618.
GeneIDi1443826.
KEGGipho:PH1510.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000001 Genomic DNA. Translation: BAA30618.1.
PIRiB71027.
RefSeqiWP_010885587.1. NC_000961.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DEOX-ray3.00A/B16-236[»]
3BPPX-ray2.30A16-236[»]
3VIVX-ray2.25A/B16-236[»]
3WG5X-ray2.40A/B16-236[»]
3WWVX-ray2.40A371-441[»]
ProteinModelPortaliO59179.
SMRiO59179. Positions 20-235.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi70601.PH1510.

Protein family/group databases

MEROPSiS49.005.
TCDBi8.A.21.2.1. the stomatin/podocin/band 7/nephrosis.2/spfh (stomatin) family.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAA30618; BAA30618; BAA30618.
GeneIDi1443826.
KEGGipho:PH1510.

Phylogenomic databases

eggNOGiarCOG01910. Archaea.
COG1030. LUCA.
HOGENOMiHOG000217027.
KOiK07403.
OMAiILYASHV.

Enzyme and pathway databases

BioCyciPHOR70601:GJWR-1510-MONOMER.
BRENDAi3.4.21.B56. 5244.

Miscellaneous databases

EvolutionaryTraceiO59179.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
3.90.226.10. 2 hits.
InterProiIPR029045. ClpP/crotonase-like_dom.
IPR023562. ClpP/TepA.
IPR012340. NA-bd_OB-fold.
IPR002810. NfeD-like_C.
[Graphical view]
PfamiPF00574. CLP_protease. 1 hit.
PF01957. NfeD. 1 hit.
[Graphical view]
SUPFAMiSSF52096. SSF52096. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiSTOPP_PYRHO
AccessioniPrimary (citable) accession number: O59179
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 14, 2014
Last sequence update: August 1, 1998
Last modified: November 11, 2015
This is version 88 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, Complete proteome

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.