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GLPG_YERPN
ID   GLPG_YERPN              Reviewed;         278 AA.
AC   Q1CCK6; D1Q2W6;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 89.
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=YPN_3947;
GN   ORFNames=YP516_4479;
OS   Yersinia pestis bv. Antiqua (strain Nepal516).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=377628;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nepal516;
RX   PubMed=16740952; DOI=10.1128/jb.00124-06;
RA   Chain P.S.G., Hu P., Malfatti S.A., Radnedge L., Larimer F., Vergez L.M.,
RA   Worsham P., Chu M.C., Andersen G.L.;
RT   "Complete genome sequence of Yersinia pestis strains Antiqua and Nepal516:
RT   evidence of gene reduction in an emerging pathogen.";
RL   J. Bacteriol. 188:4453-4463(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nepal516;
RA   Plunkett G. III, Anderson B.D., Baumler D.J., Burland V., Cabot E.L.,
RA   Glasner J.D., Mau B., Neeno-Eckwall E., Perna N.T., Munk A.C., Tapia R.,
RA   Green L.D., Rogers Y.C., Detter J.C., Bruce D.C., Brettin T.S.;
RT   "Yersinia pestis Nepal516A whole genome shotgun sequencing project.";
RL   Submitted (APR-2009) 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}.
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DR   EMBL; CP000305; ABG20274.1; -; Genomic_DNA.
DR   EMBL; ACNQ01000019; EEO74869.1; -; Genomic_DNA.
DR   RefSeq; WP_002216348.1; NZ_ACNQ01000019.1.
DR   AlphaFoldDB; Q1CCK6; -.
DR   SMR; Q1CCK6; -.
DR   EnsemblBacteria; ABG20274; ABG20274; YPN_3947.
DR   GeneID; 57974477; -.
DR   KEGG; ypn:YPN_3947; -.
DR   HOGENOM; CLU_058989_0_0_6; -.
DR   OMA; LLGHCWI; -.
DR   Proteomes; UP000008936; 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_0000321702"
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
 
 
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