ID GSPG_PSEAE Reviewed; 142 AA. AC Q00514; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-1992, sequence version 1. DT 27-MAR-2024, entry version 141. DE RecName: Full=Type II secretion system core protein G {ECO:0000303|PubMed:8331069}; DE Short=T2SS core protein G; DE AltName: Full=General secretion pathway protein G; DE AltName: Full=PilD-dependent protein PddA; DE Flags: Precursor; GN Name=xcpT; Synonyms=pddA; OrderedLocusNames=PA3101; OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1). OC Bacteria; Pseudomonadota; 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 / RC 1C / 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 / RC 1C / 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-9. 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, SUBUNIT, AND INTERACTION WITH PILA; XCPU; XCPV AND XCPW. 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 / RC 1C / 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 XCPX. 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 [8] RP SUBCELLULAR LOCATION. RX PubMed=17172336; DOI=10.1128/jb.01236-06; RA Arts J., van Boxtel R., Filloux A., Tommassen J., Koster M.; RT "Export of the pseudopilin XcpT of the Pseudomonas aeruginosa type II RT secretion system via the signal recognition particle-Sec pathway."; RL J. Bacteriol. 189:2069-2076(2007). RN [9] RP STRUCTURE BY NMR OF 33-142. RX PubMed=19747550; DOI=10.1016/j.jsb.2009.09.003; RA Alphonse S., Durand E., Douzi B., Waegele B., Darbon H., Filloux A., RA Voulhoux R., Bernard C.; RT "Structure of the Pseudomonas aeruginosa XcpT pseudopilin, a major RT component of the type II secretion system."; RL J. Struct. Biol. 169:75-80(2010). CC -!- FUNCTION: Core component of the type II secretion system required for CC the energy-dependent secretion of extracellular factors such as CC proteases and toxins from the periplasm (PubMed:9282737). Pseudopilin CC (pilin-like) protein that polymerizes to form the pseudopilus. Further CC polymerization triggers pseudopilus growth (PubMed:16012171). Type II CC pseudopilus confers increased bacterial adhesive capabilities CC (PubMed:12700254). {ECO:0000269|PubMed:12700254, CC ECO:0000269|PubMed:16012171, ECO:0000269|PubMed:9282737}. CC -!- SUBUNIT: Type II secretion system is composed of four main components: CC the outer membrane complex, the inner membrane complex, the cytoplasmic CC secretion ATPase and the periplasm-spanning pseudopilus. Forms CC homomultimers (PubMed:16012171). Interacts with pseudopilin tip ternary CC complex made of XcpX, XcpU, XcpV and XcpW (PubMed:16012171). Interacts CC with PilA (PubMed:9282737). {ECO:0000269|PubMed:16012171, CC ECO:0000269|PubMed:9282737}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:17172336, CC ECO:0000269|PubMed:8331069}; Single-pass membrane protein CC {ECO:0000255}. Note=Translocation to the cell inner membrane is CC independent of the presence of other Xcp components but depends on a CC functional Sec apparatus. {ECO:0000269|PubMed:17172336}. CC -!- PTM: Cleaved by the 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. CC {ECO:0000269|PubMed:8331069}. CC -!- SIMILARITY: Belongs to the GSP G family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAG06489.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X62666; CAA44535.1; -; Genomic_DNA. DR EMBL; M80792; AAA25946.1; -; Genomic_DNA. DR EMBL; AE004091; AAG06489.1; ALT_INIT; Genomic_DNA. DR PIR; E83258; E83258. DR PIR; S25386; SKPSXT. DR RefSeq; NP_251791.1; NC_002516.2. DR PDB; 2KEP; NMR; -; A=33-142. DR PDBsum; 2KEP; -. DR AlphaFoldDB; Q00514; -. DR BMRB; Q00514; -. DR SMR; Q00514; -. DR IntAct; Q00514; 1. DR STRING; 208964.PA3101; -. DR iPTMnet; Q00514; -. DR PaxDb; 208964-PA3101; -. DR DNASU; 878731; -. DR GeneID; 878731; -. DR KEGG; pae:PA3101; -. DR PATRIC; fig|208964.12.peg.3253; -. DR PseudoCAP; PA3101; -. DR HOGENOM; CLU_091705_2_1_6; -. DR InParanoid; Q00514; -. DR OrthoDB; 9795612at2; -. DR PhylomeDB; Q00514; -. DR EvolutionaryTrace; Q00514; -. DR Proteomes; UP000002438; Chromosome. 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; 3.30.700.10; Glycoprotein, Type 4 Pilin; 1. DR InterPro; IPR000983; Bac_GSPG_pilin. DR InterPro; IPR012902; N_methyl_site. DR InterPro; IPR045584; Pilin-like. DR InterPro; IPR013545; T2SS_protein-GspG_C. DR InterPro; IPR010054; Type2_sec_GspG. DR NCBIfam; TIGR02532; IV_pilin_GFxxxE; 1. DR NCBIfam; TIGR01710; typeII_sec_gspG; 1. DR PANTHER; PTHR30093; GENERAL SECRETION PATHWAY PROTEIN G; 1. DR PANTHER; PTHR30093:SF44; TYPE II SECRETION SYSTEM CORE PROTEIN G-RELATED; 1. DR Pfam; PF07963; N_methyl; 1. DR Pfam; PF08334; T2SSG; 1. DR PRINTS; PR00813; BCTERIALGSPG. DR SUPFAM; SSF54523; Pili subunits; 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..8 FT /note="Leader sequence" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01070, FT ECO:0000269|PubMed:8331069" FT /id="PRO_0000024208" FT CHAIN 9..142 FT /note="Type II secretion system core protein G" FT /id="PRO_0000024209" FT TRANSMEM 9..29 FT /note="Helical" FT /evidence="ECO:0000255" FT REGION 121..142 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 9 FT /note="N-methylphenylalanine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01070, FT ECO:0000269|PubMed:8331069" FT CONFLICT 131 FT /note="S -> T (in Ref. 2; AAA25946)" FT /evidence="ECO:0000305" FT HELIX 38..61 FT /evidence="ECO:0007829|PDB:2KEP" FT HELIX 70..76 FT /evidence="ECO:0007829|PDB:2KEP" FT TURN 91..93 FT /evidence="ECO:0007829|PDB:2KEP" FT STRAND 107..109 FT /evidence="ECO:0007829|PDB:2KEP" FT STRAND 113..116 FT /evidence="ECO:0007829|PDB:2KEP" FT STRAND 118..121 FT /evidence="ECO:0007829|PDB:2KEP" FT STRAND 130..135 FT /evidence="ECO:0007829|PDB:2KEP" FT STRAND 137..139 FT /evidence="ECO:0007829|PDB:2KEP" SQ SEQUENCE 142 AA; 15449 MW; B498621CFC45B9B7 CRC64; MQRRQQSGFT LIEIMVVVVI LGILAALVVP QVMSRPDQAK VTVAKGDIKA IAAALDMYKL DNFAYPSTQQ GLEALVKKPT GNPQPKNWNK DGYLKKLPVD PWGNPYQYLA PGTKGPFDLY SLGADGKEGG SDNDADIGNW DN //