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   27-MAR-2024, entry version 144.
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; 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=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 /
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   [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 /
RC   1C / 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 /
RC   1C / 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   EMDB; EMD-8860; -.
DR   SMR; P35818; -.
DR   DIP; DIP-60809N; -.
DR   STRING; 208964.PA3105; -.
DR   TCDB; 1.B.22.1.2; the outer bacterial membrane secretin (secretin) family.
DR   PaxDb; 208964-PA3105; -.
DR   ABCD; P35818; 1 sequenced antibody.
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   OrthoDB; 9775455at2; -.
DR   PhylomeDB; P35818; -.
DR   BioCyc; PAER208964:G1FZ6-3161-MONOMER; -.
DR   Proteomes; UP000002438; Chromosome.
DR   GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
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; IPR049371; GspD-like_N0.
DR   InterPro; IPR001775; GspD/PilQ.
DR   InterPro; IPR005644; NolW-like.
DR   InterPro; IPR038591; NolW-like_sf.
DR   InterPro; IPR004846; T2SS/T3SS_dom.
DR   InterPro; IPR013356; T2SS_GspD.
DR   InterPro; IPR004845; T2SS_GspD_CS.
DR   NCBIfam; TIGR02517; type_II_gspD; 1.
DR   PANTHER; PTHR30332; PROBABLE GENERAL SECRETION PATHWAY PROTEIN D; 1.
DR   PANTHER; PTHR30332:SF27; SECRETIN GSPD-RELATED; 1.
DR   Pfam; PF00263; Secretin; 1.
DR   Pfam; PF03958; Secretin_N; 3.
DR   Pfam; PF21305; type_II_gspD_N0; 1.
DR   PRINTS; PR00811; BCTERIALGSPD.
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
//