GLPG_ECO45
ID GLPG_ECO45 Reviewed; 276 AA.
AC B7MDQ0;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 75.
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}; OrderedLocusNames=ECS88_3813;
OS Escherichia coli O45:K1 (strain S88 / ExPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585035;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S88 / ExPEC;
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
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; CU928161; CAR05025.1; -; Genomic_DNA.
DR RefSeq; WP_000928723.1; NC_011742.1.
DR AlphaFoldDB; B7MDQ0; -.
DR SMR; B7MDQ0; -.
DR MEROPS; S54.016; -.
DR EnsemblBacteria; CAR05025; CAR05025; ECS88_3813.
DR GeneID; 58460244; -.
DR KEGG; ecz:ECS88_3813; -.
DR HOGENOM; CLU_058989_0_0_6; -.
DR OMA; LLGHCWI; -.
DR Proteomes; UP000000747; Chromosome.
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_1000147852"
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; 31307 MW; 6F67374E609968FC CRC64;
MLMITSFANP RVAQAFVDYM ATQGVILTIQ QHNQSDVWLA DESQAERVRA ELARFLENPA
DPRYLAASWQ AGHTGSGLHY RRYPFFAALR ERAGPVTWVM MIACVVVFIA MQILGDQEVM
LWLAWPFDPT LKFEFWRYFT HALMHFSLMH ILFNLLWWWY LGGAVEKRLG SGKLIVITLI
SALLSGYVQQ KFSGPWFGGL SGVVYALMGY VWLRGERDPQ SGIYLQRGLI IFALIWIVAG
WFDLFGMSMA NGAHIAGLAV GLAMAFVDSL NARKRK
