GSPD_PSEAE
ID GSPD_PSEAE Reviewed; 658 AA.
AC P35818; Q9HZB2;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Secretin XcpQ {ECO:0000303|PubMed:23188826};
DE AltName: Full=General secretion pathway protein D;
DE AltName: Full=Type II secretion system protein D;
DE Short=T2SS protein D;
DE Flags: Precursor;
GN Name=xcpQ {ECO:0000303|PubMed:7934833}; OrderedLocusNames=PA3105;
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=7934833; DOI=10.1111/j.1365-2958.1993.tb02674.x;
RA Akrim M., Bally M., Ball G., Tommassen J., Teerink H., Filloux A.,
RA Lazdunski A.;
RT "Xcp-mediated protein secretion in Pseudomonas aeruginosa: identification
RT of two additional genes and evidence for regulation of xcp gene
RT expression.";
RL Mol. Microbiol. 10:431-443(1993).
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] {ECO:0007744|PDB:4E9J, ECO:0007744|PDB:4EC5}
RP X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS) OF 35-277, AND FUNCTION.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=23188826; DOI=10.1074/jbc.m112.432096;
RA Van der Meeren R., Wen Y., Van Gelder P., Tommassen J., Devreese B.,
RA Savvides S.N.;
RT "New insights into the assembly of bacterial secretins: structural studies
RT of the periplasmic domain of XcpQ from Pseudomonas aeruginosa.";
RL J. Biol. Chem. 288:1214-1225(2013).
RN [4] {ECO:0007744|PDB:5WLN}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.57 ANGSTROMS) OF 35-658, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=29042496; DOI=10.1128/mbio.01344-17;
RA Hay I.D., Belousoff M.J., Lithgow T.;
RT "Structural basis of type 2 secretion system engagement between the inner
RT and outer bacterial membranes.";
RL MBio 8:0-0(2017).
RN [5] {ECO:0007744|PDB:5MP2, ECO:0007744|PDB:5NGI}
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 35-274, FUNCTION, DOMAIN, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=29042493; DOI=10.1128/mbio.01185-17;
RA Douzi B., Trinh N.T.T., Michel-Souzy S., Desmyter A., Ball G., Barbier P.,
RA Kosta A., Durand E., Forest K.T., Cambillau C., Roussel A., Voulhoux R.;
RT "Unraveling the self-assembly of the Pseudomonas aeruginosa XcpQ secretin
RT periplasmic domain provides new molecular insights into type II secretion
RT system secreton architecture and dynamics.";
RL MBio 8:0-0(2017).
CC -!- FUNCTION: Involved in a type II secretion system (T2SS, formerly
CC general secretion pathway, GSP) for the export of proteins (Probable).
CC This subunit forms the outer membrane channel (By similarity). Among
CC its substrates are PrpL, elastase LasB, chitin binding protein D
CC (CbpD), aminopeptidase PaAP, and metalloprotease ImpA (PubMed:29042496,
CC PubMed:29042493). {ECO:0000250|UniProtKB:P45779,
CC ECO:0000269|PubMed:29042493, ECO:0000269|PubMed:29042496,
CC ECO:0000305|PubMed:10984043}.
CC -!- SUBUNIT: Forms a cylindrical channel with 15 subunits. The closed
CC pentadecameric channel is 170 Angstroms long and 140 Angstroms in
CC diameter. {ECO:0000269|PubMed:29042496}.
CC -!- INTERACTION:
CC P35818; P35818: xcpQ; NbExp=2; IntAct=EBI-16224942, EBI-16224942;
CC -!- SUBCELLULAR LOCATION: Cell outer membrane
CC {ECO:0000305|PubMed:29042496}. Note=Most of the protein is in the
CC periplasm which it traverses to contact proteins of the cell inner
CC membrane. {ECO:0000305|PubMed:23188826, ECO:0000305|PubMed:29042493,
CC ECO:0000305|PubMed:29042496}.
CC -!- DOMAIN: The N0, N1, N2 and N3 domains are periplasmic, while the
CC secretin and S domains form a channel that is partially inserted in the
CC outer membrane. The N1, N2 and N3 domains each form a periplasmic ring;
CC the N0 domain was present but not resolved by electron microscopy. The
CC secretin domain forms a double beta-barrel structure; the outer barrel
CC has a diameter of about 140 Angstroms while the inner barrel forms the
CC central gate with a small pore in the closed state (PubMed:29042496).
