ID   PILA3_THET2             Reviewed;         233 AA.
AC   Q72JC2;
DT   12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=Pilin-like protein PilA3 {ECO:0000303|PubMed:12839734};
DE   Flags: Precursor;
GN   Name=pilA3; OrderedLocusNames=TT_C0856;
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).
CC   -!- FUNCTION: Plays an essential role in natural DNA transformation but is
CC       not required for pilus biogenesis. {ECO:0000269|PubMed:12839734}.
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   -!- DISRUPTION PHENOTYPE: Mutants have a wild-type piliation phenotype but
CC       are deficient in transformation. {ECO:0000269|PubMed:12839734}.
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DR   EMBL; AE017221; AAS81200.1; -; Genomic_DNA.
DR   RefSeq; WP_011173285.1; NC_005835.1.
DR   AlphaFoldDB; Q72JC2; -.
DR   SMR; Q72JC2; -.
DR   STRING; 262724.TT_C0856; -.
DR   EnsemblBacteria; AAS81200; AAS81200; TT_C0856.
DR   KEGG; tth:TT_C0856; -.
DR   eggNOG; COG4966; Bacteria.
DR   HOGENOM; CLU_1204321_0_0_0; -.
DR   OMA; AGARYWN; -.
DR   OrthoDB; 1300736at2; -.
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   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Cell outer membrane; Membrane;
KW   Methylation; Periplasm; Transmembrane; Transmembrane helix.
FT   PROPEP          1..4
FT                   /note="Leader sequence"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01070,
FT                   ECO:0000305"
FT                   /id="PRO_0000450704"
FT   CHAIN           5..233
FT                   /note="Pilin-like protein PilA3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01070"
FT                   /id="PRO_0000450705"
FT   TRANSMEM        5..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          121..143
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        124..143
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         5
FT                   /note="N-methylphenylalanine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01070"
SQ   SEQUENCE   233 AA;  24977 MW;  4A14684693730A8D CRC64;
     MKRGFTLVEV LVAMAILVVV LAVGVRYFAS TSELARNTQA RSELQDRVRM VMQVVTADLQ
     MAGARYWNSG NQNQAFSLPL PPLSGSNMGP KDTLTLYYVT SLRDLASACR RVDYGFEGDT
     LRRSDVNATP SSGSDCTTPP PNSQPLAEGM LALDIQYQCS DGSRKDTPDC GTDAYPRSAK
     VTVAGYSLTS VTNPGPASLT TVTGKTLACP QGRACYALTQ EVLMPNLKPL PTP