(data stored in SCRATCH zone)

SWISSPROT: 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   11-DEC-2019, entry version 141.
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}.
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   SMR; P54493; -.
DR   STRING; 224308.BSU24870; -.
DR   MEROPS; S54.014; -.
DR   PaxDb; P54493; -.
DR   PRIDE; P54493; -.
DR   EnsemblBacteria; CAB14418; CAB14418; BSU24870.
DR   GeneID; 938211; -.
DR   KEGG; bsu:BSU24870; -.
DR   PATRIC; fig|224308.179.peg.2706; -.
DR   eggNOG; ENOG4107ZXI; Bacteria.
DR   eggNOG; COG0705; LUCA.
DR   HOGENOM; HOG000262065; -.
DR   InParanoid; P54493; -.
DR   KO; K19225; -.
DR   OMA; YPPVDDW; -.
DR   PhylomeDB; P54493; -.
DR   BioCyc; BSUB:BSU24870-MONOMER; -.
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   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; IPR013026; TPR-contain_dom.
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; SSF48452; SSF48452; 1.
DR   PROSITE; PS50005; TPR; 2.
DR   PROSITE; PS50293; TPR_REGION; 1.
PE   1: Evidence at protein level;
DR   PRODOM; P54493.
DR   SWISS-2DPAGE; P54493.
KW   Cell membrane; Hydrolase; Membrane; Protease; Reference proteome; Repeat;
KW   Serine protease; TPR repeat; Transmembrane; 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"
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
//

If you have problems or comments...

PBIL Back to PBIL home page