ID   GSPJ_KLEPN              Reviewed;         198 AA.
AC   P15749;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   25-MAY-2022, entry version 79.
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=Pullulanase secretion protein PulJ;
DE   Flags: Precursor;
GN   Name=pulJ;
OS   Klebsiella pneumoniae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=573;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=UNF 5023;
RX   PubMed=2129543; DOI=10.1007/bf00633815;
RA   Reyss I., Pugsley A.P.;
RT   "Five additional genes in the pulC-O operon of the Gram-negative bacterium
RT   Klebsiella oxytoca UNF5023 which are required for pullulanase secretion.";
RL   Mol. Gen. Genet. 222:176-184(1990).
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 PulG. {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; M32613; AAA25132.1; -; Genomic_DNA.
DR   AlphaFoldDB; P15749; -.
DR   SMR; P15749; -.
DR   TCDB; 3.A.15.1.1; the outer membrane protein secreting main terminal branch (mtb) family.
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_0000024254"
FT   CHAIN           8..198
FT                   /note="Type II secretion system protein J"
FT                   /id="PRO_0000024255"
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   198 AA;  22206 MW;  956977D5EF4E410D CRC64;
     MIRRSSGFTL VEMLLALAIL AALSVAAVTV LQNVMRADTL TRDKSGRMQA LQQTFSQMAA
     DFSQIIPRRS RDSASLFFAG RFQLGSDDGA IAFSRNGWPN PLGLLPRSEI QNVSYRLRGS
     QLERLNYDQQ DPLPGSQPTV TIVLRDVRAF GLRFYASGRW QDEWQQAQTL PQGLEVTLTL
     EPYGEIRRLF LLTPGDSR