glpG

Functionⁱ

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

Caution

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

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 key	Position(s)	DescriptionActions	Graphical view	Length
Active siteⁱ	201	Nucleophile4 Publications		1
Active siteⁱ	254	4 Publications		1

GO - Molecular functionⁱ

endopeptidase activity
Source: EcoCyc
Inferred from mutant phenotypeⁱ
- 24315097
identical protein binding
Source: IntAct
Inferred from physical interactionⁱ
- 17051161
- 25009246
serine-type endopeptidase activity
Source: EcoCyc
Inferred from direct assayⁱ

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

proteolysis
Source: EcoCyc
Inferred from direct assayⁱ

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Hydrolase, Protease, Serine protease

Molecular function

Hydrolase, Protease, Serine protease

Enzyme and pathway databases

BioCycⁱ	EcoCyc:EG10397-MONOMER MetaCyc:EG10397-MONOMER
BRENDAⁱ	3.4.21.105 2026

Protein family/group databases

MEROPS protease database More...MEROPSⁱ	S54.016
TCDBⁱ	9.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
Organismⁱ	Escherichia coli (strain K12)
Taxonomic identifierⁱ	83333 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › Escherichia coli
Proteomesⁱ	UP000000318 Componentⁱ: Chromosome UP000000625 Componentⁱ: Chromosome

Organism-specific databases

EcoGeneⁱ	EG10397 glpG

EcoGeneⁱ

EG10397 glpG

Subcellular locationⁱ

Cell inner membrane
1 Publication
Manual assertion based on experiment inⁱ
- Ref.7
  "Proteolytic action of GlpG, a rhomboid protease in the Escherichia coli cytoplasmic membrane."
  Maegawa S., Ito K., Akiyama Y.
  Biochemistry 44:13543-13552(2005) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, MUTAGENESIS OF ASN-154; SER-201 AND HIS-254.
; Multi-pass membrane protein
1 Publication
Manual assertion based on experiment inⁱ
- Ref.7
  "Proteolytic action of GlpG, a rhomboid protease in the Escherichia coli cytoplasmic membrane."
  Maegawa S., Ito K., Akiyama Y.
  Biochemistry 44:13543-13552(2005) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, MUTAGENESIS OF ASN-154; SER-201 AND HIS-254.

Topology

Feature key	Position(s)	DescriptionActions	Length
Topological domainⁱ	1 – 93	CytoplasmicCuratedAdd BLAST	93
Transmembraneⁱ	94 – 114	Helical; Name=1CuratedAdd BLAST	21
Topological domainⁱ	115 – 141	PeriplasmicCuratedAdd BLAST	27
Transmembraneⁱ	142 – 162	Helical; Name=2CuratedAdd BLAST	21
Topological domainⁱ	163 – 168	CytoplasmicCurated	6
Transmembraneⁱ	169 – 189	Helical; Name=3CuratedAdd BLAST	21
Topological domainⁱ	190 – 191	PeriplasmicCurated	2
Transmembraneⁱ	192 – 212	Helical; Name=4CuratedAdd BLAST	21
Topological domainⁱ	213 – 222	CytoplasmicCurated	10
Transmembraneⁱ	223 – 245	Helical; Name=5CuratedAdd BLAST	23
Topological domainⁱ	246 – 249	PeriplasmicCurated	4
Transmembraneⁱ	250 – 272	Helical; Name=6CuratedAdd BLAST	23
Topological domainⁱ	273 – 276	CytoplasmicCurated	4

GO - Cellular componentⁱ

integral component of plasma membrane
Source: EcoCyc
Inferred from direct assayⁱ
- 16216077
plasma membrane
Source: EcoCyc
Inferred from direct assayⁱ

View the complete GO annotation on QuickGO ...

Keywords - Cellular componentⁱ

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	154	N → A: Reduced catalytic activity. 2 Publications	1
Mutagenesisⁱ	199	G → C: Loss of catalytic activity. 1 Publication	1
Mutagenesisⁱ	201	S → A or C: Loss of catalytic activity. 4 Publications	1
Mutagenesisⁱ	254	H → A or C: Loss of catalytic activity. 3 Publications	1

Chemistry databases

Drug and drug target database More...DrugBankⁱ	DB04147 Lauryl Dimethylamine-N-Oxide

DrugBankⁱ

DB04147 Lauryl Dimethylamine-N-Oxide

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000087515	1 – 276	Rhomboid protease GlpGAdd BLAST		276

Proteomic databases

PaxDbⁱ	P09391
PRIDEⁱ	P09391

Interactionⁱ

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
itself		3	EBI-9134140,EBI-9134140

With

Entry

#Exp.

