(data stored in ACNUC1104 zone)

SWISSPROT: D3UYB4_XENBS

ID   D3UYB4_XENBS            Unreviewed;       277 AA.
AC   D3UYB4;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAY-2019, entry version 60.
DE   RecName: Full=Rhomboid protease GlpG {ECO:0000256|HAMAP-Rule:MF_01594};
DE            EC=3.4.21.105 {ECO:0000256|HAMAP-Rule:MF_01594};
DE   AltName: Full=Intramembrane serine protease {ECO:0000256|HAMAP-Rule:MF_01594};
GN   Name=glpG {ECO:0000256|HAMAP-Rule:MF_01594,
GN   ECO:0000313|EMBL:CBJ79292.1};
GN   OrderedLocusNames=XBJ1_0141 {ECO:0000313|EMBL:CBJ79292.1};
OS   Xenorhabdus bovienii (strain SS-2004).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406818 {ECO:0000313|EMBL:CBJ79292.1, ECO:0000313|Proteomes:UP000002045};
RN   [1] {ECO:0000313|Proteomes:UP000002045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SS-2004 {ECO:0000313|Proteomes:UP000002045};
RA   Goodrich-Blair H., Barbazuk B., Bode H.B., Darby C., Du Z., Forst S.,
RA   Gaudriault S., Goldman B.S., Goodner B., Henkhaus J., Latreille P.,
RA   Medigue C., Miller N., Norton S., Ogier J.C., Rouy Z., Slater S.,
RA   Suen G.;
RT   "Complete genome sequence of Xenorhabdus nematophila (strain ATCC
RT   19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6).";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBJ79292.1, ECO:0000313|Proteomes:UP000002045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SS-2004 {ECO:0000313|EMBL:CBJ79292.1,
RC   ECO:0000313|Proteomes:UP000002045};
RX   PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA   Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA   Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C.,
RA   de Leon L., Drace K., Du Z., Givaudan A., Herbert Tran E.E.,
RA   Jewell K.A., Knack J.J., Krasomil-Osterfeld K.C., Kukor R., Lanois A.,
RA   Latreille P., Leimgruber N.K., Lipke C.M., Liu R., Lu X.,
RA   Martens E.C., Marri P.R., Medigue C., Menard M.L., Miller N.M.,
RA   Morales-Soto N., Norton S., Ogier J.C., Orchard S.S., Park D.,
RA   Park Y., Qurollo B.A., Sugar D.R., Richards G.R., Rouy Z.,
RA   Slominski B., Slominski K., Snyder H., Tjaden B.C., van der Hoeven R.,
RA   Welch R.D., Wheeler C., Xiang B., Barbazuk B., Gaudriault S.,
RA   Goodner B., Slater S.C., Forst S., Goldman B.S., Goodrich-Blair H.;
RT   "The entomopathogenic bacterial endosymbionts xenorhabdus and
RT   photorhabdus: convergent lifestyles from divergent genomes.";
RL   PLoS ONE 6:e27909-e27909(2011).
CC   -!- FUNCTION: Rhomboid-type serine protease that catalyzes
CC       intramembrane proteolysis. {ECO:0000256|HAMAP-Rule:MF_01594}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Cleaves type-1 transmembrane domains using a catalytic
CC         dyad composed of serine and histidine that are contributed by
CC         different transmembrane domains.; EC=3.4.21.105;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01594};
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_01594, ECO:0000256|SAAS:SAAS00671960}; Multi-pass membrane
CC       protein {ECO:0000256|HAMAP-Rule:MF_01594,
CC       ECO:0000256|SAAS:SAAS00671960}.
CC   -!- SIMILARITY: Belongs to the peptidase S54 family.
CC       {ECO:0000256|HAMAP-Rule:MF_01594, ECO:0000256|SAAS:SAAS00671957}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01594}.
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DR   EMBL; FN667741; CBJ79292.1; -; Genomic_DNA.
DR   RefSeq; WP_012986759.1; NC_013892.1.
DR   STRING; 406818.XBJ1_0141; -.
DR   MEROPS; S54.016; -.
DR   EnsemblBacteria; CBJ79292; CBJ79292; XBJ1_0141.
DR   GeneID; 8829765; -.
DR   KEGG; xbo:XBJ1_0141; -.
DR   PATRIC; fig|406818.4.peg.128; -.
DR   eggNOG; ENOG4105EBW; Bacteria.
DR   eggNOG; COG0705; LUCA.
DR   HOGENOM; HOG000269640; -.
DR   KO; K02441; -.
DR   OMA; GLLGHCW; -.
DR   BioCyc; XBOV406818:XBJ1_RS00625-MONOMER; -.
DR   Proteomes; UP000002045; 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   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   TIGRFAMs; TIGR04239; rhombo_GlpG; 1.
PE   3: Inferred from homology;
DR   PRODOM; D3UYB4.
DR   SWISS-2DPAGE; D3UYB4.
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_01594,
KW   ECO:0000256|SAAS:SAAS00671958};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01594,
KW   ECO:0000256|SAAS:SAAS00671969};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002045};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01594};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01594,
KW   ECO:0000256|SAAS:SAAS00671965};
KW   Protease {ECO:0000256|HAMAP-Rule:MF_01594};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002045};
KW   Serine protease {ECO:0000256|HAMAP-Rule:MF_01594};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_01594,
KW   ECO:0000256|SAAS:SAAS00671963};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01594,
KW   ECO:0000256|SAAS:SAAS00671964}.
FT   TRANSMEM     99    117       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01594}.
FT   TRANSMEM    137    163       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01594}.
FT   TRANSMEM    198    215       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01594}.
FT   TRANSMEM    227    244       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01594}.
FT   TRANSMEM    250    269       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01594}.
FT   DOMAIN        1     85       Rhomboid_N. {ECO:0000259|Pfam:PF12122}.
FT   DOMAIN      133    270       Rhomboid. {ECO:0000259|Pfam:PF01694}.
FT   ACT_SITE    203    203       Nucleophile. {ECO:0000256|HAMAP-Rule:
FT                                MF_01594}.
FT   ACT_SITE    256    256       {ECO:0000256|HAMAP-Rule:MF_01594}.
SQ   SEQUENCE   277 AA;  31480 MW;  867BD50BC2499D49 CRC64;
     MIHVTSISNP RLAQAFIDYM VTQGIHLTMR PTHEPALVEL WLEDENQLSF VEQELNQFSR
     DPFNERYQTA SWQAGKSGYS FKYHNSLNLS TLKSQSGPLT ISVTALCILV YLWMQVAGDS
     DVMRWLAWPN GEQYLELWRW VSPALLHFSL THLLFNLALW WYLGSQVERH MGAGKLFEIT
     IVSAVFTDWA QSLFSGSHFG GLSGVVYALI SYVWLTGEMS PKRGISVPRG LIAISVIWLL
     VGYFDMFSLN IANAAHFSGL IIGLLMGLWD NLRKQKN
//

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