GSPK_PSEAE
ID GSPK_PSEAE Reviewed; 333 AA.
AC Q00518;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Type II secretion system protein K;
DE Short=T2SS protein K;
DE AltName: Full=General secretion pathway protein K;
DE Flags: Precursor;
GN Name=xcpX; OrderedLocusNames=PA3097;
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 [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 [3]
RP FUNCTION, MUTAGENESIS OF GLY-7, AND CLEAVAGE BY PREPILIN PEPTIDASE.
RX PubMed=9466253; DOI=10.1046/j.1365-2958.1998.00653.x;
RA Bleves S., Voulhoux R., Michel G., Lazdunski A., Tommassen J., Filloux A.;
RT "The secretion apparatus of Pseudomonas aeruginosa: identification of a
RT fifth pseudopilin, XcpX (GspK family).";
RL Mol. Microbiol. 27:31-40(1998).
RN [4]
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 [5]
RP FUNCTION, AND INTERACTION WITH XCPT.
RX PubMed=16012171; DOI=10.1074/jbc.m505812200;
RA Durand E., Michel G., Voulhoux R., Kuerner J., Bernadac A., Filloux A.;
RT "XcpX controls biogenesis of the Pseudomonas aeruginosa XcpT-containing
RT pseudopilus.";
RL J. Biol. Chem. 280:31378-31389(2005).
RN [6]
RP FUNCTION, AND INTERACTION WITH XCPV; XCPW AMD XCPU.
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 [7]
RP X-RAY CRYSTALLOGRAPHY (2.04 ANGSTROMS) OF 44-316, AND FUNCTION.
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:30346996). Plays a role in
CC pseudopilus assembly and seems to control its length (PubMed:16012171).
CC Interacts with the pseudopilus tip complex that is critical for the
CC recognition and binding of secretion substrates (PubMed:19828448,
CC PubMed:9466253). Type II pseudopilus confers increased bacterial
CC adhesive capabilities (PubMed:12700254). {ECO:0000269|PubMed:12700254,
CC ECO:0000269|PubMed:16012171, ECO:0000269|PubMed:19828448,
CC ECO:0000269|PubMed:30346996, ECO:0000269|PubMed:9466253}.
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 the tip of the type II pseudopilus subunits XcpV, XcpU and XcpW
CC (PubMed:19828448, PubMed:30346996). Interacts with core component XcpT
CC (PubMed:16012171). {ECO:0000269|PubMed:16012171,
CC ECO:0000269|PubMed:19828448, ECO:0000269|PubMed:30346996}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}.
CC -!- PTM: Cleaved by prepilin peptidase. {ECO:0000269|PubMed:9466253}.
CC -!- SIMILARITY: Belongs to the GSP K family. {ECO:0000305}.
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DR EMBL; X62666; CAA44539.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG06485.1; -; Genomic_DNA.
DR PIR; S25390; SKPSXX.
DR RefSeq; NP_251787.1; NC_002516.2.
DR RefSeq; WP_003103524.1; NZ_QZGE01000009.1.
DR PDB; 5VTM; X-ray; 2.04 A; X=44-316.
DR PDB; 6UTU; X-ray; 2.85 A; C/F/I=44-316.
DR PDBsum; 5VTM; -.
DR PDBsum; 6UTU; -.
DR AlphaFoldDB; Q00518; -.
DR SMR; Q00518; -.
DR STRING; 287.DR97_4836; -.
DR PaxDb; Q00518; -.
DR PRIDE; Q00518; -.
DR DNASU; 882779; -.
DR EnsemblBacteria; AAG06485; AAG06485; PA3097.
DR GeneID; 882779; -.
DR KEGG; pae:PA3097; -.
DR PATRIC; fig|208964.12.peg.3249; -.
DR PseudoCAP; PA3097; -.
DR HOGENOM; CLU_057294_1_0_6; -.
DR InParanoid; Q00518; -.
DR OMA; AYWYSIG; -.
