GLPG_YERE8
ID GLPG_YERE8 Reviewed; 278 AA.
AC A1JSF0;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 82.
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=YE3988;
OS Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 /
OS 8081).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=393305;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 13174 / 8081;
RX PubMed=17173484; DOI=10.1371/journal.pgen.0020206;
RA Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L.,
RA Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T.,
RA Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S.,
RA Sanders M., Whitehead S., Quail M.A., Dougan G., Parkhill J.,
RA Prentice M.B.;
RT "The complete genome sequence and comparative genome analysis of the high
RT pathogenicity Yersinia enterocolitica strain 8081.";
RL PLoS Genet. 2:2039-2051(2006).
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; AM286415; CAL14008.1; -; Genomic_DNA.
DR RefSeq; WP_005174723.1; NC_008800.1.
DR RefSeq; YP_001008134.1; NC_008800.1.
DR AlphaFoldDB; A1JSF0; -.
DR SMR; A1JSF0; -.
DR STRING; 393305.YE3988; -.
DR MEROPS; S54.016; -.
DR EnsemblBacteria; CAL14008; CAL14008; YE3988.
DR KEGG; yen:YE3988; -.
DR PATRIC; fig|393305.7.peg.4246; -.
DR eggNOG; COG0705; Bacteria.
DR HOGENOM; CLU_058989_0_0_6; -.
DR OMA; LLGHCWI; -.
DR Proteomes; UP000000642; 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_0000321699"
FT TRANSMEM 95..115
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 170..190
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 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; 31336 MW; 28832C62E4335902 CRC64;
MVRVIAISNL RLAQAFVDYM ATRHVALEVK PDSQGAEIWL TDDEQLPQVQ HELEQFLLDP
LNPRYQAASW QSGNLHSNLP YQRFSYLQTL RSQAGPLTLS VMVLCIAIYI LMQIVGDGAV
MSWLAWPRDN SQYLQIWRWV SHAFLHFSLL HILFNLMWWW YLAGQMEKRL GTGKLLVLTI
VSALFSGWGQ SLFSGVNFGG LSGVVYALMG YVWLTGERAP ERGISLPRGL MAFSVLWLVA
GYFDILGLSI ANAAHVSGLI IGLLMAFWDT RNSAKTTQ
