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GLPG_ECOUT
ID   GLPG_ECOUT              Reviewed;         276 AA.
AC   Q1R5L1;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, 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=UTI89_C3924;
OS   Escherichia coli (strain UTI89 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=364106;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UTI89 / UPEC;
RX   PubMed=16585510; DOI=10.1073/pnas.0600938103;
RA   Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A.,
RA   Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S.,
RA   Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J.,
RA   Gordon J.I.;
RT   "Identification of genes subject to positive selection in uropathogenic
RT   strains of Escherichia coli: a comparative genomics approach.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(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; CP000243; ABE09353.1; -; Genomic_DNA.
DR   RefSeq; WP_000928723.1; NC_007946.1.
DR   AlphaFoldDB; Q1R5L1; -.
DR   SMR; Q1R5L1; -.
DR   MEROPS; S54.016; -.
DR   EnsemblBacteria; ABE09353; ABE09353; UTI89_C3924.
DR   GeneID; 58460244; -.
DR   KEGG; eci:UTI89_C3924; -.
DR   HOGENOM; CLU_058989_0_0_6; -.
DR   OMA; LLGHCWI; -.
DR   Proteomes; UP000001952; 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_0000321679"
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;  31307 MW;  6F67374E609968FC CRC64;
     MLMITSFANP RVAQAFVDYM ATQGVILTIQ QHNQSDVWLA DESQAERVRA ELARFLENPA
     DPRYLAASWQ AGHTGSGLHY RRYPFFAALR ERAGPVTWVM MIACVVVFIA MQILGDQEVM
     LWLAWPFDPT LKFEFWRYFT HALMHFSLMH ILFNLLWWWY LGGAVEKRLG SGKLIVITLI
     SALLSGYVQQ KFSGPWFGGL SGVVYALMGY VWLRGERDPQ SGIYLQRGLI IFALIWIVAG
     WFDLFGMSMA NGAHIAGLAV GLAMAFVDSL NARKRK
 
 
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