ID   GLPG_SERP5              Reviewed;         278 AA.
AC   A8GKU2;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   03-AUG-2022, entry version 84.
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=Spro_4639;
OS   Serratia proteamaculans (strain 568).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=399741;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=568;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Taghavi S., Newman L.,
RA   Vangronsveld J., van der Lelie D., Richardson P.;
RT   "Complete sequence of chromosome of Serratia proteamaculans 568.";
RL   Submitted (SEP-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; CP000826; ABV43732.1; -; Genomic_DNA.
DR   RefSeq; WP_012147314.1; NC_009832.1.
DR   AlphaFoldDB; A8GKU2; -.
DR   SMR; A8GKU2; -.
DR   STRING; 399741.Spro_4639; -.
DR   MEROPS; S54.016; -.
DR   EnsemblBacteria; ABV43732; ABV43732; Spro_4639.
DR   KEGG; spe:Spro_4639; -.
DR   eggNOG; COG0705; Bacteria.
DR   HOGENOM; CLU_058989_0_0_6; -.
DR   OMA; LLGHCWI; -.
DR   OrthoDB; 2053476at2; -.
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_0000321692"
FT   TRANSMEM        95..115
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        170..190
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        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;  31389 MW;  4676F2524C1F1C40 CRC64;
     MVRVIAVSNP RLAQAFVDYM TTQGIELRVH NTGEAAEIWL ADDSHLEQVQ HELQQFLIDP
     LNSRYRAASW QAGNTDADLH YQGFSYLQTL RSKAGPLTLG VMALCIVVYI LMQILGDDTL
     MYWLSWPQDS SQYLQLWRWV SHAFLHFSLL HITFNLLWWW YLGGPLEKRL GSGKLFVLAV
     VSAFFSGWAQ SLFSGALFGG LSGVVYALMG YCWLSGERAP ERGLMLPRGL MVFSVLWLVA
     GYFDILGMSI ANAAHVAGLV LGLLMAFWDT RHRAHNEQ