GLPG_HAEIN
ID GLPG_HAEIN Reviewed; 192 AA.
AC P44783;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Rhomboid protease GlpG;
DE EC=3.4.21.105;
DE AltName: Full=Intramembrane serine protease;
GN Name=glpG; OrderedLocusNames=HI_0618;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), ACTIVE SITE, REACTION MECHANISM, AND
RP SUBCELLULAR LOCATION.
RX PubMed=17210913; DOI=10.1073/pnas.0609981104;
RA Lemieux M.J., Fischer S.J., Cherney M.M., Bateman K.S., James M.N.G.;
RT "The crystal structure of the rhomboid peptidase from Haemophilus
RT influenzae provides insight into intramembrane proteolysis.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:750-754(2007).
CC -!- FUNCTION: Rhomboid-type serine protease that catalyzes intramembrane
CC proteolysis. {ECO:0000250}.
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;
CC -!- INTERACTION:
CC P44783; P44783: glpG; NbExp=2; IntAct=EBI-10098079, EBI-10098079;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:17210913}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:17210913}.
CC -!- SIMILARITY: Belongs to the peptidase S54 family. {ECO:0000305}.
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DR EMBL; L42023; AAC22277.1; -; Genomic_DNA.
DR PIR; I64081; I64081.
DR RefSeq; NP_438776.1; NC_000907.1.
DR RefSeq; WP_005648561.1; NC_000907.1.
DR PDB; 2NR9; X-ray; 2.20 A; A=1-192.
DR PDB; 3ODJ; X-ray; 2.84 A; A=1-192.
DR PDBsum; 2NR9; -.
DR PDBsum; 3ODJ; -.
DR AlphaFoldDB; P44783; -.
DR PCDDB; P44783; -.
DR SMR; P44783; -.
DR IntAct; P44783; 1.
DR MINT; P44783; -.
DR STRING; 71421.HI_0618; -.
DR DrugBank; DB08367; (R)-2-(FORMYLOXY)-3-(PHOSPHONOOXY)PROPYL PENTANOATE.
DR MEROPS; S54.024; -.
DR TCDB; 9.B.104.1.7; the rhomboid protease (rhomboid) family.
DR EnsemblBacteria; AAC22277; AAC22277; HI_0618.
DR KEGG; hin:HI_0618; -.
DR PATRIC; fig|71421.8.peg.642; -.
DR eggNOG; COG0705; Bacteria.
DR HOGENOM; CLU_121865_0_0_6; -.
DR OMA; PEGFFTM; -.
DR PhylomeDB; P44783; -.
DR BioCyc; HINF71421:G1GJ1-639-MON; -.
DR BRENDA; 3.4.21.105; 2529.
DR EvolutionaryTrace; P44783; -.
DR Proteomes; UP000000579; 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:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1540.10; -; 1.
DR InterPro; IPR022764; Peptidase_S54_rhomboid_dom.
DR InterPro; IPR035952; Rhomboid-like_sf.
DR Pfam; PF01694; Rhomboid; 1.
DR SUPFAM; SSF144091; SSF144091; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Hydrolase; Membrane;
KW Protease; Reference proteome; Serine protease; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..192
FT /note="Rhomboid protease GlpG"
FT /id="PRO_0000087516"
FT TOPO_DOM 1..10
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 11..31
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 32..57
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 58..78
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 79..82
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 83..103
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 104..107
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 108..128
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 129..141
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 142..162
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 163
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 164..184
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 185..192
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 116
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:17210913"
FT ACT_SITE 169
FT /evidence="ECO:0000269|PubMed:17210913"
FT HELIX 10..27
FT /evidence="ECO:0007829|PDB:2NR9"
FT HELIX 31..38
FT /evidence="ECO:0007829|PDB:2NR9"
FT HELIX 44..48
FT /evidence="ECO:0007829|PDB:2NR9"
FT HELIX 52..55
FT /evidence="ECO:0007829|PDB:2NR9"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:2NR9"
FT HELIX 63..84
FT /evidence="ECO:0007829|PDB:2NR9"
FT HELIX 86..108
FT /evidence="ECO:0007829|PDB:2NR9"
FT HELIX 116..131
FT /evidence="ECO:0007829|PDB:2NR9"
FT TURN 144..148
FT /evidence="ECO:0007829|PDB:2NR9"
FT TURN 150..152
FT /evidence="ECO:0007829|PDB:2NR9"
FT HELIX 153..156
FT /evidence="ECO:0007829|PDB:2NR9"
FT HELIX 166..191
FT /evidence="ECO:0007829|PDB:2NR9"
SQ SEQUENCE 192 AA; 21657 MW; B76A7A658037217E CRC64;
MKNFLAQQGK ITLILTALCV LIYLAQQLGF EDDIMYLMHY PAYEEQDSEV WRYISHTLVH
LSNLHILFNL SWFFIFGGMI ERTFGSVKLL MLYVVASAIT GYVQNYVSGP AFFGLSGVVY
AVLGYVFIRD KLNHHLFDLP EGFFTMLLVG IALGFISPLF GVEMGNAAHI SGLIVGLIWG
FIDSKLRKNS LE
