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P09391

- GLPG_ECOLI

UniProt

P09391 - GLPG_ECOLI

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Protein

Rhomboid protease GlpG

Gene

glpG

Organism
Escherichia coli (strain K12)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei201 – 2011Nucleophile
Active sitei254 – 2541

GO - Molecular functioni

  1. endopeptidase activity Source: EcoCyc
  2. serine-type endopeptidase activity Source: EcoCyc

GO - Biological processi

  1. 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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10397. glpG.

Subcellular locationi

Cell inner membrane 1 Publication; Multi-pass membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 9393CytoplasmicCuratedAdd
BLAST
Transmembranei94 – 11421Helical; Name=1CuratedAdd
BLAST
Topological domaini115 – 14127PeriplasmicCuratedAdd
BLAST
Transmembranei142 – 16221Helical; Name=2CuratedAdd
BLAST
Topological domaini163 – 1686CytoplasmicCurated
Transmembranei169 – 18921Helical; Name=3CuratedAdd
BLAST
Topological domaini190 – 1912PeriplasmicCurated
Transmembranei192 – 21221Helical; Name=4CuratedAdd
BLAST
Topological domaini213 – 22210CytoplasmicCurated
Transmembranei223 – 24523Helical; Name=5CuratedAdd
BLAST
Topological domaini246 – 2494PeriplasmicCurated
Transmembranei250 – 27223Helical; Name=6CuratedAdd
BLAST
Topological domaini273 – 2764CytoplasmicCurated

GO - Cellular componenti

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

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi154 – 1541N → A: Reduced catalytic activity. 2 Publications
Mutagenesisi199 – 1991G → C: Loss of catalytic activity. 1 Publication
Mutagenesisi201 – 2011S → A or C: Loss of catalytic activity. 4 Publications
Mutagenesisi254 – 2541H → A or C: Loss of catalytic activity. 3 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 276276Rhomboid protease GlpGPRO_0000087515Add
BLAST

Proteomic databases

PRIDEiP09391.

Expressioni

Gene expression databases

GenevestigatoriP09391.

Interactioni

Protein-protein interaction databases

DIPiDIP-9796N.
IntActiP09391. 1 interaction.
STRINGi511145.b3424.

Structurei

Secondary structure

1
276
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 98Combined sources
Helixi10 – 2213Combined sources
Beta strandi27 – 304Combined sources
Beta strandi32 – 409Combined sources
Helixi42 – 443Combined sources
Helixi45 – 5713Combined sources
Helixi62 – 654Combined sources
Helixi95 – 11420Combined sources
Helixi116 – 1238Combined sources
Helixi129 – 1313Combined sources
Helixi137 – 1404Combined sources
Helixi141 – 1433Combined sources
Helixi148 – 16922Combined sources
Helixi171 – 19323Combined sources
Helixi201 – 21717Combined sources
Helixi219 – 2213Combined sources
Helixi227 – 24115Combined sources
Turni242 – 2454Combined sources
Helixi251 – 27020Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP09391.
SMRiP09391. Positions 2-67, 91-271.
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

eggNOGiCOG0705.
HOGENOMiHOG000269640.
InParanoidiP09391.
KOiK02441.
OMAiRWFSHAL.
OrthoDBiEOG60SCRR.
PhylomeDBiP09391.

Family and domain databases

Gene3Di1.20.1540.10. 1 hit.
HAMAPiMF_01594. Rhomboid_GlpG.
InterProiIPR022732. Peptidase_S54_GlpG_N.
IPR002610. Peptidase_S54_rhomboid.
IPR022764. Peptidase_S54_rhomboid_dom.
IPR023662. Rhomboid_protease_GlpG.
[Graphical view]
PANTHERiPTHR22936. PTHR22936. 1 hit.
PfamiPF12122. DUF3582. 1 hit.
PF01694. Rhomboid. 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 AAA58222.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti51 – 522EL → DV in AAA23890. (PubMed:3045764)Curated
Sequence conflicti51 – 522EL → DV in CAA30398. (PubMed:3045764)Curated
Sequence conflicti51 – 522EL → DV in AAC28166. (PubMed:8955387)Curated
Sequence conflicti51 – 522EL → DV in AAA58222. (PubMed:9278503)Curated
Sequence conflicti178 – 1792TL → RS in AAA23890. (PubMed:3045764)Curated
Sequence conflicti178 – 1792TL → RS in CAA30398. (PubMed:3045764)Curated
Sequence conflicti193 – 1931S → T in AAA23890. (PubMed:3045764)Curated
Sequence conflicti193 – 1931S → T in CAA30398. (PubMed:3045764)Curated

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.
RefSeqiYP_026220.1. NC_000913.3.
YP_492009.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAT48182; AAT48182; b3424.
BAE77868; BAE77868; BAE77868.
GeneIDi12933111.
947936.
KEGGiecj:Y75_p3753.
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 .
PIRi C65138. BVECGG.
RefSeqi YP_026220.1. NC_000913.3.
YP_492009.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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 [» ]
ProteinModelPortali P09391.
SMRi P09391. Positions 2-67, 91-271.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-9796N.
IntActi P09391. 1 interaction.
STRINGi 511145.b3424.

