GSPJ_PSEAE
ID GSPJ_PSEAE Reviewed; 237 AA.
AC Q00517;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 122.
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=PilD-dependent protein PddD;
DE Flags: Precursor;
GN Name=xcpW; Synonyms=pddD; OrderedLocusNames=PA3098;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=1588814; DOI=10.1111/j.1365-2958.1992.tb01550.x;
RA Bally M., Filloux A., Akrim M., Ball G., Lazdunski A., Tommassen J.;
RT "Protein secretion in Pseudomonas aeruginosa: characterization of seven xcp
RT genes and processing of secretory apparatus components by prepilin
RT peptidase.";
RL Mol. Microbiol. 6:1121-1131(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1309616; DOI=10.1073/pnas.89.1.47;
RA Nunn D.N., Lory S.;
RT "Components of the protein-excretion apparatus of Pseudomonas aeruginosa
RT are processed by the type IV prepilin peptidase.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:47-51(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [4]
RP SUBCELLULAR LOCATION, CLEAVAGE, AND METHYLATION AT PHE-7.
RC STRAIN=PAK;
RX PubMed=8331069; DOI=10.1128/jb.175.14.4375-4382.1993;
RA Nunn D.N., Lory S.;
RT "Cleavage, methylation, and localization of the Pseudomonas aeruginosa
RT export proteins XcpT, -U, -V, and -W.";
RL J. Bacteriol. 175:4375-4382(1993).
RN [5]
RP FUNCTION, AND INTERACTION WITH XCPT.
RX PubMed=9282737; DOI=10.1046/j.1365-2958.1997.4561818.x;
RA Lu H.M., Motley S.T., Lory S.;
RT "Interactions of the components of the general secretion pathway: role of
RT Pseudomonas aeruginosa type IV pilin subunits in complex formation and
RT extracellular protein secretion.";
RL Mol. Microbiol. 25:247-259(1997).
RN [6]
RP FUNCTION.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=12700254; DOI=10.1128/jb.185.9.2749-2758.2003;
RA Durand E., Bernadac A., Ball G., Lazdunski A., Sturgis J.N., Filloux A.;
RT "Type II protein secretion in Pseudomonas aeruginosa: the pseudopilus is a
RT multifibrillar and adhesive structure.";
RL J. Bacteriol. 185:2749-2758(2003).
RN [7]
RP FUNCTION, AND INTERACTION WITH XCPU; XCPV AMD XCPX.
RX PubMed=19828448; DOI=10.1074/jbc.m109.042366;
RA Douzi B., Durand E., Bernard C., Alphonse S., Cambillau C., Filloux A.,
RA Tegoni M., Voulhoux R.;
RT "The XcpV/GspI pseudopilin has a central role in the assembly of a
RT quaternary complex within the T2SS pseudopilus.";
RL J. Biol. Chem. 284:34580-34589(2009).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 28-237.
RX PubMed=21245534; DOI=10.1107/s0907444910051954;
RA Franz L.P., Douzi B., Durand E., Dyer D.H., Voulhoux R., Forest K.T.;
RT "Structure of the minor pseudopilin XcpW from the Pseudomonas aeruginosa
RT type II secretion system.";
RL Acta Crystallogr. D 67:124-130(2011).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 28-237, FUNCTION, INTERACTION
RP WITH XCPU, AND DISRUPTION PHENOTYPE.
RX PubMed=30346996; DOI=10.1371/journal.ppat.1007343;
RA Zhang Y., Faucher F., Zhang W., Wang S., Neville N., Poole K., Zheng J.,
RA Jia Z.;
RT "Structure-guided disruption of the pseudopilus tip complex inhibits the
RT Type II secretion in Pseudomonas aeruginosa.";
RL PLoS Pathog. 14:E1007343-E1007343(2018).
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 (PubMed:9282737). Part of the pseudopilus
CC tip complex that is critical for the recognition and binding of
CC secretion substrates (PubMed:19828448, PubMed:30346996). Type II
CC pseudopilus confers increased bacterial adhesive capabilities
CC (PubMed:12700254). {ECO:0000269|PubMed:12700254,
CC ECO:0000269|PubMed:19828448, ECO:0000269|PubMed:30346996,
CC ECO:0000269|PubMed:9282737}.
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. Forms the tip
CC of the type II pseudopilus by interacting with XcpV, XcpU and XcpX
CC (PubMed:19828448, PubMed:30346996). Interacts with core component XcpT
CC (PubMed:9282737). {ECO:0000269|PubMed:19828448,
CC ECO:0000269|PubMed:30346996, ECO:0000269|PubMed:9282737}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:8331069};
CC Single-pass membrane protein {ECO:0000255}.
