GSPJ_DICCH
ID GSPJ_DICCH Reviewed; 206 AA.
AC P24689;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 25-MAY-2022, entry version 78.
DE RecName: Full=Type II secretion system protein J;
DE Short=T2SS protein J;
DE AltName: Full=General secretion pathway protein J;
DE AltName: Full=Pectic enzymes secretion protein OutJ;
DE Flags: Precursor;
GN Name=outJ;
OS Dickeya chrysanthemi (Pectobacterium chrysanthemi) (Erwinia chrysanthemi).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Dickeya.
OX NCBI_TaxID=556;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=EC16;
RX PubMed=1992458; DOI=10.1073/pnas.88.3.1079;
RA He S.Y., Lindeberg M., Chatterjee A.K., Collmer A.;
RT "Cloned Erwinia chrysanthemi out genes enable Escherichia coli to
RT selectively secrete a diverse family of heterologous proteins to its
RT milieu.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:1079-1083(1991).
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 OutG. {ECO:0000250|UniProtKB:Q00517}.
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; M37886; AAA24828.1; -; Genomic_DNA.
DR EMBL; L02214; AAA24837.1; -; Genomic_DNA.
DR AlphaFoldDB; P24689; -.
DR SMR; P24689; -.
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 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Membrane; Methylation;
KW Protein transport; Transmembrane; Transmembrane helix; Transport.
FT PROPEP 1..7
FT /note="Leader sequence"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01070"
FT /id="PRO_0000024252"
FT CHAIN 8..206
FT /note="Type II secretion system protein J"
FT /id="PRO_0000024253"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 8
FT /note="N-methylphenylalanine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01070"
SQ SEQUENCE 206 AA; 23500 MW; 9C37A0B40B1BDBBC CRC64;
MKQPERGFTL LEVMLALAIF AALSLAASQV MNGVMRNDEA SARKEARLAE LQRGFSLMER
DFSQIVPRRS QGYELGFYAE RYQLSSADWA VSFIRNGWLN PLGIMPRSEL QRVGYRLRGD
TLERLFYDSS EPLSTQEPAV RPVLTGVTGF VLRFFGKDGW QERWDDPANL PQGIAIVVTL
RDYGEITRIF LITPRYGAAT QRRSER