IntAct

Notes

itself

3

EBI-9134140,EBI-9134140

GO - Molecular functionⁱ

identical protein binding
Source: IntAct
Inferred from physical interactionⁱ
- 17051161
- 25009246

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	4262105, 40 interactors
Database of interacting proteins More...DIPⁱ	DIP-9796N
IntActⁱ	P09391, 3 interactors
Molecular INTeraction database More...MINTⁱ	P09391
STRINGⁱ	316385.ECDH10B_3598

Chemistry databases

BindingDBⁱ

P09391

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	2 – 9	Combined sources	8
Helixⁱ	10 – 22	Combined sources	13
Beta strandⁱ	27 – 30	Combined sources	4
Beta strandⁱ	32 – 40	Combined sources	9
Helixⁱ	42 – 44	Combined sources	3
Helixⁱ	45 – 57	Combined sources	13
Helixⁱ	62 – 65	Combined sources	4
Helixⁱ	95 – 114	Combined sources	20
Helixⁱ	116 – 123	Combined sources	8
Helixⁱ	129 – 131	Combined sources	3
Helixⁱ	137 – 140	Combined sources	4
Helixⁱ	141 – 143	Combined sources	3
Helixⁱ	148 – 169	Combined sources	22
Helixⁱ	171 – 193	Combined sources	23
Helixⁱ	201 – 217	Combined sources	17
Helixⁱ	219 – 221	Combined sources	3
Helixⁱ	227 – 241	Combined sources	15
Turnⁱ	242 – 245	Combined sources	4
Turnⁱ	247 – 249	Combined sources	3
Helixⁱ	251 – 270	Combined sources	20

Show more details

3D structure databases

ProteinModelPortalⁱ	P09391
SMRⁱ	P09391
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ

P09391

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

eggNOGⁱ	ENOG4105EBW Bacteria COG0705 LUCA
HOGENOMⁱ	HOG000269640
InParanoidⁱ	P09391
KEGG Orthology (KO) More...KOⁱ	K02441
PhylomeDBⁱ	P09391

Family and domain databases

Gene3Dⁱ	1.20.1540.10, 1 hit 3.30.70.2350, 1 hit
HAMAPⁱ	MF_01594 Rhomboid_GlpG, 1 hit
InterProⁱ	View protein in InterPro IPR038236 GlpG_N_sf IPR022732 Peptidase_S54_GlpG_N IPR002610 Peptidase_S54_rhomboid IPR022764 Peptidase_S54_rhomboid_dom IPR035952 Rhomboid-like_sf IPR023662 Rhomboid_protease_GlpG
PANTHERⁱ	PTHR22936 PTHR22936, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF01694 Rhomboid, 1 hit PF12122 Rhomboid_N, 1 hit
TIGRFAMsⁱ	TIGR04239 rhombo_GlpG, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

P09391-1 [UniParc]FASTA Add 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 key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	51 – 52	EL → DV in AAA23890 (PubMed:3045764).Curated	2
Sequence conflictⁱ	51 – 52	EL → DV in CAA30398 (PubMed:3045764).Curated	2
Sequence conflictⁱ	51 – 52	EL → DV in AAC28166 (PubMed:8955387).Curated	2
Sequence conflictⁱ	51 – 52	EL → DV in AAA58222 (PubMed:9278503).Curated	2
Sequence conflictⁱ	178 – 179	TL → RS in AAA23890 (PubMed:3045764).Curated	2
Sequence conflictⁱ	178 – 179	TL → RS in CAA30398 (PubMed:3045764).Curated	2
Sequence conflictⁱ	193	S → T in AAA23890 (PubMed:3045764).Curated	1
Sequence conflictⁱ	193	S → T in CAA30398 (PubMed:3045764).Curated	1

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
PIRⁱ	C65138 BVECGG
NCBI Reference Sequences More...RefSeqⁱ	WP_000928723.1, NZ_LN832404.1 YP_026220.1, NC_000913.3

Genome annotation databases

EnsemblBacteriaⁱ	AAT48182; AAT48182; b3424 BAE77868; BAE77868; BAE77868
GeneIDⁱ	947936
KEGGⁱ	ecj:JW5687 eco:b3424
PATRICⁱ	fig\|1411691.4.peg.3305

Protein	Similar proteins		Species	Score	Length	Source
P09391	Rhomboid protease GlpG		ECO27		276	UniRef100_B7UKC8
Rhomboid protease GlpG		ECO45		276
Rhomboid protease GlpG		ECOBW		276
Rhomboid protease GlpG		ECODH		276
Rhomboid protease GlpG		ECOHS		276
+76

Protein	Similar proteins		Species	Score	Length	Source
P09391	Rhomboid protease GlpG		SHIFL		276	UniRef90_Q83PV6
Rhomboid protease GlpG		ECO7I		276
Rhomboid protease GlpG		CITK8		276
Rhomboid protease GlpG		ECO24		276
Rhomboid protease GlpG		ECO55		276
+486

Protein	Similar proteins		Species	Score	Length	Source
P09391	Rhomboid protease GlpG		PECAS		276	UniRef50_Q6CZL3
Rhomboid protease GlpG		YERP3		278
Rhomboid protease GlpG		YERPA		278
Rhomboid protease GlpG		YERPB		278
Rhomboid protease GlpG		YERPE		278
+1675

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
PIRⁱ	C65138 BVECGG
RefSeqⁱ	WP_000928723.1, NZ_LN832404.1 YP_026220.1, NC_000913.3

