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Protein

Rhomboid protease GlpG

Gene

glpG

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Rhomboid-type serine protease that catalyzes intramembrane proteolysis.2 Publications

Catalytic activityi

Cleaves type-1 transmembrane domains using a catalytic dyad composed of serine and histidine that are contributed by different transmembrane domains.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei201Nucleophile4 Publications1
Active sitei2544 Publications1

GO - Molecular functioni

  • endopeptidase activity Source: EcoCyc
  • serine-type endopeptidase activity Source: EcoCyc

GO - Biological processi

  • protein processing Source: GO_Central
  • proteolysis Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Enzyme and pathway databases

BioCyciEcoCyc:EG10397-MONOMER.
ECOL316407:JW5687-MONOMER.
MetaCyc:EG10397-MONOMER.
BRENDAi3.4.21.105. 2026.

Protein family/group databases

MEROPSiS54.016.
TCDBi9.B.104.1.1. the rhomboid protease (rhomboid) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Rhomboid protease GlpG (EC:3.4.21.105)
Alternative name(s):
Intramembrane serine protease
Gene namesi
Name:glpG
Ordered Locus Names:b3424, JW5687
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10397. glpG.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 93CytoplasmicCuratedAdd BLAST93
Transmembranei94 – 114Helical; Name=1CuratedAdd BLAST21
Topological domaini115 – 141PeriplasmicCuratedAdd BLAST27
Transmembranei142 – 162Helical; Name=2CuratedAdd BLAST21
Topological domaini163 – 168CytoplasmicCurated6
Transmembranei169 – 189Helical; Name=3CuratedAdd BLAST21
Topological domaini190 – 191PeriplasmicCurated2
Transmembranei192 – 212Helical; Name=4CuratedAdd BLAST21
Topological domaini213 – 222CytoplasmicCurated10
Transmembranei223 – 245Helical; Name=5CuratedAdd BLAST23
Topological domaini246 – 249PeriplasmicCurated4
Transmembranei250 – 272Helical; Name=6CuratedAdd BLAST23
Topological domaini273 – 276CytoplasmicCurated4

GO - Cellular componenti

  • integral component of plasma membrane Source: EcoCyc
  • plasma membrane Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi154N → A: Reduced catalytic activity. 2 Publications1
Mutagenesisi199G → C: Loss of catalytic activity. 1 Publication1
Mutagenesisi201S → A or C: Loss of catalytic activity. 4 Publications1
Mutagenesisi254H → A or C: Loss of catalytic activity. 3 Publications1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000875151 – 276Rhomboid protease GlpGAdd BLAST276

Proteomic databases

PaxDbiP09391.
PRIDEiP09391.

Interactioni

Protein-protein interaction databases

BioGridi4262105. 13 interactors.
DIPiDIP-9796N.
IntActiP09391. 2 interactors.
STRINGi511145.b3424.

Chemistry databases

BindingDBiP09391.

Structurei

Secondary structure

1276
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 9Combined sources8
Helixi10 – 22Combined sources13
Beta strandi27 – 30Combined sources4
Beta strandi32 – 40Combined sources9
Helixi42 – 44Combined sources3
Helixi45 – 57Combined sources13
Helixi62 – 65Combined sources4
Helixi95 – 114Combined sources20
Helixi116 – 123Combined sources8
Helixi129 – 131Combined sources3
Helixi137 – 140Combined sources4
Helixi141 – 143Combined sources3
Helixi148 – 169Combined sources22
Helixi171 – 193Combined sources23
Helixi201 – 217Combined sources17
Helixi219 – 221Combined sources3
Helixi227 – 241Combined sources15
Turni242 – 245Combined sources4
Turni247 – 249Combined sources3
Helixi251 – 270Combined sources20

