PILA4_THET2
ID PILA4_THET2 Reviewed; 131 AA.
AC Q72JC0;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=Type IV wide pilus major component PilA4 {ECO:0000303|PubMed:12839734};
DE AltName: Full=Type IV major pilin PilA4;
DE Flags: Precursor;
GN Name=pilA4; OrderedLocusNames=TT_C0858;
OS Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=262724;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
RX PubMed=15064768; DOI=10.1038/nbt956;
RA Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H.,
RA Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C.,
RA Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P.,
RA Kramer W., Merkl R., Gottschalk G., Fritz H.-J.;
RT "The genome sequence of the extreme thermophile Thermus thermophilus.";
RL Nat. Biotechnol. 22:547-553(2004).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12839734; DOI=10.1128/aem.69.7.3695-3700.2003;
RA Friedrich A., Rumszauer J., Henne A., Averhoff B.;
RT "Pilin-like proteins in the extremely thermophilic bacterium Thermus
RT thermophilus HB27: implication in competence for natural transformation and
RT links to type IV pilus biogenesis.";
RL Appl. Environ. Microbiol. 69:3695-3700(2003).
RN [3]
RP FUNCTION, GLYCOSYLATION, SUBCELLULAR LOCATION, AND INTERACTION WITH PILQ.
RX PubMed=16857013; DOI=10.1111/j.1742-4658.2006.05335.x;
RA Rumszauer J., Schwarzenlander C., Averhoff B.;
RT "Identification, subcellular localization and functional interactions of
RT PilMNOWQ and PilA4 involved in transformation competency and pilus
RT biogenesis in the thermophilic bacterium Thermus thermophilus HB27.";
RL FEBS J. 273:3261-3272(2006).
RN [4]
RP FUNCTION.
RX PubMed=19396940; DOI=10.1111/j.1462-2920.2008.01801.x;
RA Schwarzenlander C., Haase W., Averhoff B.;
RT "The role of single subunits of the DNA transport machinery of Thermus
RT thermophilus HB27 in DNA binding and transport.";
RL Environ. Microbiol. 11:801-808(2009).
RN [5]
RP INDUCTION BY LOW TEMPERATURE.
RX PubMed=24935261; DOI=10.1111/1574-6968.12506;
RA Salzer R., Kern T., Joos F., Averhoff B.;
RT "Environmental factors affecting the expression of type IV pilus genes as
RT well as piliation of Thermus thermophilus.";
RL FEMS Microbiol. Lett. 357:56-62(2014).
RN [6] {ECO:0007744|PDB:6XXD}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.22 ANGSTROMS) OF 7-121, DISRUPTION
RP PHENOTYPE, GLYCOSYLATION, FUNCTION, AND DISULFIDE BOND.
RX PubMed=32376942; DOI=10.1038/s41467-020-15650-w;
RA Neuhaus A., Selvaraj M., Salzer R., Langer J.D., Kruse K., Kirchner L.,
RA Sanders K., Daum B., Averhoff B., Gold V.A.M.;
RT "Cryo-electron microscopy reveals two distinct type IV pili assembled by
RT the same bacterium.";
RL Nat. Commun. 11:2231-2231(2020).
CC -!- FUNCTION: Plays an essential role in the assembly of two types of T4P
CC pili: a wide and a narrow that participate in natural transformation
CC and twitching motility (PubMed:32376942). Major component of the wide
CC pilus that is essential for natural transformation working as a DNA
CC translocator structure that spans the inner and outer membranes
CC (PubMed:12839734, PubMed:19396940, PubMed:32376942, PubMed:16857013).
CC In addition, participates in the assembly of the narrow pilus composed
CC of the PilA5 subunit that is required for twitching motility
CC (PubMed:32376942). {ECO:0000269|PubMed:12839734,
CC ECO:0000269|PubMed:16857013, ECO:0000269|PubMed:19396940,
CC ECO:0000269|PubMed:32376942}.
