GLPG_SALTI
ID GLPG_SALTI Reviewed; 276 AA.
AC Q8Z229; Q7C5W6;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 119.
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=STY4279, t3989;
OS Salmonella typhi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT CT18.";
RL J. Bacteriol. 185:2330-2337(2003).
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; AE014613; AAO71459.1; -; Genomic_DNA.
DR EMBL; AL513382; CAD08097.1; -; Genomic_DNA.
DR RefSeq; NP_458387.1; NC_003198.1.
DR RefSeq; WP_000928705.1; NZ_WSUR01000001.1.
DR AlphaFoldDB; Q8Z229; -.
DR SMR; Q8Z229; -.
DR STRING; 220341.16505076; -.
DR MEROPS; S54.016; -.
DR EnsemblBacteria; AAO71459; AAO71459; t3989.
DR KEGG; stt:t3989; -.
DR KEGG; sty:STY4279; -.
DR PATRIC; fig|220341.7.peg.4372; -.
DR eggNOG; COG0705; Bacteria.
DR HOGENOM; CLU_058989_0_0_6; -.
DR OMA; LLGHCWI; -.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; 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_0000321690"
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; 31427 MW; EA5129221DE6C52E CRC64;
MLMITSFANP RVAQAFVDYM ATQGVILTIQ QHNQSDIWLA DESQAERVRV ELARFIENPG
DPRYLAASWQ SGQTNSGLRY RRFPFLATLR ERAGPVTWIV MLACVVVYIA MSLIGDQTVM
VWLAWPFDPV LKFEVWRYFT HIFMHFSLMH ILFNLLWWWY LGGAVEKRLG SGKLIVITVI
SALLSGYVQQ KFSGPWFGGL SGVVYALMGY VWLRGERDPQ SGIYLQRGLI IFALLWIVAG
WFDWFGMSMA NGAHIAGLIV GLAMAFVDTL NARKRT
