GLPG_ECO5E
ID GLPG_ECO5E Reviewed; 276 AA.
AC B5YTX6;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Rhomboid protease GlpG {ECO:0000255|HAMAP-Rule:MF_01594};
DE EC=3.4.21.105 {ECO:0000255|HAMAP-Rule:MF_01594};
DE AltName: Full=Intramembrane serine protease {ECO:0000255|HAMAP-Rule:MF_01594};
GN Name=glpG {ECO:0000255|HAMAP-Rule:MF_01594};
GN OrderedLocusNames=ECH74115_4732;
OS Escherichia coli O157:H7 (strain EC4115 / EHEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=444450;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EC4115 / EHEC;
RX PubMed=22135463; DOI=10.1073/pnas.1107176108;
RA Eppinger M., Mammel M.K., Leclerc J.E., Ravel J., Cebula T.A.;
RT "Genomic anatomy of Escherichia coli O157:H7 outbreaks.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20142-20147(2011).
CC -!- FUNCTION: Rhomboid-type serine protease that catalyzes intramembrane
CC proteolysis. {ECO:0000255|HAMAP-Rule:MF_01594}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleaves type-1 transmembrane domains using a catalytic dyad
CC composed of serine and histidine that are contributed by different
CC transmembrane domains.; EC=3.4.21.105; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01594};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01594}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01594}.
CC -!- SIMILARITY: Belongs to the peptidase S54 family. {ECO:0000255|HAMAP-
CC Rule:MF_01594}.
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DR EMBL; CP001164; ACI36519.1; -; Genomic_DNA.
DR RefSeq; WP_000928722.1; NC_011353.1.
DR AlphaFoldDB; B5YTX6; -.
DR SMR; B5YTX6; -.
DR MEROPS; S54.016; -.
DR KEGG; ecf:ECH74115_4732; -.
DR HOGENOM; CLU_058989_0_0_6; -.
DR OMA; LLGHCWI; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-UniRule.
DR Gene3D; 1.20.1540.10; -; 1.
DR Gene3D; 3.30.70.2350; -; 1.
DR HAMAP; MF_01594; Rhomboid_GlpG; 1.
DR InterPro; IPR038236; GlpG_N_sf.
DR InterPro; IPR022732; Peptidase_S54_GlpG_N.
DR InterPro; IPR022764; Peptidase_S54_rhomboid_dom.
DR InterPro; IPR035952; Rhomboid-like_sf.
DR InterPro; IPR023662; Rhomboid_protease_GlpG.
DR Pfam; PF01694; Rhomboid; 1.
DR Pfam; PF12122; Rhomboid_N; 1.
DR SUPFAM; SSF144091; SSF144091; 1.
DR TIGRFAMs; TIGR04239; rhombo_GlpG; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Hydrolase; Membrane; Protease;
KW Serine protease; Transmembrane; Transmembrane helix.
FT CHAIN 1..276
FT /note="Rhomboid protease GlpG"
FT /id="PRO_1000147853"
FT TRANSMEM 94..114
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01594"
FT TRANSMEM 142..162
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01594"
FT TRANSMEM 169..189
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01594"
FT TRANSMEM 192..212
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01594"
FT TRANSMEM 229..249
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01594"
FT TRANSMEM 250..270
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01594"
FT ACT_SITE 201
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01594"
FT ACT_SITE 254
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01594"
SQ SEQUENCE 276 AA; 31277 MW; 7B367D1E8E98D8FC CRC64;
MLMITSFANP RVAQAFVDYM ATQGVILTIQ QHNQSDVWLA DESQAERVRA ELARFLENPA
DPRYLAASWQ AGHTGSGLHY RRYPFFAALR ERAGPVTWVM MIACVVVFIA MQILGDQEVM
LWLAWPFDPA LKFEFWRYFT HALMHFSLMH ILFNLLWWWY LGGAVEKRLG SGKLIVITLI
SALLSGYVQQ KFSGPWFGGL SGVVYALMGY VWLRGERDPQ SGIYLQRGLI IFALIWIVAG
WFDLFGMSMA NGAHIAGLAV GLAMAFVDSL NARKRK