DR PhylomeDB; Q00518; -.
DR BioCyc; PAER208964:G1FZ6-3153-MON; -.
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 Gene3D; 1.10.40.60; -; 2.
DR InterPro; IPR005628; GspK.
DR InterPro; IPR038072; GspK_central_sf.
DR InterPro; IPR045584; Pilin-like.
DR PANTHER; PTHR38831; PTHR38831; 1.
DR Pfam; PF03934; T2SSK; 1.
DR PIRSF; PIRSF002786; XcpX; 1.
DR SUPFAM; SSF158544; SSF158544; 2.
DR SUPFAM; SSF54523; SSF54523; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Membrane;
KW Protein transport; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT PROPEP 1..7
FT /note="Leader sequence"
FT /evidence="ECO:0000269|PubMed:9466253"
FT /id="PRO_0000449562"
FT CHAIN 8..333
FT /note="Type II secretion system protein K"
FT /id="PRO_0000449563"
FT TRANSMEM 8..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..333
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT REGION 313..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 7
FT /note="G->V: Complete loss of secretion."
FT /evidence="ECO:0000269|PubMed:9466253"
FT HELIX 45..65
FT /evidence="ECO:0007829|PDB:5VTM"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:5VTM"
FT STRAND 98..104
FT /evidence="ECO:0007829|PDB:5VTM"
FT HELIX 106..108
FT /evidence="ECO:0007829|PDB:5VTM"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:5VTM"
FT HELIX 112..115
FT /evidence="ECO:0007829|PDB:5VTM"
FT HELIX 123..135
FT /evidence="ECO:0007829|PDB:5VTM"
FT HELIX 140..154
FT /evidence="ECO:0007829|PDB:5VTM"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:5VTM"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:5VTM"
FT HELIX 168..171
FT /evidence="ECO:0007829|PDB:5VTM"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:5VTM"
FT HELIX 188..193
FT /evidence="ECO:0007829|PDB:5VTM"
FT HELIX 198..204
FT /evidence="ECO:0007829|PDB:5VTM"
FT HELIX 205..207
FT /evidence="ECO:0007829|PDB:5VTM"
FT TURN 219..221
FT /evidence="ECO:0007829|PDB:5VTM"
FT HELIX 224..230
FT /evidence="ECO:0007829|PDB:5VTM"
FT HELIX 235..245
FT /evidence="ECO:0007829|PDB:5VTM"
FT TURN 246..248
FT /evidence="ECO:0007829|PDB:5VTM"
FT HELIX 253..261
FT /evidence="ECO:0007829|PDB:5VTM"
FT TURN 262..264
FT /evidence="ECO:0007829|PDB:6UTU"
FT STRAND 272..275
FT /evidence="ECO:0007829|PDB:5VTM"
FT STRAND 277..287
FT /evidence="ECO:0007829|PDB:5VTM"
FT STRAND 290..300
FT /evidence="ECO:0007829|PDB:5VTM"
FT STRAND 306..312
FT /evidence="ECO:0007829|PDB:5VTM"
SQ SEQUENCE 333 AA; 37000 MW; DCFCF3E4830DCC0E CRC64;
MRRGQNGVAL ITVLLVVAVV TIVCAGLIIR QQLAIRSSAN QLHVRQAWHY ALGGERLAEA
VLRRDLRQGG ENTREPVDHL GEAWARPMTP FKLDDGGELR VRIEDPSGRF NLNGLVRKRK
VKPDSVKQFR RLLATLGMKE EIVQGLPDRL ADWLDADQNP QGEQGAEDNQ YLLEAPAYRA
ANRSFKDVSE LRLLKLSEAD YRRLLPFVSA LPEDAPLNVN TASVPVLAAM FEIDPGQAEN
IVDARGREGF QSKDDFTKHL TQLGSKTGNV SYAVGTRYFQ VISEVSLGDR RQVLVSTLQR
GKDGKIRVMA RDMGQGGLPI PSTGGDDWKK DER
