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P09391

- GLPG_ECOLI

UniProt

P09391 - GLPG_ECOLI

Protein

Rhomboid protease GlpG

Gene

glpG

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 5 (11 Oct 2004)
      Previous versions | rss
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    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

    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

    GO - Cellular componenti

    1. integral component of plasma membrane Source: EcoCyc

    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 – 98
    Helixi10 – 2213
    Beta strandi27 – 304
    Beta strandi32 – 409
    Helixi42 – 443
    Helixi45 – 5713
    Helixi62 – 654
    Helixi95 – 11420
    Helixi116 – 1238
    Helixi129 – 1313
    Helixi137 – 1404
    Helixi141 – 1433
    Helixi148 – 16922
    Helixi171 – 19323
    Helixi201 – 21717
    Helixi219 – 2213
    Helixi227 – 24115
    Turni242 – 2454
    Helixi251 – 27020

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 9393CytoplasmicCuratedAdd
    BLAST
    Topological domaini115 – 14127PeriplasmicCuratedAdd
    BLAST
    Topological domaini163 – 1686CytoplasmicCurated
    Topological domaini190 – 1912PeriplasmicCurated
    Topological domaini213 – 22210CytoplasmicCurated
    Topological domaini246 – 2494PeriplasmicCurated
    Topological domaini273 – 2764CytoplasmicCurated

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei94 – 11421Helical; Name=1CuratedAdd
    BLAST
    Transmembranei142 – 16221Helical; Name=2CuratedAdd
    BLAST
    Transmembranei169 – 18921Helical; Name=3CuratedAdd
    BLAST
    Transmembranei192 – 21221Helical; Name=4CuratedAdd
    BLAST
    Transmembranei223 – 24523Helical; Name=5CuratedAdd
    BLAST
    Transmembranei250 – 27223Helical; Name=6CuratedAdd
    BLAST

    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.
    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

    MLMITSFANP RVAQAFVDYM ATQGVILTIQ QHNQSDVWLA DESQAERVRA    50
    ELARFLENPA DPRYLAASWQ AGHTGSGLHY RRYPFFAALR ERAGPVTWVM 100
    MIACVVVFIA MQILGDQEVM LWLAWPFDPT LKFEFWRYFT HALMHFSLMH 150
    ILFNLLWWWY LGGAVEKRLG SGKLIVITLI SALLSGYVQQ KFSGPWFGGL 200
    SGVVYALMGY VWLRGERDPQ SGIYLQRGLI IFALIWIVAG WFDLFGMSMA 250
    NGAHIAGLAV GLAMAFVDSL NARKRK 276
    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.

    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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.
    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

    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: October 1, 2014
    This is version 125 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