ID   GLPG_SALPK              Reviewed;         276 AA.
AC   B5BHH5;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 69.
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=SSPA3157;
OS   Salmonella paratyphi A (strain AKU_12601).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=554290;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AKU_12601;
RX   PubMed=19159446; DOI=10.1186/1471-2164-10-36;
RA   Holt K.E., Thomson N.R., Wain J., Langridge G.C., Hasan R., Bhutta Z.A.,
RA   Quail M.A., Norbertczak H., Walker D., Simmonds M., White B., Bason N.,
RA   Mungall K., Dougan G., Parkhill J.;
RT   "Pseudogene accumulation in the evolutionary histories of Salmonella
RT   enterica serovars Paratyphi A and Typhi.";
RL   BMC Genomics 10:36-36(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; FM200053; CAR61412.1; -; Genomic_DNA.
DR   RefSeq; WP_000928706.1; NC_011147.1.
DR   AlphaFoldDB; B5BHH5; -.
DR   SMR; B5BHH5; -.
DR   KEGG; sek:SSPA3157; -.
DR   HOGENOM; CLU_058989_0_0_6; -.
DR   OMA; LLGHCWI; -.
DR   Proteomes; UP000001869; 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_1000147866"
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;  31457 MW;  EA51292201FB04EE CRC64;
     MLMITSFANP RVAQAFVDYM ATQGVILTIQ QHNQSDIWLA DESQAERVRV ELARFIENPG
     DPRYLAASWQ SGQTNSGLRY RRFPFLATLR ERAGPVTWIV MLACVVVYIA MSLIGDQTVM
     VWLAWPFDPV LKFEVWRYFT HIFMHFSLMH ILFNLLWWWY LGGAVEKRLG SGKLIVITVI
     SALLSGYVQQ KFSGPWFGGL SGVVYALMGY VWLRGERDPQ SGIYLQRGLI IFALLWIVAS
     WFDWFGMSMA NGAHIAGLIV GLAMAFVDTL NARKRT