CC -!- SUBUNIT: Interacts with PilQ. {ECO:0000269|PubMed:16857013}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:16857013}; Single-pass membrane protein
CC {ECO:0000255}. Cell outer membrane {ECO:0000269|PubMed:16857013};
CC Single-pass membrane protein {ECO:0000255}. Periplasm
CC {ECO:0000269|PubMed:16857013}. Note=The single N-terminal transmembrane
CC is initially involved in the correct localization to the inner
CC membrane. Once the leader sequence cleaved, this region plays a role in
CC multimerization and protein-protein interactions in the periplasm and
CC the outer membrane. {ECO:0000305|PubMed:16857013}.
CC -!- INDUCTION: By growth in minimal medium or low temperature leading to a
CC significant increase in pilA4 transcripts.
CC {ECO:0000269|PubMed:24935261}.
CC -!- PTM: Found in three forms of 14-kDa, 18-kDa and a glycosylated 23-kDa
CC form (PubMed:16857013). Both narrow and wide pili are glycosylated
CC (PubMed:32376942). {ECO:0000269|PubMed:16857013,
CC ECO:0000269|PubMed:32376942}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutants show defect in both DNA
CC transformation and twitching motility. {ECO:0000269|PubMed:12839734,
CC ECO:0000269|PubMed:32376942}.
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DR EMBL; AE017221; AAS81202.1; -; Genomic_DNA.
DR PDB; 6XXD; EM; 3.22 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=7-131.
DR PDBsum; 6XXD; -.
DR AlphaFoldDB; Q72JC0; -.
DR SMR; Q72JC0; -.
DR STRING; 262724.TT_C0858; -.
DR EnsemblBacteria; AAS81202; AAS81202; TT_C0858.
DR KEGG; tth:TT_C0858; -.
DR eggNOG; COG2165; Bacteria.
DR HOGENOM; CLU_091705_7_4_0; -.
DR OMA; CAVARHD; -.
DR Proteomes; UP000000592; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015627; C:type II protein secretion system complex; IEA:InterPro.
DR GO; GO:0015628; P:protein secretion by the type II secretion system; IEA:InterPro.
DR InterPro; IPR000983; Bac_GSPG_pilin.
DR InterPro; IPR012902; N_methyl_site.
DR InterPro; IPR045584; Pilin-like.
DR Pfam; PF07963; N_methyl; 1.
DR PRINTS; PR00813; BCTERIALGSPG.
DR SUPFAM; SSF54523; SSF54523; 1.
DR TIGRFAMs; TIGR02532; IV_pilin_GFxxxE; 1.
DR PROSITE; PS00409; PROKAR_NTER_METHYL; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Cell outer membrane;
KW Disulfide bond; Glycoprotein; Membrane; Methylation; Periplasm;
KW Transmembrane; Transmembrane helix.
FT PROPEP 1..6
FT /note="Leader sequence"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01070,
FT ECO:0000305"
FT /id="PRO_0000450706"
FT CHAIN 7..131
FT /note="Type IV wide pilus major component PilA4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01070"
FT /id="PRO_0000450707"
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 DISULFID 95..130
FT /evidence="ECO:0000269|PubMed:32376942"
FT HELIX 9..25
FT /evidence="ECO:0007829|PDB:6XXD"
FT HELIX 30..60
FT /evidence="ECO:0007829|PDB:6XXD"
FT HELIX 67..73
FT /evidence="ECO:0007829|PDB:6XXD"
FT STRAND 85..88
FT /evidence="ECO:0007829|PDB:6XXD"
FT STRAND 95..98
FT /evidence="ECO:0007829|PDB:6XXD"
FT STRAND 103..110
FT /evidence="ECO:0007829|PDB:6XXD"
FT TURN 111..113
FT /evidence="ECO:0007829|PDB:6XXD"
FT STRAND 114..124
FT /evidence="ECO:0007829|PDB:6XXD"
SQ SEQUENCE 131 AA; 13901 MW; A7F64A5E07A3FFA4 CRC64;
MRNAKGFTLI ELLIVIAIIA ILAAVLIPNL LAARKRANDT VVTAYLNDAV KFQEMYQIDN
NSYTSNQAAL ISLGLKSTPA NVTFSIVSAS ANSYCMIAGH SGGTVWFAAT PDKGVYKTNT
AVTSSQPESC P