CC Isolated N-terminus (domains N0, N1 and N2) assembles as a hexamer of
CC dimers (i.e. dodecamers). The N0 domain probably moves during export
CC (PubMed:29042493). It has been suggested that the C15 symmetry of the
CC C-terminus may transit to a C6 symmetry by displacement of 3 of the N-
CC terminii (Probable). {ECO:0000269|PubMed:29042493,
CC ECO:0000269|PubMed:29042496, ECO:0000305|PubMed:29042493,
CC ECO:0000305|PubMed:29042496}.
CC -!- DISRUPTION PHENOTYPE: Loss of export of PrpL, elastase LasB, chitin
CC binding protein D (CbpD), aminopeptidase PaAP, and metalloprotease
CC ImpA, still exports LapA and AprA. {ECO:0000269|PubMed:29042493}.
CC -!- SIMILARITY: Belongs to the bacterial secretin family. GSP D subfamily.
CC {ECO:0000305}.
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DR EMBL; X68594; CAA48582.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG06493.1; -; Genomic_DNA.
DR PIR; S39653; S39653.
DR RefSeq; NP_251795.1; NC_002516.2.
DR RefSeq; WP_003113934.1; NZ_QZGE01000009.1.
DR PDB; 4E9J; X-ray; 2.03 A; A/B=35-277.
DR PDB; 4EC5; X-ray; 2.20 A; A/B=35-277.
DR PDB; 5MP2; X-ray; 2.90 A; A/B=35-274.
DR PDB; 5NGI; X-ray; 2.98 A; A/B=35-275.
DR PDB; 5WLN; EM; 3.57 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O=35-658.
DR PDBsum; 4E9J; -.
DR PDBsum; 4EC5; -.
DR PDBsum; 5MP2; -.
DR PDBsum; 5NGI; -.
DR PDBsum; 5WLN; -.
DR AlphaFoldDB; P35818; -.
DR SMR; P35818; -.
DR DIP; DIP-60809N; -.
DR STRING; 287.DR97_4828; -.
DR TCDB; 1.B.22.1.2; the outer bacterial membrane secretin (secretin) family.
DR PaxDb; P35818; -.
DR PRIDE; P35818; -.
DR ABCD; P35818; 1 sequenced antibody.
DR EnsemblBacteria; AAG06493; AAG06493; PA3105.
DR GeneID; 880114; -.
DR KEGG; pae:PA3105; -.
DR PATRIC; fig|208964.12.peg.3257; -.
DR PseudoCAP; PA3105; -.
DR HOGENOM; CLU_006756_1_1_6; -.
DR InParanoid; P35818; -.
DR OMA; YAVVEMD; -.
DR PhylomeDB; P35818; -.
DR BioCyc; PAER208964:G1FZ6-3161-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0015627; C:type II protein secretion system complex; IDA:PseudoCAP.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0009306; P:protein secretion; IBA:GO_Central.
DR GO; GO:0015628; P:protein secretion by the type II secretion system; IDA:PseudoCAP.
DR Gene3D; 3.30.1370.120; -; 3.
DR InterPro; IPR001775; GspD/PilQ.
DR InterPro; IPR005644; NolW-like.
DR InterPro; IPR038591; NolW-like_sf.
DR InterPro; IPR004846; T2SS/T3SS.
DR InterPro; IPR013356; T2SS_GspD.
DR InterPro; IPR004845; T2SS_GspD_CS.
DR Pfam; PF00263; Secretin; 1.
DR Pfam; PF03958; Secretin_N; 3.
DR PRINTS; PR00811; BCTERIALGSPD.
DR TIGRFAMs; TIGR02517; type_II_gspD; 1.
DR PROSITE; PS00875; T2SP_D; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell outer membrane; Membrane; Protein transport;
KW Reference proteome; Signal; Transmembrane; Transmembrane beta strand;
KW Transport.
