GSPH_PSEAE
ID GSPH_PSEAE Reviewed; 172 AA.
AC Q00515;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Type II secretion system protein H {ECO:0000303|PubMed:8331069};
DE Short=T2SS minor pseudopilin H;
DE AltName: Full=General secretion pathway protein H;
DE AltName: Full=PilD-dependent protein PddB;
DE Flags: Precursor;
GN Name=xcpU; Synonyms=pddB; OrderedLocusNames=PA3100;
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-7.
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, AND INTERACTION WITH XCPT.
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 XCPV; XCPW AMD XCPX.
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).
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:9282737). Part of the pseudopilus
CC tip complex that is critical for the recognition and binding of
CC secretion substrates (PubMed:19828448). Type II pseudopilus confers
CC increased bacterial adhesive capabilities (PubMed:12700254).
CC {ECO:0000269|PubMed:12700254, ECO:0000269|PubMed:19828448,
CC ECO:0000269|PubMed:9282737}.
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. Forms the tip
CC of the type II pseudopilus by interacting with XcpV, XcpW and XcpX
CC (PubMed:19828448). Interacts with core component XcpT (PubMed:9282737).
CC {ECO:0000269|PubMed:19828448, ECO:0000269|PubMed:9282737}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:8331069};
CC Single-pass membrane protein {ECO:0000255}.
CC -!- PTM: Cleaved by 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 by prepilin
CC peptidase. {ECO:0000269|PubMed:8331069}.
CC -!- SIMILARITY: Belongs to the GSP H family. {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; CAA44536.1; -; Genomic_DNA.
DR EMBL; M80792; AAA25947.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG06488.1; -; Genomic_DNA.
DR PIR; S25387; SKPSXU.
DR RefSeq; NP_251790.1; NC_002516.2.
DR RefSeq; WP_003103530.1; NZ_QZGE01000009.1.
DR AlphaFoldDB; Q00515; -.
DR SMR; Q00515; -.
DR STRING; 287.DR97_4833; -.
DR PaxDb; Q00515; -.
DR EnsemblBacteria; AAG06488; AAG06488; PA3100.
DR GeneID; 882756; -.
DR KEGG; pae:PA3100; -.
DR PATRIC; fig|208964.12.peg.3252; -.
DR PseudoCAP; PA3100; -.
DR HOGENOM; CLU_111963_2_1_6; -.
DR InParanoid; Q00515; -.
DR OMA; DETAMRW; -.
DR BioCyc; PAER208964:G1FZ6-3156-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:0044096; C:type IV pilus; IBA:GO_Central.
DR GO; GO:0071978; P:bacterial-type flagellum-dependent swarming motility; IMP:PseudoCAP.
DR GO; GO:0015628; P:protein secretion by the type II secretion system; IDA:PseudoCAP.
DR GO; GO:0044010; P:single-species biofilm formation; IMP:PseudoCAP.
DR GO; GO:0043683; P:type IV pilus assembly; IBA:GO_Central.
DR GO; GO:0043107; P:type IV pilus-dependent motility; IBA:GO_Central.
DR InterPro; IPR012902; N_methyl_site.
DR InterPro; IPR045584; Pilin-like.
DR InterPro; IPR022346; T2SS_GspH.
DR InterPro; IPR002416; T2SS_protein-GspH.
DR Pfam; PF12019; GspH; 1.
DR Pfam; PF07963; N_methyl; 1.
DR PRINTS; PR00885; BCTERIALGSPH.
DR SUPFAM; SSF54523; SSF54523; 1.
DR TIGRFAMs; TIGR02532; IV_pilin_GFxxxE; 1.
DR TIGRFAMs; TIGR01708; typeII_sec_gspH; 1.
DR PROSITE; PS00409; PROKAR_NTER_METHYL; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Membrane; Methylation;
KW Protein transport; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT PROPEP 1..6
FT /note="Leader sequence"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01070,
FT ECO:0000269|PubMed:8331069"
FT /id="PRO_0000024224"
FT CHAIN 7..172
FT /note="Type II secretion system protein H"
FT /id="PRO_0000024225"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 7
FT /note="N-methylphenylalanine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01070,
FT ECO:0000269|PubMed:8331069"
FT CONFLICT 82
FT /note="K -> N (in Ref. 2; AAA25947)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 172 AA; 19148 MW; C42F83D5CA32958A CRC64;
MRASRGFTLI ELMVVMVIIS VLIGLAVLST GFASTSRELD SEAERLAGLI GVLTDEAVLD
NREYGLRLER DAYQVLRYDE AKARWLPVAR DSHRLPEWAE LTFELDGQPL VLAGSKGEKE
QKKGTDQPQL LILSSGELSP FRLRLAERGP EGRALSLSSD GFRLPRVEVA RR
