GLPG_YERP3
ID GLPG_YERP3 Reviewed; 278 AA.
AC A7FNW6;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 83.
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=YpsIP31758_3996;
OS Yersinia pseudotuberculosis serotype O:1b (strain IP 31758).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=349747;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IP 31758;
RX PubMed=17784789; DOI=10.1371/journal.pgen.0030142;
RA Eppinger M., Rosovitz M.J., Fricke W.F., Rasko D.A., Kokorina G.,
RA Fayolle C., Lindler L.E., Carniel E., Ravel J.;
RT "The complete genome sequence of Yersinia pseudotuberculosis IP31758, the
RT causative agent of Far East scarlet-like fever.";
RL PLoS Genet. 3:1508-1523(2007).
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; CP000720; ABS48326.1; -; Genomic_DNA.
DR RefSeq; WP_002216348.1; NC_009708.1.
DR AlphaFoldDB; A7FNW6; -.
DR SMR; A7FNW6; -.
DR MEROPS; S54.016; -.
DR EnsemblBacteria; ABS48326; ABS48326; YpsIP31758_3996.
DR GeneID; 57974477; -.
DR KEGG; ypi:YpsIP31758_3996; -.
DR HOGENOM; CLU_058989_0_0_6; -.
DR OMA; LLGHCWI; -.
DR Proteomes; UP000002412; 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..278
FT /note="Rhomboid protease GlpG"
FT /id="PRO_0000321705"
FT TRANSMEM 94..114
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01594"
FT TRANSMEM 143..163
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01594"
FT TRANSMEM 175..195
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01594"
FT TRANSMEM 196..216
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01594"
FT TRANSMEM 224..241
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01594"
FT TRANSMEM 245..267
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01594"
FT ACT_SITE 202
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01594"
FT ACT_SITE 255
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01594"
SQ SEQUENCE 278 AA; 31305 MW; FEDBBAE0532C9AB4 CRC64;
MTRVIVISNL RLAQAFVDYM ATHHVALEIR PDAQGVEIWL ADDEQLSAVQ HELEQFLLDP
LNPRYQAASW QAGNVNSNLP YQRFSYLQTL RSQAGPLTLS VMVLCIAIYI LMLITGDMAV
MSWLAWPYNS SQYLQIWRWV SHAFLHFSLL HILFNLMWWW YLGGQMEKRL GTSKLLVLTI
VSAVFSGWGQ SLFSGANFGG LSGVVYALMG YVWLTGERAP ERGISLPRGL MAFSVLWLIA
GYFDILGLSI ANAAHVSGLI IGLLMAFWDT RNSARTVQ