FT SIGNAL 1..34
FT /evidence="ECO:0000255"
FT CHAIN 35..658
FT /note="Secretin XcpQ"
FT /id="PRO_0000013104"
FT REGION 51..141
FT /note="N0"
FT /evidence="ECO:0000305|PubMed:29042493"
FT REGION 142..205
FT /note="N1"
FT /evidence="ECO:0000305|PubMed:29042493"
FT REGION 206..279
FT /note="N2"
FT /evidence="ECO:0000305|PubMed:29042493"
FT REGION 280..365
FT /note="N3"
FT /evidence="ECO:0000305|PubMed:29042493"
FT REGION 302..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 368..606
FT /note="Secretin"
FT /evidence="ECO:0000305|PubMed:29042493"
FT REGION 608..658
FT /note="S domain"
FT /evidence="ECO:0000305|PubMed:29042493"
FT COMPBIAS 302..318
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 466
FT /note="May serve as a pivot that allows opening of the
FT central gate for substrate egress"
FT /evidence="ECO:0000250|UniProtKB:P45779"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:4E9J"
FT STRAND 52..61
FT /evidence="ECO:0007829|PDB:4E9J"
FT HELIX 62..73
FT /evidence="ECO:0007829|PDB:4E9J"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:4E9J"
FT STRAND 86..96
FT /evidence="ECO:0007829|PDB:4E9J"
FT HELIX 97..110
FT /evidence="ECO:0007829|PDB:4E9J"
FT STRAND 113..117
FT /evidence="ECO:0007829|PDB:4E9J"
FT STRAND 119..126
FT /evidence="ECO:0007829|PDB:4E9J"
FT STRAND 145..150
FT /evidence="ECO:0007829|PDB:4E9J"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:4E9J"
FT HELIX 156..163
FT /evidence="ECO:0007829|PDB:4E9J"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:4E9J"
FT STRAND 171..176
FT /evidence="ECO:0007829|PDB:4E9J"
FT HELIX 177..179
FT /evidence="ECO:0007829|PDB:4E9J"
FT STRAND 181..186
FT /evidence="ECO:0007829|PDB:4E9J"
FT HELIX 188..202
FT /evidence="ECO:0007829|PDB:4E9J"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:5MP2"
FT STRAND 209..213
FT /evidence="ECO:0007829|PDB:4E9J"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:4E9J"
FT HELIX 219..231
FT /evidence="ECO:0007829|PDB:4E9J"
FT STRAND 235..237
FT /evidence="ECO:0007829|PDB:4EC5"
FT STRAND 242..246
FT /evidence="ECO:0007829|PDB:4E9J"
FT HELIX 247..249
FT /evidence="ECO:0007829|PDB:4E9J"
FT STRAND 251..257
FT /evidence="ECO:0007829|PDB:4E9J"
FT HELIX 258..271
FT /evidence="ECO:0007829|PDB:4E9J"
SQ SEQUENCE 658 AA; 69953 MW; EC2F81FD1A185D50 CRC64;
MSQPLLRALF APSSRSYVPA VLLSLALGIQ AAHAENSGGN AFVPAGNQQE AHWTINLKDA
DIREFIDQIS EITGETFVVD PRVKGQVSVV SKAQLSLSEV YQLFLSVMST HGFTVVAQGD
QARIVPNAEA KTEAGGGQSA PDRLETRVIQ VQQSPVSELI PLIRPLVPQY GHLAAVPSAN
ALIISDRSAN IARIEDVIRQ LDQKGSHDYS VINLRYGWVM DAAEVLNNAM SRGQAKGAAG
AQVIADARTN RLIILGPPQA RAKLVQLAQS LDTPTARSAN TRVIRLRHND AKTLAETLGQ
ISEGMKNNGG QGGEQTGGGR PSNILIRADE STNALVLLAD PDTVNALEDI VRQLDVPRAQ
VLVEAAIVEI SGDIQDAVGV QWAINKGGMG GTKTNFANTG LSIGTLLQSL ESNKAPESIP
DGAIVGIGSS SFGALVTALS ANTKSNLLST PSLLTLDNQK AEILVGQNVP FQTGSYTTNS
EGSSNPFTTV ERKDIGVSLK VTPHINDGAA LRLEIEQEIS ALLPNAQQRN NTDLITSKRS
IKSTILAENG QVIVIGGLIQ DDVSQAESKV PLLGDIPLLG RLFRSTKDTH TKRNLMVFLR
PTVVRDSAGL AALSGKKYSD IRVIDGTRGP EGRPSILPTN ANQLFDGQAV DLRELMTE
