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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)DescriptionActionsGraphical viewLength
Active sitei97Nucleophile1
Active sitei138Proton donor/acceptor1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Enzyme and pathway databases

BioCyciPHOR70601:GJWR-1509-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)DescriptionActionsGraphical viewLength
Transmembranei239 – 259HelicalSequence analysisAdd BLAST21
Transmembranei271 – 291HelicalSequence analysisAdd BLAST21
Transmembranei307 – 327HelicalSequence analysisAdd BLAST21
Transmembranei344 – 364HelicalSequence analysisAdd BLAST21

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi62T → A: Reduces enzyme activity by over 90%. 1 Publication1
Mutagenesisi97S → A: Abolishes enzyme activity. 1 Publication1
Mutagenesisi138K → A: Reduces enzyme activity by 99%. 1 Publication1
Mutagenesisi168D → A: Reduces enzyme activity by 97%. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 20Sequence analysisAdd BLAST20
ChainiPRO_000042902221 – 441Membrane-bound protease PH1510Add BLAST421

Interactioni

Subunit structurei

Homodimer.4 Publications

Protein-protein interaction databases

STRINGi70601.PH1510.

Structurei

Secondary structure

1441
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi23 – 31Combined sources9
Helixi35 – 50Combined sources16
Beta strandi54 – 63Combined sources10
Helixi67 – 78Combined sources12
Beta strandi84 – 88Combined sources5
Beta strandi94 – 96Combined sources3
Helixi98 – 104Combined sources7
Beta strandi106 – 111Combined sources6
Beta strandi116 – 118Combined sources3
Beta strandi122 – 126Combined sources5
Beta strandi128 – 130Combined sources3
Beta strandi132 – 134Combined sources3
Helixi137 – 153Combined sources17
Helixi158 – 166Combined sources9
Helixi173 – 178Combined sources6
Beta strandi183 – 185Combined sources3
Helixi189 – 196Combined sources8
Beta strandi218 – 221Combined sources4
Helixi226 – 236Combined sources11
Helixi376 – 379Combined sources4
Beta strandi383 – 388Combined sources6
Beta strandi390 – 398Combined sources9
Beta strandi401 – 409Combined sources9
Beta strandi418 – 425Combined sources8
Beta strandi428 – 433Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO59179.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni64 – 67Substrate binding4
Regioni119 – 124Substrate binding6

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

CDDicd07015. Clp_protease_NfeD. 1 hit.
Gene3Di3.90.226.10. 2 hits.
InterProiIPR029045. ClpP/crotonase-like_dom.
IPR023562. ClpP/TepA.
IPR002810. NfeD-like_C.
IPR033853. PH1510-N.
[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
PDB 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.
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-1509-MONOMER.
BRENDAi3.4.21.B56. 5244.

Miscellaneous databases

EvolutionaryTraceiO59179.

Family and domain databases

CDDicd07015. Clp_protease_NfeD. 1 hit.
Gene3Di3.90.226.10. 2 hits.
InterProiIPR029045. ClpP/crotonase-like_dom.
IPR023562. ClpP/TepA.
IPR002810. NfeD-like_C.
IPR033853. PH1510-N.
[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 30, 2016
This is version 91 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.