PILP_PSEAE
ID PILP_PSEAE Reviewed; 174 AA.
AC G3XCX7;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Type IV pilus inner membrane component PilP {ECO:0000303|PubMed:19857645};
DE Flags: Precursor;
GN Name=pilP; OrderedLocusNames=PA5041;
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 [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 [2]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PILM; PILO AND PILN, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=19857645; DOI=10.1016/j.jmb.2009.09.034;
RA Ayers M., Sampaleanu L.M., Tammam S., Koo J., Harvey H., Howell P.L.,
RA Burrows L.L.;
RT "PilM/N/O/P proteins form an inner membrane complex that affects the
RT stability of the Pseudomonas aeruginosa type IV pilus secretin.";
RL J. Mol. Biol. 394:128-142(2009).
RN [3]
RP INTERACTION WITH PILO AND PILN.
RX PubMed=22053789; DOI=10.1111/j.1365-2958.2011.07903.x;
RA Tammam S., Sampaleanu L.M., Koo J., Sundaram P., Ayers M., Chong P.A.,
RA Forman-Kay J.D., Burrows L.L., Howell P.L.;
RT "Characterization of the PilN, PilO and PilP type IVa pilus subcomplex.";
RL Mol. Microbiol. 82:1496-1514(2011).
RN [4]
RP FUNCTION, AND INTERACTION WITH PILQ.
RX PubMed=23457250; DOI=10.1128/jb.00032-13;
RA Tammam S., Sampaleanu L.M., Koo J., Manoharan K., Daubaras M.,
RA Burrows L.L., Howell P.L.;
RT "PilMNOPQ from the Pseudomonas aeruginosa type IV pilus system form a
RT transenvelope protein interaction network that interacts with PilA.";
RL J. Bacteriol. 195:2126-2135(2013).
RN [5] {ECO:0007744|PDB:2Y4Y}
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 83-171 IN COMPLEX WITH ZINC.
RA Berry J., Derrick J.P.;
RT "Structure of a Domain from the Type Iv Pilus Biogenesis Lipoprotein Pilp,
RT from Pseudomonas Aeruginosa.";
RL Submitted (JAN-2011) to the PDB data bank.
RN [6] {ECO:0007744|PDB:2Y4X}
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 83-171.
RA Berry J., Derrick J.P.;
RT "Structure of a Domain from the Type Iv Pilus Biogenesis Lipoprotein
RT Pilp.";
RL Submitted (JAN-2011) to the PDB data bank.
CC -!- FUNCTION: Inner membrane component of the type IV (T4S) secretion
CC system that plays a role in surface and host cell adhesion,
CC colonization, biofilm maturation, virulence, and twitching, a form of
CC surface-associated motility. PilN/PilO heterodimers form the foundation
CC of the inner-membrane PilM/PilN/PilO/PilP complex which plays an
CC essential role in the assembly of a functional T4 pilus
CC (PubMed:19857645). PilP connects PilO to the secretin PilQ. In turn,
CC the PilM/PilN/PilO/PilP/PilQ complex facilitates transit of the pilus
CC through the periplasm and clamps the pilus in the cell envelope
CC (PubMed:23457250). {ECO:0000269|PubMed:19857645,
CC ECO:0000269|PubMed:23457250}.
CC -!- SUBUNIT: Interacts with PilO, PilN and PilM (PubMed:19857645,
CC PubMed:22053789). Interacts (via C-terminus) with the outer membrane
CC secretin PilQ (PubMed:23457250). {ECO:0000269|PubMed:19857645,
CC ECO:0000269|PubMed:22053789, ECO:0000269|PubMed:23457250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:19857645}; Lipid-anchor {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutants lack surface pili.
CC {ECO:0000269|PubMed:19857645}.
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DR EMBL; AE004091; AAG08426.1; -; Genomic_DNA.
DR PIR; S77729; S77729.
DR RefSeq; NP_253728.1; NC_002516.2.
DR RefSeq; WP_003095836.1; NZ_QZGE01000002.1.
DR PDB; 2Y4X; X-ray; 1.70 A; A/B=83-171.
DR PDB; 2Y4Y; X-ray; 1.70 A; A/B/C/D=83-171.
DR PDBsum; 2Y4X; -.
DR PDBsum; 2Y4Y; -.
DR AlphaFoldDB; G3XCX7; -.
DR SMR; G3XCX7; -.
DR STRING; 287.DR97_2396; -.
DR PaxDb; G3XCX7; -.
DR PRIDE; G3XCX7; -.
DR EnsemblBacteria; AAG08426; AAG08426; PA5041.
DR GeneID; 880984; -.
DR KEGG; pae:PA5041; -.
DR PATRIC; fig|208964.12.peg.5285; -.
DR PseudoCAP; PA5041; -.
DR HOGENOM; CLU_109321_1_0_6; -.
DR InParanoid; G3XCX7; -.
DR OMA; SGCWTER; -.
DR PhylomeDB; G3XCX7; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0044096; C:type IV pilus; IMP:PseudoCAP.
DR GO; GO:0043683; P:type IV pilus assembly; IMP:PseudoCAP.
DR GO; GO:0043107; P:type IV pilus-dependent motility; IMP:PseudoCAP.
DR InterPro; IPR007446; PilP.
DR Pfam; PF04351; PilP; 1.
DR PIRSF; PIRSF016481; Pilus_assembly_PilP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Lipoprotein; Membrane;
KW Palmitate; Reference proteome; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 18..174
FT /note="Type IV pilus inner membrane component PilP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT /id="PRO_5003460107"
FT LIPID 18
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 18
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:2Y4Y"
FT HELIX 93..96
FT /evidence="ECO:0007829|PDB:2Y4X"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:2Y4X"
FT STRAND 103..110
FT /evidence="ECO:0007829|PDB:2Y4X"
FT STRAND 113..120
FT /evidence="ECO:0007829|PDB:2Y4X"
FT STRAND 123..127
FT /evidence="ECO:0007829|PDB:2Y4X"
FT TURN 134..137
FT /evidence="ECO:0007829|PDB:2Y4X"
FT STRAND 138..144
FT /evidence="ECO:0007829|PDB:2Y4X"
FT STRAND 147..155
FT /evidence="ECO:0007829|PDB:2Y4X"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:2Y4X"
FT STRAND 161..169
FT /evidence="ECO:0007829|PDB:2Y4X"
SQ SEQUENCE 174 AA; 19054 MW; 52ED3027DA8E2E8F CRC64;
MRARLILSSL LLASLAGCGG GSDFADLQSY MDEVRARPKG TIEPLPKFQP YEAFTYSAAS
LRSPFQPPVK IDLTVRQKGN KVIKPDETRV KQFLEGFNIE TFEMVGTLSN AQGTFALVKG
AGGVHRVRVG DYLGRNDGKV VGISEGKIDV IEIVPDGEGN WLERPRSLTL KERS
