PILN_PSEAE
ID PILN_PSEAE Reviewed; 198 AA.
AC G3XD30;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 03-AUG-2022, entry version 52.
DE RecName: Full=Type IV pilus inner membrane component PilN {ECO:0000303|PubMed:19857645};
GN Name=pilN; OrderedLocusNames=PA5043;
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 PILP, 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 FUNCTION, AND INTERACTION WITH PILO AND PILM.
RX PubMed=19857646; DOI=10.1016/j.jmb.2009.09.037;
RA Sampaleanu L.M., Bonanno J.B., Ayers M., Koo J., Tammam S., Burley S.K.,
RA Almo S.C., Burrows L.L., Howell P.L.;
RT "Periplasmic domains of Pseudomonas aeruginosa PilN and PilO form a stable
RT heterodimeric complex.";
RL J. Mol. Biol. 394:143-159(2009).
RN [4]
RP INTERACTION WITH PILP AND PILO.
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 [5]
RP INTERACTION WITH PILO, AND SUBUNIT.
RX PubMed=27474743; DOI=10.1074/jbc.m116.738377;
RA Leighton T.L., Yong D.H., Howell P.L., Burrows L.L.;
RT "Type IV Pilus Alignment Subcomplex Proteins PilN and PilO Form Homo- and
RT Heterodimers in Vivo.";
RL J. Biol. Chem. 291:19923-19938(2016).
RN [6] {ECO:0007744|PDB:5EOU}
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 1-12, FUNCTION, AND INTERACTION
RP WITH PILM.
RX PubMed=27022027; DOI=10.1074/jbc.m116.718353;
RA McCallum M., Tammam S., Little D.J., Robinson H., Koo J., Shah M.,
RA Calmettes C., Moraes T.F., Burrows L.L., Howell P.L.;
RT "PilN Binding Modulates the Structure and Binding Partners of the
RT Pseudomonas aeruginosa Type IVa Pilus Protein PilM.";
RL J. Biol. Chem. 291:11003-11015(2016).
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, PubMed:19857646). In turn, associates with PilM and
CC facilitates PilM functionally relevant structural changes
CC (PubMed:27022027). {ECO:0000269|PubMed:19857645,
CC ECO:0000269|PubMed:19857646, ECO:0000269|PubMed:27022027}.
CC -!- SUBUNIT: Homodimer (PubMed:27474743). Interacts with PilO
CC (PubMed:19857645, PubMed:19857646, PubMed:22053789, PubMed:27474743).
CC Interacts with PilP (via N-terminus) (PubMed:22053789). Interacts (via
CC N-terminus) with PilM; this interaction modulates PilM ATP binding site
CC (PubMed:19857646, PubMed:27022027). {ECO:0000269|PubMed:19857645,
CC ECO:0000269|PubMed:19857646, ECO:0000269|PubMed:22053789,
CC ECO:0000269|PubMed:27022027, ECO:0000269|PubMed:27474743}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:19857645}; Single-pass type II membrane protein
CC {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutants lack surface pili.
CC {ECO:0000269|PubMed:19857645}.
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DR EMBL; AE004091; AAG08428.1; -; Genomic_DNA.
DR PIR; S77727; S77727.
DR RefSeq; NP_253730.1; NC_002516.2.
DR RefSeq; WP_003095839.1; NZ_QZGE01000002.1.
DR PDB; 5EOU; X-ray; 2.40 A; A/B=1-12.
DR PDBsum; 5EOU; -.
DR AlphaFoldDB; G3XD30; -.
DR SMR; G3XD30; -.
DR STRING; 287.DR97_2398; -.
DR PaxDb; G3XD30; -.
DR PRIDE; G3XD30; -.
DR EnsemblBacteria; AAG08428; AAG08428; PA5043.
DR GeneID; 881025; -.
DR KEGG; pae:PA5043; -.
DR PATRIC; fig|208964.12.peg.5287; -.
DR PseudoCAP; PA5043; -.
DR HOGENOM; CLU_081304_1_2_6; -.
DR InParanoid; G3XD30; -.
DR OMA; DRNLPVH; -.
DR PhylomeDB; G3XD30; -.
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: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; IPR007813; PilN.
DR Pfam; PF05137; PilN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..198
FT /note="Type IV pilus inner membrane component PilN"
FT /id="PRO_0000450557"
FT TRANSMEM 19..39
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 198 AA; 22214 MW; 7920C66DB3351DDC CRC64;
MARINLLPWR EELREQRKQQ FLVILGGVLV ASAALVFLGD QYFTAAIENQ NARNDFLRKE
IVVLDARIKE ISELKSRRQQ LLERMKIIQD LQGNRPIIGR VFDQLVRTLP DGVYFTDLKM
TGKNIAIAGA AESNNRVSNL MRNMDASEWL TAPTLNEVKA VTQGAVDQAN VFQLTVQQTQ
PGEEDAKAKH GVAQGAKK