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	2IC8	X-ray	2.10	A	91-272	[»]
	2IRV	X-ray	2.30	A/B	92-273	[»]
	2LEP	NMR	-	A	1-61	[»]
	2NRF	X-ray	2.60	A/B	91-272	[»]
	2O7L	X-ray	2.50	A	93-272	[»]
	2XOV	X-ray	1.65	A	91-271	[»]
	2XOW	X-ray	2.09	A	92-270	[»]
	2XTU	X-ray	1.85	A	91-271	[»]
	2XTV	X-ray	1.70	A	93-272	[»]
	3B44	X-ray	1.70	A	91-270	[»]
	3B45	X-ray	1.90	A	91-270	[»]
	3TXT	X-ray	2.30	A	92-270	[»]
	3UBB	X-ray	2.60	A	91-272	[»]
	3ZEB	X-ray	2.20	A	92-270	[»]
	3ZMH	X-ray	2.30	A	91-270	[»]
	3ZMI	X-ray	2.20	A	92-270	[»]
	3ZMJ	X-ray	2.30	A	92-270	[»]
	3ZOT	X-ray	2.40	A	92-271	[»]
	4H1D	X-ray	2.90	A	92-270	[»]
	4HDD	X-ray	1.35	A	2-74	[»]
	4NJN	X-ray	2.40	A	87-276	[»]
	4NJP	X-ray	2.40	A	87-276	[»]
	5F5B	X-ray	2.30	A	87-276	[»]
	5F5D	X-ray	2.50	A	87-276	[»]
	5F5G	X-ray	2.30	A	87-276	[»]
	5F5J	X-ray	2.40	A	87-276	[»]
	5F5K	X-ray	2.40	A	87-276	[»]
	5MT6	X-ray	2.16	A	91-270	[»]
	5MT7	X-ray	2.05	A	91-271	[»]
	5MT8	X-ray	1.95	A	92-270	[»]
ProteinModelPortalⁱ	P09391
SMRⁱ	P09391
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	4262105, 40 interactors
DIPⁱ	DIP-9796N
IntActⁱ	P09391, 3 interactors
MINTⁱ	P09391
STRINGⁱ	316385.ECDH10B_3598

Chemistry databases

BindingDBⁱ	P09391
DrugBankⁱ	DB04147 Lauryl Dimethylamine-N-Oxide

Protein family/group databases

MEROPSⁱ	S54.016
TCDBⁱ	9.B.104.1.1 the rhomboid protease (rhomboid) family

Proteomic databases

PaxDbⁱ	P09391
PRIDEⁱ	P09391

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

EnsemblBacteriaⁱ	AAT48182; AAT48182; b3424 BAE77868; BAE77868; BAE77868
GeneIDⁱ	947936
KEGGⁱ	ecj:JW5687 eco:b3424
PATRICⁱ	fig\|1411691.4.peg.3305

Organism-specific databases

EchoBASEⁱ	EB0392
EcoGeneⁱ	EG10397 glpG

Phylogenomic databases

eggNOGⁱ	ENOG4105EBW Bacteria COG0705 LUCA
HOGENOMⁱ	HOG000269640
InParanoidⁱ	P09391
KOⁱ	K02441
PhylomeDBⁱ	P09391

Enzyme and pathway databases

BioCycⁱ	EcoCyc:EG10397-MONOMER MetaCyc:EG10397-MONOMER
BRENDAⁱ	3.4.21.105 2026

Miscellaneous databases

EvolutionaryTraceⁱ	P09391
Protein Ontology More...PROⁱ	PR:P09391

Family and domain databases

Gene3Dⁱ	1.20.1540.10, 1 hit 3.30.70.2350, 1 hit
HAMAPⁱ	MF_01594 Rhomboid_GlpG, 1 hit
InterProⁱ	View protein in InterPro IPR038236 GlpG_N_sf IPR022732 Peptidase_S54_GlpG_N IPR002610 Peptidase_S54_rhomboid IPR022764 Peptidase_S54_rhomboid_dom IPR035952 Rhomboid-like_sf IPR023662 Rhomboid_protease_GlpG
PANTHERⁱ	PTHR22936 PTHR22936, 1 hit
Pfamⁱ	View protein in Pfam PF01694 Rhomboid, 1 hit PF12122 Rhomboid_N, 1 hit
TIGRFAMsⁱ	TIGR04239 rhombo_GlpG, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	GLPG_ECOLI
Accessionⁱ	P09391Primary (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 7, 2018
	This is version 152 of the entry and version 5 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Prokaryotic Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

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

Documents

SIMILARITY comments
Index of protein domains and families
Peptidase families
Classification of peptidase families and list of entries
PDB cross-references
Index of Protein Data Bank (PDB) cross-references
Escherichia coli
Escherichia coli (strain K12): entries and cross-references to EcoGene

UniProtKB

UniParc

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UniRef

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Supporting data

UniProtKB - P09391 (GLPG_ECOLI)

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Rhomboid protease GlpG

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Caution

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

Protein family/group databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Topology

GO - Cellular componenti

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Chemistry databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Proteomic databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

GO - Molecular functioni

Protein-protein interaction databases

Chemistry databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Phylogenomic databases

Family and domain databases

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

Experimental Info

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

Protein family/group databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Documents

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Sequence cautionⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