ID   GSPJ_PECCC              Reviewed;         216 AA.
AC   P31589;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   25-MAY-2022, entry version 81.
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   Pectobacterium carotovorum subsp. carotovorum (Erwinia carotovora subsp.
OS   carotovora).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=555;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=SCRI 193;
RX   PubMed=8326859; DOI=10.1111/j.1365-2958.1993.tb01589.x;
RA   Reeves P.J., Whitcombe D., Wharam S., Gibson M., Allison G., Bunce N.,
RA   Barallon R., Douglas P., Mulholland V., Stevens S., Walker S.,
RA   Salmond G.P.C.;
RT   "Molecular cloning and characterization of 13 out genes from Erwinia
RT   carotovora subspecies carotovora: genes encoding members of a general
RT   secretion pathway (GSP) widespread in Gram-negative bacteria.";
RL   Mol. Microbiol. 8:443-456(1993).
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 methionine 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; X70049; CAA49651.1; -; Genomic_DNA.
DR   PIR; S32864; S32864.
DR   RefSeq; WP_072036808.1; NZ_JUJR01000002.1.
DR   AlphaFoldDB; P31589; -.
DR   SMR; P31589; -.
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..25
FT                   /note="Leader sequence"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01070"
FT                   /id="PRO_0000024250"
FT   CHAIN           26..216
FT                   /note="Type II secretion system protein J"
FT                   /id="PRO_0000024251"
FT   TRANSMEM        26..46
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         26
FT                   /note="N-methylphenylalanine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01070"
SQ   SEQUENCE   216 AA;  24850 MW;  96223BCA29471070 CRC64;
     MSSKTGMCSQ TRRRREPARQ ERQQGFTLLE MILAIAIFAA LSLSAFQVLN GVMRNDEISQ
     RKAERLAEIQ RAFSQMDNDF SQMIARGSRG STSMFYAGRD QLKSDDWGVS FMRNGWQNPF
     GILPRSELQP VAYRLREHTL ERLTHVTPDP IEGLDPGVKP LLTQVDGFRL RFFSNKTWRD
     RWDNSTQLPQ GIEVVLTLRD YGEMSRMFLI TTGPVK