GLUP_BACSU
ID GLUP_BACSU Reviewed; 507 AA.
AC P54493;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Rhomboid protease GluP;
DE EC=3.4.21.105;
DE AltName: Full=Intramembrane serine protease;
GN Name=gluP; Synonyms=yqgP; OrderedLocusNames=BSU24870;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / JH642;
RX PubMed=8969508; DOI=10.1099/13500872-142-11-3103;
RA Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M.,
RA Kobayashi Y.;
RT "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the
RT Bacillus subtilis genome containing the skin element and many sporulation
RT genes.";
RL Microbiology 142:3103-3111(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP SEQUENCE REVISION TO 192; 370; 379 AND 499.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [4]
RP FUNCTION.
RC STRAIN=168;
RX PubMed=15050034; DOI=10.1186/1471-2180-4-13;
RA Mesak L.R., Mesak F.M., Dahl M.K.;
RT "Expression of a novel gene, gluP, is essential for normal Bacillus
RT subtilis cell division and contributes to glucose export.";
RL BMC Microbiol. 4:13-13(2004).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, REACTION MECHANISM, AND MUTAGENESIS OF
RP ARG-224; HIS-237; ASN-241; GLY-286; SER-288 AND HIS-339.
RX PubMed=15616571; DOI=10.1038/sj.emboj.7600537;
RA Lemberg M.K., Menendez J., Misik A., Garcia M., Koth C.M., Freeman M.;
RT "Mechanism of intramembrane proteolysis investigated with purified rhomboid
RT proteases.";
RL EMBO J. 24:464-472(2005).
RN [6]
RP FUNCTION, ACTIVITY REGULATION, AND TEMPERATURE DEPENDENCE.
RX PubMed=15684070; DOI=10.1073/pnas.0408306102;
RA Urban S., Wolfe M.S.;
RT "Reconstitution of intramembrane proteolysis in vitro reveals that pure
RT rhomboid is sufficient for catalysis and specificity.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:1883-1888(2005).
RN [7]
RP FUNCTION.
RX PubMed=16621838; DOI=10.1128/jb.188.9.3415-3419.2006;
RA Clemmer K.M., Sturgill G.M., Veenstra A., Rather P.N.;
RT "Functional characterization of Escherichia coli GlpG and additional
RT rhomboid proteins using an aarA mutant of Providencia stuartii.";
RL J. Bacteriol. 188:3415-3419(2006).
CC -!- FUNCTION: Rhomboid-type serine protease that catalyzes intramembrane
CC proteolysis. Important for normal cell division and sporulation. May
CC act as a glucose exporter. {ECO:0000269|PubMed:15050034,
CC ECO:0000269|PubMed:15616571, ECO:0000269|PubMed:15684070,
CC ECO:0000269|PubMed:16621838}.
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 -!- ACTIVITY REGULATION: Inhibited by dichloroisocoumarin (DCI) and N-p-
CC tosyl-L-phenylalanine chloromethyl ketone (TPCK), but not by other
CC serine protease inhibitors such as sulfonyl fluoride PMSF and 4-(2-
CC aminoethyl)benzenesulfonyl fluoride (AEBSF).
CC {ECO:0000269|PubMed:15684070}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Is more active at more active at 25 degrees Celsius than at 37
CC degrees Celsius. {ECO:0000269|PubMed:15684070};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15616571};
CC Multi-pass membrane protein {ECO:0000269|PubMed:15616571}.
CC -!- SIMILARITY: Belongs to the peptidase S54 family. {ECO:0000305}.
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DR EMBL; D84432; BAA12519.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14418.2; -; Genomic_DNA.
DR PIR; B69957; B69957.
DR RefSeq; NP_390367.2; NC_000964.3.
DR RefSeq; WP_003230128.1; NZ_JNCM01000036.1.
DR PDB; 6R0J; NMR; -; A=1-176.
DR PDBsum; 6R0J; -.
DR AlphaFoldDB; P54493; -.
DR BMRB; P54493; -.
DR SMR; P54493; -.
DR STRING; 224308.BSU24870; -.
DR BindingDB; P54493; -.
DR ChEMBL; CHEMBL4295579; -.
DR MEROPS; S54.014; -.
DR PaxDb; P54493; -.
DR PRIDE; P54493; -.
DR EnsemblBacteria; CAB14418; CAB14418; BSU_24870.
DR GeneID; 938211; -.
DR KEGG; bsu:BSU24870; -.
DR PATRIC; fig|224308.179.peg.2706; -.
DR eggNOG; COG0457; Bacteria.
DR eggNOG; COG0705; Bacteria.
DR InParanoid; P54493; -.
DR OMA; YPPVDDW; -.
DR PhylomeDB; P54493; -.
DR BioCyc; BSUB:BSU24870-MON; -.
DR BRENDA; 3.4.21.105; 658.
