PILA5_THET2
ID PILA5_THET2 Reviewed; 116 AA.
AC Q72GL2;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 80.
DE RecName: Full=Type IV narrow pilus major component PilA5 {ECO:0000303|PubMed:32376942};
DE AltName: Full=Type IV major pilin PilA5;
DE Flags: Precursor;
GN Name=pilA5; OrderedLocusNames=TT_C1836;
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] {ECO:0007744|PDB:6XXE}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.49 ANGSTROMS) FUNCTION, DISRUPTION
RP PHENOTYPE, AND GLYCOSYLATION.
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 forming the main structure of the
CC narrow T4P pili that participates in twitching motility.
CC {ECO:0000269|PubMed:32376942}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:Q72JC0}; Single-pass membrane protein
CC {ECO:0000255}. Cell outer membrane {ECO:0000250|UniProtKB:Q72JC0};
CC Single-pass membrane protein {ECO:0000255}. Periplasm
CC {ECO:0000250|UniProtKB:Q72JC0}. Note=The single N-terminal
CC transmembrane is initially involved in the correct localization to the
CC inner membrane. Once the leader sequence cleaved, this region plays a
CC role in multimerization and protein-protein interactions in the
CC periplasm and the outer membrane. {ECO:0000250|UniProtKB:Q72JC0}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:32376942}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutants show a defect in twitching
CC motility while DNA uptake seems not affected.
CC {ECO:0000269|PubMed:32376942}.
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DR EMBL; AE017221; AAS82178.1; -; Genomic_DNA.
DR RefSeq; WP_011174191.1; NC_005835.1.
DR PDB; 6XXE; EM; 3.49 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=6-116.
DR PDBsum; 6XXE; -.
DR AlphaFoldDB; Q72GL2; -.
DR SMR; Q72GL2; -.
DR STRING; 262724.TT_C1836; -.
DR EnsemblBacteria; AAS82178; AAS82178; TT_C1836.
DR KEGG; tth:TT_C1836; -.
DR eggNOG; COG2165; Bacteria.
DR HOGENOM; CLU_091705_7_3_0; -.
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 InterPro; IPR012902; N_methyl_site.
DR InterPro; IPR045584; Pilin-like.
DR Pfam; PF07963; N_methyl; 1.
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 Membrane; Methylation; Periplasm; Transmembrane; Transmembrane helix.
FT PROPEP 1..5
FT /note="Leader sequence"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01070,
FT ECO:0000305"
FT /id="PRO_0000450708"
FT CHAIN 6..116
FT /note="Type IV narrow pilus major component PilA5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01070"
FT /id="PRO_0000450709"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 6
FT /note="N-methylphenylalanine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01070"
FT HELIX 8..21
FT /evidence="ECO:0007829|PDB:6XXE"
FT HELIX 33..59
FT /evidence="ECO:0007829|PDB:6XXE"
FT HELIX 65..69
FT /evidence="ECO:0007829|PDB:6XXE"
FT STRAND 71..75
FT /evidence="ECO:0007829|PDB:6XXE"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:6XXE"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:6XXE"
FT TURN 95..97
FT /evidence="ECO:0007829|PDB:6XXE"
FT STRAND 100..106
FT /evidence="ECO:0007829|PDB:6XXE"
FT STRAND 108..111
FT /evidence="ECO:0007829|PDB:6XXE"
SQ SEQUENCE 116 AA; 11964 MW; A3BD240CEF947971 CRC64;
MRAKGFTLIE LAIVIVIIGI LVAIAVPRFV DLTDQANQAN VDATAAAVRS AYAIATVQAK
GIPTCDQVFA NPEGGSTSGS TWTSSDNSTT VSCNASADTF TISRGGKTRT LNLTVN
