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P09391 (GLPG_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Rhomboid protease GlpG

EC=3.4.21.105
Alternative name(s):
Intramembrane serine protease
Gene names
Name:glpG
Ordered Locus Names:b3424, JW5687
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length276 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Rhomboid-type serine protease that catalyzes intramembrane proteolysis. Ref.6 Ref.7

Catalytic activity

Cleaves type-1 transmembrane domains using a catalytic dyad composed of serine and histidine that are contributed by different transmembrane domains. HAMAP-Rule MF_01594

Subcellular location

Cell inner membrane; Multi-pass membrane protein Ref.7.

Domain

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. Ref.6

Sequence similarities

Belongs to the peptidase S54 family.

Caution

Was originally (Ref.2) identified as a repressor of the glycerol-3-phosphate regulon.

Sequence caution

The sequence AAA58222.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 276276Rhomboid protease GlpG HAMAP-Rule MF_01594
PRO_0000087515

Regions

Topological domain1 – 9393Cytoplasmic Probable
Transmembrane94 – 11421Helical; Name=1; Probable
Topological domain115 – 14127Periplasmic Probable
Transmembrane142 – 16221Helical; Name=2; Probable
Topological domain163 – 1686Cytoplasmic Probable
Transmembrane169 – 18921Helical; Name=3; Probable
Topological domain190 – 1912Periplasmic Probable
Transmembrane192 – 21221Helical; Name=4; Probable
Topological domain213 – 22210Cytoplasmic Probable
Transmembrane223 – 24523Helical; Name=5; Probable
Topological domain246 – 2494Periplasmic Probable
Transmembrane250 – 27223Helical; Name=6; Probable
Topological domain273 – 2764Cytoplasmic Probable

Sites

Active site2011Nucleophile Ref.6 Ref.11 Ref.12 Ref.13
Active site2541 Ref.6 Ref.11 Ref.12 Ref.13

Experimental info

Mutagenesis1541N → A: Reduced catalytic activity. Ref.7 Ref.9
Mutagenesis1991G → C: Loss of catalytic activity. Ref.10
Mutagenesis2011S → A or C: Loss of catalytic activity. Ref.6 Ref.7 Ref.9 Ref.10
Mutagenesis2541H → A or C: Loss of catalytic activity. Ref.7 Ref.9 Ref.10
Sequence conflict51 – 522EL → DV in AAA23890. Ref.1
Sequence conflict51 – 522EL → DV in CAA30398. Ref.1
Sequence conflict51 – 522EL → DV in AAC28166. Ref.2
Sequence conflict51 – 522EL → DV in AAA58222. Ref.3
Sequence conflict178 – 1792TL → RS in AAA23890. Ref.1
Sequence conflict178 – 1792TL → RS in CAA30398. Ref.1
Sequence conflict1931S → T in AAA23890. Ref.1
Sequence conflict1931S → T in CAA30398. Ref.1

Secondary structure

................................... 276
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P09391 [UniParc].

Last modified October 11, 2004. Version 5.
Checksum: 6F67374E609968FC

FASTA27631,307
        10         20         30         40         50         60 
MLMITSFANP RVAQAFVDYM ATQGVILTIQ QHNQSDVWLA DESQAERVRA ELARFLENPA 

        70         80         90        100        110        120 
DPRYLAASWQ AGHTGSGLHY RRYPFFAALR ERAGPVTWVM MIACVVVFIA MQILGDQEVM 

       130        140        150        160        170        180 
LWLAWPFDPT LKFEFWRYFT HALMHFSLMH ILFNLLWWWY LGGAVEKRLG SGKLIVITLI 

       190        200        210        220        230        240 
SALLSGYVQQ KFSGPWFGGL SGVVYALMGY VWLRGERDPQ SGIYLQRGLI IFALIWIVAG 

       250        260        270 
WFDLFGMSMA NGAHIAGLAV GLAMAFVDSL NARKRK 

« Hide

References

« Hide 'large scale' references
[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]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"Escherichia coli K-12: a cooperatively developed annotation snapshot -- 2005."
Riley M., Abe T., Arnaud M.B., Berlyn M.K.B., Blattner F.R., Chaudhuri R.R., Glasner J.D., Horiuchi T., Keseler I.M., Kosuge T., Mori H., Perna N.T., Plunkett G. III, Rudd K.E., Serres M.H., Thomas G.H., Thomson N.R., Wishart D., Wanner B.L.
Nucleic Acids Res. 34:1-9(2006) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRBVECGG. C65138.
RefSeqYP_026220.1. NC_000913.3.
YP_492009.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP09391.
SMRP09391. Positions 2-67, 91-271.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-9796N.
IntActP09391. 1 interaction.
STRING511145.b3424.

Protein family/group databases

MEROPSS54.016.
TCDB9.B.104.1.1. the rhomboid protease (rhomboid) family.

Proteomic databases

PRIDEP09391.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAT48182; AAT48182; b3424.
BAE77868; BAE77868; BAE77868.
GeneID12933111.
947936.
KEGGecj:Y75_p3753.
eco:b3424.
PATRIC32122284. VBIEscCol129921_3519.

Organism-specific databases

EchoBASEEB0392.
EcoGeneEG10397. glpG.

Phylogenomic databases

eggNOGCOG0705.
HOGENOMHOG000269640.
KOK02441.
OMARWFSHAL.
OrthoDBEOG60SCRR.
PhylomeDBP09391.

Enzyme and pathway databases

BioCycEcoCyc:EG10397-MONOMER.
ECOL316407:JW5687-MONOMER.
MetaCyc:EG10397-MONOMER.
BRENDA3.4.21.105. 2026.

Gene expression databases

GenevestigatorP09391.

Family and domain databases

Gene3D1.20.1540.10. 1 hit.
HAMAPMF_01594. Rhomboid_GlpG.
InterProIPR022732. Peptidase_S54_GlpG_N.
IPR002610. Peptidase_S54_rhomboid.
IPR022764. Peptidase_S54_rhomboid_dom.
IPR023662. Rhomboid_protease_GlpG.
[Graphical view]
PANTHERPTHR22936. PTHR22936. 1 hit.
PfamPF12122. DUF3582. 1 hit.
PF01694. Rhomboid. 1 hit.
[Graphical view]
TIGRFAMsTIGR04239. rhombo_GlpG. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP09391.
PROP09391.

Entry information

Entry nameGLPG_ECOLI
AccessionPrimary (citable) accession number: P09391
Secondary accession number(s): P76691, Q2M788, Q6BF32
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: October 11, 2004
Last modified: May 14, 2014
This is version 124 of the entry and version 5 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant 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