GSPJ_ECOLX
ID GSPJ_ECOLX Reviewed; 199 AA.
AC A0A4C3GMC1; Q8VPC2;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 31-JUL-2019, sequence version 1.
DT 25-MAY-2022, entry version 12.
DE RecName: Full=Type II secretion system protein J;
DE Short=T2SS protein J;
DE AltName: Full=Cholera toxin secretion protein EpsJ;
DE AltName: Full=General secretion pathway protein J;
DE Flags: Precursor;
GN Name=gspJ; ORFNames=BvCms2454_02423;
OS Escherichia coli.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=H10407;
RX PubMed=12011463; DOI=10.1073/pnas.092152899;
RA Tauschek M., Gorrell R.J., Strugnell R.A., Robins-Browne R.M.;
RT "Identification of a protein secretory pathway for the secretion of heat-
RT labile enterotoxin by an enterotoxigenic strain of Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:7066-7071(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BE2454;
RA Arimizu Y., Ogura Y.;
RT "Large scale genomics of bovine and human commensal E. coli to reveal the
RT emerging process of EHEC.";
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 26-187, AND INTERACTION WITH GSPK
RP AND GSPI.
RX PubMed=18438417; DOI=10.1038/nsmb.1426;
RA Korotkov K.V., Hol W.G.;
RT "Structure of the GspK-GspI-GspJ complex from the enterotoxigenic
RT Escherichia coli type 2 secretion system.";
RL Nat. Struct. Mol. Biol. 15:462-468(2008).
CC -!- FUNCTION: Component of the type II secretion system required for the
CC energy-dependent secretion of extracellular factors such as proteases
CC and toxins from the periplasm. Part of the pseudopilus tip complex that
CC is critical for the recognition and binding of secretion substrates.
CC {ECO:0000250|UniProtKB:Q00517}.
CC -!- SUBUNIT: Type II secretion is composed of four main components: the
CC outer membrane complex, the inner membrane complex, the cytoplasmic
CC secretion ATPase and the periplasm-spanning pseudopilus. Interacts with
CC core component GspG (By similarity). Interacts with pseudopilins GspI
CC and GspK (PubMed:18438417). {ECO:0000250|UniProtKB:Q00517,
CC ECO:0000269|PubMed:18438417}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:Q00517}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- PTM: Cleaved by prepilin peptidase. {ECO:0000250|UniProtKB:Q00517}.
CC -!- PTM: Methylated by prepilin peptidase at the amino group of the N-
CC terminal phenylalanine once the leader sequence is cleaved by prepilin
CC peptidase. {ECO:0000250|UniProtKB:Q00517}.
CC -!- SIMILARITY: Belongs to the GSP J family. {ECO:0000305}.
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DR EMBL; AY056599; AAL10699.1; -; Genomic_DNA.
DR EMBL; BFGA01000032; GCP05137.1; -; Genomic_DNA.
DR PDB; 3CI0; X-ray; 2.20 A; J=26-187.
DR PDBsum; 3CI0; -.
DR AlphaFoldDB; A0A4C3GMC1; -.
DR SMR; A0A4C3GMC1; -.
DR PATRIC; fig|562.10824.peg.3491; -.
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:0015627; C:type II protein secretion system complex; IEA:InterPro.
DR GO; GO:0015628; P:protein secretion by the type II secretion system; IEA:InterPro.
DR InterPro; IPR012902; N_methyl_site.
DR InterPro; IPR045584; Pilin-like.
DR InterPro; IPR010055; T2SS_protein-GspJ.
DR Pfam; PF07963; N_methyl; 1.
DR Pfam; PF11612; T2SSJ; 1.
DR SUPFAM; SSF54523; SSF54523; 1.
DR TIGRFAMs; TIGR01711; gspJ; 1.
DR TIGRFAMs; TIGR02532; IV_pilin_GFxxxE; 1.
DR PROSITE; PS00409; PROKAR_NTER_METHYL; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Membrane; Methylation;
KW Transmembrane; Transmembrane helix.
FT PROPEP 1..7
FT /note="Leader sequence"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01070"
FT /id="PRO_0000449549"
FT CHAIN 8..199
FT /note="Type II secretion system protein J"
FT /id="PRO_0000449550"
FT TRANSMEM 8..27
FT /note="Helical"
FT /evidence="ECO:0000305"
FT MOD_RES 8
FT /note="N-methylphenylalanine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01070"
FT HELIX 47..62
FT /evidence="ECO:0007829|PDB:3CI0"
FT STRAND 80..85
FT /evidence="ECO:0007829|PDB:3CI0"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:3CI0"
FT STRAND 91..99
FT /evidence="ECO:0007829|PDB:3CI0"
FT STRAND 115..122
FT /evidence="ECO:0007829|PDB:3CI0"
FT STRAND 125..136
FT /evidence="ECO:0007829|PDB:3CI0"
FT STRAND 143..149
FT /evidence="ECO:0007829|PDB:3CI0"
FT STRAND 153..158
FT /evidence="ECO:0007829|PDB:3CI0"
FT STRAND 163..165
FT /evidence="ECO:0007829|PDB:3CI0"
FT STRAND 175..183
FT /evidence="ECO:0007829|PDB:3CI0"
FT TURN 184..186
FT /evidence="ECO:0007829|PDB:3CI0"
FT STRAND 187..196
FT /evidence="ECO:0007829|PDB:3CI0"
SQ SEQUENCE 199 AA; 22222 MW; 8195E3992612D1E5 CRC64;
MKRTRAGFTL LEMLVAIAIF ASLALMAQQV TNGVTRVNSA VADHDQKLNL MQQTMSFLTH
DLTQMMPRPV RGDQGQREPA LLAGAGVLAS ESEGMRFVRG GVVNPLMRLP RSNLLTVGYR
IHDGYLERLA WPLTDAAGSV KPTMQKLIPA DSLRLQFYDG TRWQESWSSV QAIPVAVRMT
LHSPQWGEIE RIWLLRGPQ