Protein family/group databases

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

Proteomic databases

PRIDEi P09391.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAT48182 ; AAT48182 ; b3424 .
BAE77868 ; BAE77868 ; BAE77868 .
GeneIDi 12933111.
947936.
KEGGi ecj:Y75_p3753.
eco:b3424.
PATRICi 32122284. VBIEscCol129921_3519.

Organism-specific databases

EchoBASEi EB0392.
EcoGenei EG10397. glpG.

Phylogenomic databases

eggNOGi COG0705.
HOGENOMi HOG000269640.
InParanoidi P09391.
KOi K02441.
OMAi RWFSHAL.
OrthoDBi EOG60SCRR.
PhylomeDBi P09391.

Enzyme and pathway databases

BioCyci EcoCyc:EG10397-MONOMER.
ECOL316407:JW5687-MONOMER.
MetaCyc:EG10397-MONOMER.
BRENDAi 3.4.21.105. 2026.

Miscellaneous databases

EvolutionaryTracei P09391.
PROi P09391.

Gene expression databases

Genevestigatori P09391.

Family and domain databases

Gene3Di 1.20.1540.10. 1 hit.
HAMAPi MF_01594. Rhomboid_GlpG.
InterProi IPR022732. Peptidase_S54_GlpG_N.
IPR002610. Peptidase_S54_rhomboid.
IPR022764. Peptidase_S54_rhomboid_dom.
IPR023662. Rhomboid_protease_GlpG.
[Graphical view ]
PANTHERi PTHR22936. PTHR22936. 1 hit.
Pfami PF12122. DUF3582. 1 hit.
PF01694. Rhomboid. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR04239. rhombo_GlpG. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence of the glpR gene encoding the repressor for the glycerol-3-phosphate regulon of Escherichia coli K12."
    Choi Y.-L., Kawase S., Nishida T., Sakai H., Komano T., Kawamukai M., Utsumi R., Kohara Y., Akiyama K.
    Nucleic Acids Res. 16:7732-7732(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  2. "Repressor for the sn-glycerol 3-phosphate regulon of Escherichia coli K-12: primary structure and identification of the DNA-binding domain."
    Zeng G., Ye S., Larson T.J.
    J. Bacteriol. 178:7080-7089(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-8.
    Strain: K12.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. Cited for: SEQUENCE REVISION TO 51-52.
  5. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  6. "Structural analysis of a rhomboid family intramembrane protease reveals a gating mechanism for substrate entry."
    Wu Z., Yan N., Feng L., Oberstein A., Yan H., Baker R.P., Gu L., Jeffrey P.D., Urban S., Shi Y.
    Nat. Struct. Mol. Biol. 13:1084-1091(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE, X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 87-272, FUNCTION, TOPOLOGY, ACTIVE SITE, DOMAIN, MUTAGENESIS OF SER-201.
  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.
  8. "Global topology analysis of the Escherichia coli inner membrane proteome."
    Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.
    Science 308:1321-1323(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
    Strain: K12 / MG1655 / ATCC 47076.
  9. "Functional characterization of Escherichia coli GlpG and additional rhomboid proteins using an aarA mutant of Providencia stuartii."
    Clemmer K.M., Sturgill G.M., Veenstra A., Rather P.N.
    J. Bacteriol. 188:3415-3419(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF ASN-154; SER-201 AND HIS-254.
  10. "The intramembrane active site of GlpG, an E. coli rhomboid protease, is accessible to water and hydrolyses an extramembrane peptide bond of substrates."
    Maegawa S., Koide K., Ito K., Akiyama Y.
    Mol. Microbiol. 64:435-447(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY, MUTAGENESIS OF GLY-199; SER-201 AND HIS-254.
  11. "Crystal structure of a rhomboid family intramembrane protease."
    Wang Y., Zhang Y., Ha Y.
    Nature 444:179-180(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 91-272, TOPOLOGY, ACTIVE SITE.
  12. "Structural basis for intramembrane proteolysis by rhomboid serine proteases."
    Ben-Shem A., Fass D., Bibi E.
    Proc. Natl. Acad. Sci. U.S.A. 104:462-466(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 92-273, TOPOLOGY, ACTIVE SITE.
  13. "Open-cap conformation of intramembrane protease GlpG."
    Wang Y., Ha Y.
    Proc. Natl. Acad. Sci. U.S.A. 104:2098-2102(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 93-272, ACTIVE SITE.

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 26, 2014
This is version 127 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

External Data

Dasty 3