GSPG_PSEAE
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 03-AUG-2022, entry version 133.
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; 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-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 / 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 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};
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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; 287.DR97_4832; -.
DR PaxDb; Q00514; -.
DR PRIDE; Q00514; -.
DR DNASU; 878731; -.
DR EnsemblBacteria; AAG06489; AAG06489; PA3101.
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 OMA; EMLVVIT; -.
DR PhylomeDB; Q00514; -.
DR EvolutionaryTrace; Q00514; -.
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; 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 Pfam; PF07963; N_methyl; 1.
DR Pfam; PF08334; T2SSG; 1.
DR PRINTS; PR00813; BCTERIALGSPG.
DR SUPFAM; SSF54523; SSF54523; 1.
DR TIGRFAMs; TIGR02532; IV_pilin_GFxxxE; 1.
DR TIGRFAMs; TIGR01710; typeII_sec_gspG; 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