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2IC8X-ray2.10A91-272[»]
2IRVX-ray2.30A/B92-273[»]
2LEPNMR-A1-61[»]
2NRFX-ray2.60A/B91-272[»]
2O7LX-ray2.50A93-272[»]
2XOVX-ray1.65A91-271[»]
2XOWX-ray2.09A92-270[»]
2XTUX-ray1.85A91-271[»]
2XTVX-ray1.70A93-272[»]
3B44X-ray1.70A91-270[»]
3B45X-ray1.90A91-270[»]
3TXTX-ray2.30A92-270[»]
3UBBX-ray2.60A91-272[»]
3ZEBX-ray2.20A92-270[»]
3ZMHX-ray2.30A91-270[»]
3ZMIX-ray2.20A92-270[»]
3ZMJX-ray2.30A92-270[»]
3ZOTX-ray2.40A92-271[»]
4H1DX-ray2.90A92-270[»]
4HDDX-ray1.35A2-74[»]
4NJNX-ray2.40A87-276[»]
4NJPX-ray2.40A87-276[»]
5F5BX-ray2.30A87-276[»]
5F5DX-ray2.50A87-276[»]
5F5GX-ray2.30A87-276[»]
5F5JX-ray2.40A87-276[»]
5F5KX-ray2.40A87-276[»]
ProteinModelPortaliP09391.
SMRiP09391.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP09391.

Family & Domainsi

Domaini

The loop between transmembrane domains 5 and 6 is flexible and may readily open to the extracellular side to allow water entry into the active site cavity.1 Publication

Sequence similaritiesi

Belongs to the peptidase S54 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105EBW. Bacteria.
COG0705. LUCA.
HOGENOMiHOG000269640.
InParanoidiP09391.
KOiK02441.
OMAiHFSAMHI.
PhylomeDBiP09391.

Family and domain databases

Gene3Di1.20.1540.10. 1 hit.
HAMAPiMF_01594. Rhomboid_GlpG. 1 hit.
InterProiIPR022732. Peptidase_S54_GlpG_N.
IPR002610. Peptidase_S54_rhomboid.
IPR022764. Peptidase_S54_rhomboid_dom.
IPR023662. Rhomboid_protease_GlpG.
[Graphical view]
PANTHERiPTHR22936. PTHR22936. 1 hit.
PfamiPF01694. Rhomboid. 1 hit.
PF12122. Rhomboid_N. 1 hit.
[Graphical view]
TIGRFAMsiTIGR04239. rhombo_GlpG. 1 hit.

Sequencei

Sequence statusi: Complete.

P09391-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLMITSFANP RVAQAFVDYM ATQGVILTIQ QHNQSDVWLA DESQAERVRA
60 70 80 90 100
ELARFLENPA DPRYLAASWQ AGHTGSGLHY RRYPFFAALR ERAGPVTWVM
110 120 130 140 150
MIACVVVFIA MQILGDQEVM LWLAWPFDPT LKFEFWRYFT HALMHFSLMH
160 170 180 190 200
ILFNLLWWWY LGGAVEKRLG SGKLIVITLI SALLSGYVQQ KFSGPWFGGL
210 220 230 240 250
SGVVYALMGY VWLRGERDPQ SGIYLQRGLI IFALIWIVAG WFDLFGMSMA
260 270
NGAHIAGLAV GLAMAFVDSL NARKRK
Length:276
Mass (Da):31,307
Last modified:October 11, 2004 - v5
Checksum:i6F67374E609968FC
GO

Sequence cautioni

The sequence AAA58222 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti51 – 52EL → DV in AAA23890 (PubMed:3045764).Curated2
Sequence conflicti51 – 52EL → DV in CAA30398 (PubMed:3045764).Curated2
Sequence conflicti51 – 52EL → DV in AAC28166 (PubMed:8955387).Curated2
Sequence conflicti51 – 52EL → DV in AAA58222 (PubMed:9278503).Curated2
Sequence conflicti178 – 179TL → RS in AAA23890 (PubMed:3045764).Curated2
Sequence conflicti178 – 179TL → RS in CAA30398 (PubMed:3045764).Curated2
Sequence conflicti193S → T in AAA23890 (PubMed:3045764).Curated1
Sequence conflicti193S → T in CAA30398 (PubMed:3045764).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M54940 Genomic DNA. Translation: AAA23890.1.
X07520 Genomic DNA. Translation: CAA30398.1.
M96795 Genomic DNA. Translation: AAC28166.1.
U18997 Genomic DNA. Translation: AAA58222.1. Different initiation.
U00096 Genomic DNA. Translation: AAT48182.1.
AP009048 Genomic DNA. Translation: BAE77868.1.
PIRiC65138. BVECGG.
RefSeqiWP_000928723.1. NZ_LN832404.1.
YP_026220.1. NC_000913.3.