CC -!- PTM: Cleaved by prepilin peptidase. {ECO:0000269|PubMed:8331069}.
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:0000269|PubMed:8331069}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutant results in a non-functional T2SS
CC system. {ECO:0000269|PubMed:30346996}.
CC -!- SIMILARITY: Belongs to the GSP J family. {ECO:0000305}.
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DR EMBL; X62666; CAA44538.1; -; Genomic_DNA.
DR EMBL; M80792; AAA25949.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG06486.1; -; Genomic_DNA.
DR PIR; S25389; SKPSXW.
DR RefSeq; NP_251788.1; NC_002516.2.
DR RefSeq; WP_003110067.1; NZ_QZGE01000009.1.
DR PDB; 3NJE; X-ray; 1.85 A; A/B=28-237.
DR PDB; 5BW0; X-ray; 2.00 A; A/C/E/G=28-204.
DR PDB; 5VTM; X-ray; 2.04 A; W=44-237.
DR PDB; 6UTU; X-ray; 2.85 A; B/E/H=44-237.
DR PDBsum; 3NJE; -.
DR PDBsum; 5BW0; -.
DR PDBsum; 5VTM; -.
DR PDBsum; 6UTU; -.
DR AlphaFoldDB; Q00517; -.
DR SMR; Q00517; -.
DR STRING; 287.DR97_4835; -.
DR PaxDb; Q00517; -.
DR DNASU; 882776; -.
DR EnsemblBacteria; AAG06486; AAG06486; PA3098.
DR GeneID; 882776; -.
DR KEGG; pae:PA3098; -.
DR PATRIC; fig|208964.12.peg.3250; -.
DR PseudoCAP; PA3098; -.
DR HOGENOM; CLU_093850_1_0_6; -.
DR InParanoid; Q00517; -.
DR OMA; WYYPYPE; -.
DR PhylomeDB; Q00517; -.
DR BioCyc; PAER208964:G1FZ6-3154-MON; -.
DR EvolutionaryTrace; Q00517; -.
DR Proteomes; UP000002438; 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; IDA:PseudoCAP.
DR GO; GO:0015628; P:protein secretion by the type II secretion system; IDA:PseudoCAP.
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; 2.
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 Protein transport; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT PROPEP 1..6
FT /note="Leader sequence"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01070,
FT ECO:0000269|PubMed:8331069"
FT /id="PRO_0000024256"
FT CHAIN 7..237
FT /note="Type II secretion system protein J"
FT /id="PRO_0000024257"
FT TRANSMEM 7..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 203..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 7
FT /note="N-methylphenylalanine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01070"
FT CONFLICT 92
FT /note="F -> L (in Ref. 2; AAA25949)"
FT /evidence="ECO:0000305"
FT HELIX 42..62
FT /evidence="ECO:0007829|PDB:3NJE"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:3NJE"
FT STRAND 79..84
FT /evidence="ECO:0007829|PDB:3NJE"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:3NJE"
FT STRAND 89..94
FT /evidence="ECO:0007829|PDB:3NJE"
FT STRAND 109..116
FT /evidence="ECO:0007829|PDB:3NJE"
FT STRAND 119..126
FT /evidence="ECO:0007829|PDB:3NJE"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:5VTM"
FT HELIX 131..133
FT /evidence="ECO:0007829|PDB:3NJE"
FT STRAND 137..143
FT /evidence="ECO:0007829|PDB:3NJE"
FT STRAND 145..153
FT /evidence="ECO:0007829|PDB:3NJE"
FT STRAND 159..164
FT /evidence="ECO:0007829|PDB:3NJE"
FT HELIX 170..175
FT /evidence="ECO:0007829|PDB:3NJE"
FT STRAND 179..187
FT /evidence="ECO:0007829|PDB:3NJE"
FT TURN 188..190
FT /evidence="ECO:0007829|PDB:3NJE"
FT STRAND 191..198
FT /evidence="ECO:0007829|PDB:3NJE"
SQ SEQUENCE 237 AA; 27131 MW; D5AF6600138CE422 CRC64;
MRLQRGFTLL ELLIAIAIFA LLALATYRMF DSVMQTDQAT RVQEQRMREL VRAMGALERD
LTQAVERPVR DELGDNRGAF LSEGENDQIV EFTRGGWRNP LGQARSRLQR VRWSLSGETL
ERRYWLVLDR AQDSKPRVQQ VLDGVTALSW RFLDKEHNWQ GHWPTDEGSE EERLESLPLA
VEMTLEHRHY GKLVRVWRLL DPPLKQDQPQ GQPGGENGEN GEGGVPQPPE GMPGAPE
