ID   GLPG_YERPP              Reviewed;         278 AA.
AC   A4TGR2;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 87.
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=YPDSF_0049;
OS   Yersinia pestis (strain Pestoides F).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=386656;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pestoides F;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Di Bartolo G., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Worsham P., Chu M., Bearden S., Garcia E.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Yersinia pestis Pestoides F.";
RL   Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000668; ABP38475.1; -; Genomic_DNA.
DR   RefSeq; WP_002216348.1; NZ_CP009715.1.
DR   AlphaFoldDB; A4TGR2; -.
DR   SMR; A4TGR2; -.
DR   GeneID; 57974477; -.
DR   KEGG; ypp:YPDSF_0049; -.
DR   PATRIC; fig|386656.14.peg.522; -.
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..278
FT                   /note="Rhomboid protease GlpG"
FT                   /id="PRO_0000321703"
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