DR Proteomes; UP000001570; 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; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1540.10; -; 1.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR022764; Peptidase_S54_rhomboid_dom.
DR InterPro; IPR035952; Rhomboid-like_sf.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF01694; Rhomboid; 1.
DR SMART; SM00028; TPR; 2.
DR SUPFAM; SSF144091; SSF144091; 1.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS50005; TPR; 2.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Hydrolase; Membrane; Protease;
KW Reference proteome; Repeat; Serine protease; TPR repeat; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..507
FT /note="Rhomboid protease GluP"
FT /id="PRO_0000049812"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 229..249
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 261..281
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 283..303
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 312..332
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 340..360
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 365..385
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 424..457
FT /note="TPR 1"
FT REPEAT 458..491
FT /note="TPR 2"
FT ACT_SITE 288
FT /note="Nucleophile"
FT /evidence="ECO:0000305"
FT ACT_SITE 339
FT /note="Charge relay system"
FT /evidence="ECO:0000305"
FT MUTAGEN 224
FT /note="R->A: Reduced protease activity."
FT /evidence="ECO:0000269|PubMed:15616571"
FT MUTAGEN 237
FT /note="H->A: Reduced protease activity."
FT /evidence="ECO:0000269|PubMed:15616571"
FT MUTAGEN 241
FT /note="N->A: No effect on protease activity in vitro."
FT /evidence="ECO:0000269|PubMed:15616571"
FT MUTAGEN 286
FT /note="G->A: Loss of protease activity."
FT /evidence="ECO:0000269|PubMed:15616571"
FT MUTAGEN 288
FT /note="S->A: Loss of protease activity."
FT /evidence="ECO:0000269|PubMed:15616571"
FT MUTAGEN 339
FT /note="H->A: Loss of protease activity."
FT /evidence="ECO:0000269|PubMed:15616571"
FT CONFLICT 192
FT /note="F -> S (in Ref. 1; BAA12519)"
FT /evidence="ECO:0000305"
FT CONFLICT 370
FT /note="L -> F (in Ref. 1; BAA12519)"
FT /evidence="ECO:0000305"
FT CONFLICT 379
FT /note="L -> S (in Ref. 1; BAA12519)"
FT /evidence="ECO:0000305"
FT CONFLICT 499
FT /note="R -> W (in Ref. 1; BAA12519)"
FT /evidence="ECO:0000305"
FT HELIX 3..16
FT /evidence="ECO:0007829|PDB:6R0J"
FT TURN 17..19
FT /evidence="ECO:0007829|PDB:6R0J"
FT STRAND 21..24
FT /evidence="ECO:0007829|PDB:6R0J"
FT STRAND 28..34
FT /evidence="ECO:0007829|PDB:6R0J"
FT STRAND 43..48
FT /evidence="ECO:0007829|PDB:6R0J"
FT HELIX 54..75
FT /evidence="ECO:0007829|PDB:6R0J"
FT STRAND 78..90
FT /evidence="ECO:0007829|PDB:6R0J"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:6R0J"
FT HELIX 96..100
FT /evidence="ECO:0007829|PDB:6R0J"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:6R0J"
FT STRAND 109..117
FT /evidence="ECO:0007829|PDB:6R0J"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:6R0J"
FT HELIX 121..128
FT /evidence="ECO:0007829|PDB:6R0J"
FT HELIX 134..137
FT /evidence="ECO:0007829|PDB:6R0J"
FT TURN 139..141
FT /evidence="ECO:0007829|PDB:6R0J"
FT HELIX 146..168
FT /evidence="ECO:0007829|PDB:6R0J"
SQ SEQUENCE 507 AA; 56462 MW; D019B4543C2D9670 CRC64;
MFLLEYTYWK IAAHLVNSGY GVIQAGESDE IWLEAPDKSS HDLVRLYKHD LDFRQEMVRD
IEEQAERVER VRHQLGRRRM KLLNVFFSTE APVDDWEEIA KKTFEKGTVS VEPAIVRGTM
LRDDLQAVFP SFRTEDCSEE HASFENAQMA RERFLSLVLK QEEQRKTEAA VFQNGKPTFT
YLFIALQILM FFLLEINGGS TNTETLVAFG AKENSLIAQG EWWRLLTPIV LHIGIAHLAF
NTLALWSVGT AVERMYGSGR FLLIYLAAGI TGSIASFVFS PYPSAGASGA IFGCLGALLY
VALSNRKMFL RTIGTNIIVI IIINLGFGFA VSNIDNSGHI GGLIGGFFAA AALGLPKAGA
FGKRLLSAVL LIALAVGFLY YGLHSPSHQE SALIQQASEL YQEGKYEEVT ELLNGEAAQK
DASADLLKIL AVSDIQIGEY DQAVSLLERA VKKEPKDHAS YYNLALLYAE KNELAQAEKA
IQTAVKLKPK EQRYKELQRQ IENNKES
