PILO_PSEAE
ID PILO_PSEAE Reviewed; 207 AA.
AC G3XD51;
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 PilO {ECO:0000303|PubMed:19857645};
GN Name=pilO; OrderedLocusNames=PA5042;
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; PILN 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 PILN.
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 PILN, AND MUTAGENESIS OF MET-92.
RX PubMed=25917913; DOI=10.1128/jb.00220-15;
RA Leighton T.L., Dayalani N., Sampaleanu L.M., Howell P.L., Burrows L.L.;
RT "Novel Role for PilNO in Type IV Pilus Retraction Revealed by Alignment
RT Subcomplex Mutations.";
RL J. Bacteriol. 197:2229-2238(2015).
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 {ECO:0000269|PubMed:19857645, ECO:0000269|PubMed:19857646}.
CC -!- SUBUNIT: Interacts with PilN (PubMed:19857645, PubMed:19857646,
CC PubMed:25917913). Interacts with PilP (via N-terminus)
CC (PubMed:19857645). Interacts with PilM (PubMed:19857645).
CC {ECO:0000269|PubMed:19857645, ECO:0000269|PubMed:19857646,
CC ECO:0000269|PubMed:25917913}.
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; AAG08427.1; -; Genomic_DNA.
DR PIR; S77728; S77728.
DR RefSeq; NP_253729.1; NC_002516.2.
DR RefSeq; WP_003103268.1; NZ_QZGE01000002.1.
DR AlphaFoldDB; G3XD51; -.
DR SMR; G3XD51; -.
DR STRING; 287.DR97_2397; -.
DR PaxDb; G3XD51; -.
DR PRIDE; G3XD51; -.
DR DNASU; 880985; -.
DR EnsemblBacteria; AAG08427; AAG08427; PA5042.
DR GeneID; 880985; -.
DR KEGG; pae:PA5042; -.
DR PATRIC; fig|208964.12.peg.5286; -.
DR PseudoCAP; PA5042; -.
DR HOGENOM; CLU_102444_1_0_6; -.
DR InParanoid; G3XD51; -.
DR OMA; TARTFRY; -.
DR PhylomeDB; G3XD51; -.
DR EvolutionaryTrace; G3XD51; -.
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 Gene3D; 3.30.70.60; -; 1.
DR InterPro; IPR007445; PilO.
DR InterPro; IPR014717; Transl_elong_EF1B/ribosomal_S6.
DR Pfam; PF04350; PilO; 1.
DR PIRSF; PIRSF016482; PilO; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..207
FT /note="Type IV pilus inner membrane component PilO"
FT /id="PRO_0000450558"
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MUTAGEN 92
FT /note="M->K: Reduced twitching motility and hyperpiliated
FT surface pili."
FT /evidence="ECO:0000269|PubMed:25917913"
SQ SEQUENCE 207 AA; 22819 MW; 99ADBD4424FFD127 CRC64;
MSLASSLESL RKIDINDLDL NNIGSWPAAV KVIVCVLLTA AVLALGYNFH LSDMQAQLEQ
QAAEEETLKQ QFSTKAFQAA NLEAYKAQMK EMEESFGALL RQLPSDTEVP GLLEDITRTG
LGSGLEFEEI KLLPEVAQQF YIELPIQISV VGGYHDLATF VSGVSSLPRI VTLHDFEIKP
VAPGSTSKLR MSILAKTYRY NDKGLKK