Genome annotation databases

EnsemblBacteriaiAAT48182; AAT48182; b3424.
BAE77868; BAE77868; BAE77868.
GeneIDi947936.
KEGGiecj:JW5687.
eco:b3424.
PATRICi32122284. VBIEscCol129921_3519.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M54940 Genomic DNA. Translation: AAA23890.1.
X07520 Genomic DNA. Translation: CAA30398.1.
M96795 Genomic DNA. Translation: AAC28166.1.
U18997 Genomic DNA. Translation: AAA58222.1. Different initiation.
U00096 Genomic DNA. Translation: AAT48182.1.
AP009048 Genomic DNA. Translation: BAE77868.1.
PIRiC65138. BVECGG.
RefSeqiWP_000928723.1. NZ_LN832404.1.
YP_026220.1. NC_000913.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2IC8X-ray2.10A91-272[»]
2IRVX-ray2.30A/B92-273[»]
2LEPNMR-A1-61[»]
2NRFX-ray2.60A/B91-272[»]
2O7LX-ray2.50A93-272[»]
2XOVX-ray1.65A91-271[»]
2XOWX-ray2.09A92-270[»]
2XTUX-ray1.85A91-271[»]
2XTVX-ray1.70A93-272[»]
3B44X-ray1.70A91-270[»]
3B45X-ray1.90A91-270[»]
3TXTX-ray2.30A92-270[»]
3UBBX-ray2.60A91-272[»]
3ZEBX-ray2.20A92-270[»]
3ZMHX-ray2.30A91-270[»]
3ZMIX-ray2.20A92-270[»]
3ZMJX-ray2.30A92-270[»]
3ZOTX-ray2.40A92-271[»]
4H1DX-ray2.90A92-270[»]
4HDDX-ray1.35A2-74[»]
4NJNX-ray2.40A87-276[»]
4NJPX-ray2.40A87-276[»]
5F5BX-ray2.30A87-276[»]
5F5DX-ray2.50A87-276[»]
5F5GX-ray2.30A87-276[»]
5F5JX-ray2.40A87-276[»]
5F5KX-ray2.40A87-276[»]
ProteinModelPortaliP09391.
SMRiP09391.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262105. 13 interactors.
DIPiDIP-9796N.
IntActiP09391. 2 interactors.
STRINGi511145.b3424.

Chemistry databases

BindingDBiP09391.

Protein family/group databases

MEROPSiS54.016.
TCDBi9.B.104.1.1. the rhomboid protease (rhomboid) family.

Proteomic databases

PaxDbiP09391.
PRIDEiP09391.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAT48182; AAT48182; b3424.
BAE77868; BAE77868; BAE77868.
GeneIDi947936.
KEGGiecj:JW5687.
eco:b3424.
PATRICi32122284. VBIEscCol129921_3519.

Organism-specific databases

EchoBASEiEB0392.
EcoGeneiEG10397. glpG.

Phylogenomic databases

eggNOGiENOG4105EBW. Bacteria.
COG0705. LUCA.
HOGENOMiHOG000269640.
InParanoidiP09391.
KOiK02441.
OMAiHFSAMHI.
PhylomeDBiP09391.

Enzyme and pathway databases

BioCyciEcoCyc:EG10397-MONOMER.
ECOL316407:JW5687-MONOMER.
MetaCyc:EG10397-MONOMER.
BRENDAi3.4.21.105. 2026.

Miscellaneous databases

EvolutionaryTraceiP09391.
PROiP09391.

Family and domain databases

Gene3Di1.20.1540.10. 1 hit.
HAMAPiMF_01594. Rhomboid_GlpG. 1 hit.
InterProiIPR022732. Peptidase_S54_GlpG_N.
IPR002610. Peptidase_S54_rhomboid.
IPR022764. Peptidase_S54_rhomboid_dom.
IPR023662. Rhomboid_protease_GlpG.
[Graphical view]
PANTHERiPTHR22936. PTHR22936. 1 hit.
PfamiPF01694. Rhomboid. 1 hit.
PF12122. Rhomboid_N. 1 hit.
[Graphical view]
TIGRFAMsiTIGR04239. rhombo_GlpG. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiGLPG_ECOLI
AccessioniPrimary (citable) accession number: P09391
Secondary accession number(s): P76691, Q2M788, Q6BF32
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: October 11, 2004
Last modified: November 2, 2016
This is version 140 of the entry and version 5 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

Was originally identified as a repressor of the glycerol-3-phosphate regulon.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Peptidase families
    Classification of peptidase families and list of entries
  4. 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.