ID   GSPJ_KLEOK              Reviewed;         199 AA.
AC   A0A0H3H7Y9;
DT   22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT   16-SEP-2015, sequence version 1.
DT   25-MAY-2022, entry version 27.
DE   RecName: Full=Type II secretion system protein J;
DE            Short=T2SS protein J;
DE   Flags: Precursor;
GN   Name=pulJ; OrderedLocusNames=KOX_13595;
OS   Klebsiella oxytoca (strain ATCC 8724 / DSM 4798 / JCM 20051 / NBRC 3318 /
OS   NRRL B-199 / KCTC 1686 / BUCSAV 143 / CCM 1901).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=1006551;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8724 / DSM 4798 / JCM 20051 / NBRC 3318 / NRRL B-199 / KCTC
RC   1686 / BUCSAV 143 / CCM 1901;
RX   PubMed=22493189; DOI=10.1128/jb.00026-12;
RA   Shin S.H., Kim S., Kim J.Y., Lee S., Um Y., Oh M.K., Kim Y.R., Lee J.,
RA   Yang K.S.;
RT   "Complete genome sequence of Klebsiella oxytoca KCTC 1686, used in
RT   production of 2,3-butanediol.";
RL   J. Bacteriol. 194:2371-2372(2012).
RN   [2]
RP   FUNCTION, INTERACTION WITH PULJ AND PULH, DISRUPTION PHENOTYPE, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=22157749; DOI=10.1038/emboj.2011.454;
RA   Cisneros D.A., Bond P.J., Pugsley A.P., Campos M., Francetic O.;
RT   "Minor pseudopilin self-assembly primes type II secretion pseudopilus
RT   elongation.";
RL   EMBO J. 31:1041-1053(2012).
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:0000269|PubMed:22157749}; 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   -!- DISRUPTION PHENOTYPE: Deletion mutant shows longer pili but their
CC       number is reduced. {ECO:0000269|PubMed:22157749}.
CC   -!- SIMILARITY: Belongs to the GSP J family. {ECO:0000305}.
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DR   EMBL; CP003218; AEX04443.1; -; Genomic_DNA.
DR   RefSeq; WP_014228301.1; NC_016612.1.
DR   AlphaFoldDB; A0A0H3H7Y9; -.
DR   SMR; A0A0H3H7Y9; -.
DR   EnsemblBacteria; AEX04443; AEX04443; KOX_13595.
DR   KEGG; kox:KOX_13595; -.
DR   HOGENOM; CLU_093850_0_0_6; -.
DR   OMA; WYYPYPE; -.
DR   Proteomes; UP000007843; 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: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   Cell inner membrane; Cell membrane; Membrane; Methylation; Transmembrane;
KW   Transmembrane helix.
FT   PROPEP          1..8
FT                   /note="Leader sequence"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01070"
FT                   /id="PRO_0000449551"
FT   CHAIN           9..199
FT                   /note="Type II secretion system protein J"
FT                   /id="PRO_0000449552"
FT   TRANSMEM        9..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         9
FT                   /note="N-methylphenylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q00517"
SQ   SEQUENCE   199 AA;  23058 MW;  0CCC20133BDA6B68 CRC64;
     MSRCRERGFT LLEMLLALAI FAALSLSAFQ ILQGVMRNDE MAQRQVQRLT ELQRAFVYLE
     GDFGQIIPRP PRGDERLFYA ARYQRQSADW SISFMRNGWQ NPMGILPRSE LQRVGYRLRH
     QQLERLSYVH TDPQAGEEPI VKVLLKDVSA FRLRFFANGM WRDSWNDTTR LPEGIEVSLV
     VADVGEVSRL FFVTTGEQA