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Protein

Rhomboid protease GlpG

Gene

glpG

Organism
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Rhomboid-type serine protease that catalyzes intramembrane proteolysis.By similarity

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 sitei116 – 1161Nucleophile1 Publication
Active sitei169 – 16911 Publication

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • serine-type endopeptidase activity Source: GO_Central

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Enzyme and pathway databases

BRENDAi3.4.21.105. 2529.

Protein family/group databases

MEROPSiS54.024.

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:HI_0618
OrganismiHaemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Taxonomic identifieri71421 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus
Proteomesi
  • UP000000579 Componenti: Chromosome

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1010CytoplasmicSequence analysis
Transmembranei11 – 3121Helical; Name=1Sequence analysisAdd
BLAST
Topological domaini32 – 5726PeriplasmicSequence analysisAdd
BLAST
Transmembranei58 – 7821Helical; Name=2Sequence analysisAdd
BLAST
Topological domaini79 – 824CytoplasmicSequence analysis
Transmembranei83 – 10321Helical; Name=3Sequence analysisAdd
BLAST
Topological domaini104 – 1074PeriplasmicSequence analysis
Transmembranei108 – 12821Helical; Name=4Sequence analysisAdd
BLAST
Topological domaini129 – 14113CytoplasmicSequence analysisAdd
BLAST
Transmembranei142 – 16221Helical; Name=5Sequence analysisAdd
BLAST
Topological domaini163 – 1631PeriplasmicSequence analysis
Transmembranei164 – 18421Helical; Name=6Sequence analysisAdd
BLAST
Topological domaini185 – 1928CytoplasmicSequence analysis

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 192192Rhomboid protease GlpGPRO_0000087516Add
BLAST

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-10098079,EBI-10098079

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

IntActiP44783. 1 interaction.
STRINGi71421.HI0618.

Structurei

Secondary structure

1
192
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi10 – 2718Combined sources
Helixi31 – 388Combined sources
Helixi44 – 485Combined sources
Helixi52 – 554Combined sources
Helixi56 – 583Combined sources
Helixi63 – 8422Combined sources
Helixi86 – 10823Combined sources
Helixi116 – 13116Combined sources
Turni144 – 1485Combined sources
Turni150 – 1523Combined sources
Helixi153 – 1564Combined sources
Helixi166 – 19126Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2NR9X-ray2.20A1-192[»]
3ODJX-ray2.84A1-192[»]
ProteinModelPortaliP44783.
SMRiP44783. Positions 4-192.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP44783.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S54 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105EBW. Bacteria.
COG0705. LUCA.
KOiK02441.
OMAiPEGFFTM.
OrthoDBiEOG60SCRR.
PhylomeDBiP44783.

Family and domain databases

Gene3Di1.20.1540.10. 1 hit.
InterProiIPR002610. Peptidase_S54_rhomboid.
IPR022764. Peptidase_S54_rhomboid_dom.
[Graphical view]
PANTHERiPTHR22936. PTHR22936. 1 hit.
PfamiPF01694. Rhomboid. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P44783-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKNFLAQQGK ITLILTALCV LIYLAQQLGF EDDIMYLMHY PAYEEQDSEV
60 70 80 90 100
WRYISHTLVH LSNLHILFNL SWFFIFGGMI ERTFGSVKLL MLYVVASAIT
110 120 130 140 150
GYVQNYVSGP AFFGLSGVVY AVLGYVFIRD KLNHHLFDLP EGFFTMLLVG
160 170 180 190
IALGFISPLF GVEMGNAAHI SGLIVGLIWG FIDSKLRKNS LE
Length:192
Mass (Da):21,657
Last modified:November 1, 1995 - v1
Checksum:iB76A7A658037217E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L42023 Genomic DNA. Translation: AAC22277.1.
PIRiI64081.
RefSeqiNP_438776.1. NC_000907.1.
WP_005648561.1. NC_000907.1.

Genome annotation databases

EnsemblBacteriaiAAC22277; AAC22277; HI_0618.
GeneIDi950685.
KEGGihin:HI0618.
PATRICi20189819. VBIHaeInf48452_0642.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L42023 Genomic DNA. Translation: AAC22277.1.
PIRiI64081.
RefSeqiNP_438776.1. NC_000907.1.
WP_005648561.1. NC_000907.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2NR9X-ray2.20A1-192[»]
3ODJX-ray2.84A1-192[»]
ProteinModelPortaliP44783.
SMRiP44783. Positions 4-192.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP44783. 1 interaction.
STRINGi71421.HI0618.

Protein family/group databases

MEROPSiS54.024.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC22277; AAC22277; HI_0618.
GeneIDi950685.
KEGGihin:HI0618.
PATRICi20189819. VBIHaeInf48452_0642.

Phylogenomic databases

eggNOGiENOG4105EBW. Bacteria.
COG0705. LUCA.
KOiK02441.
OMAiPEGFFTM.
OrthoDBiEOG60SCRR.
PhylomeDBiP44783.

Enzyme and pathway databases

BRENDAi3.4.21.105. 2529.

Miscellaneous databases

EvolutionaryTraceiP44783.

Family and domain databases

Gene3Di1.20.1540.10. 1 hit.
InterProiIPR002610. Peptidase_S54_rhomboid.
IPR022764. Peptidase_S54_rhomboid_dom.
[Graphical view]
PANTHERiPTHR22936. PTHR22936. 1 hit.
PfamiPF01694. Rhomboid. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.
  2. "The crystal structure of the rhomboid peptidase from Haemophilus influenzae provides insight into intramembrane proteolysis."
    Lemieux M.J., Fischer S.J., Cherney M.M., Bateman K.S., James M.N.G.
    Proc. Natl. Acad. Sci. U.S.A. 104:750-754(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), ACTIVE SITE, REACTION MECHANISM, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiGLPG_HAEIN
AccessioniPrimary (citable) accession number: P44783
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: February 17, 2016
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Haemophilus influenzae
    Haemophilus influenzae (strain Rd): entries and gene names
  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.