PILA2_THET2
ID PILA2_THET2 Reviewed; 193 AA.
AC Q72JC3;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 75.
DE RecName: Full=Pilin-like protein PilA2 {ECO:0000303|PubMed:12839734};
DE Flags: Precursor;
GN Name=pilA2; OrderedLocusNames=TT_C0855;
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; AAS81199.1; -; Genomic_DNA.
DR RefSeq; WP_011173284.1; NC_005835.1.
DR AlphaFoldDB; Q72JC3; -.
DR SMR; Q72JC3; -.
DR STRING; 262724.TT_C0855; -.
DR EnsemblBacteria; AAS81199; AAS81199; TT_C0855.
DR KEGG; tth:TT_C0855; -.
DR eggNOG; COG2165; Bacteria.
DR HOGENOM; CLU_1460655_0_0_0; -.
DR OMA; RRVTCYD; -.
DR OrthoDB; 1820074at2; -.
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_0000450702"
FT CHAIN 5..193
FT /note="Pilin-like protein PilA2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01070"
FT /id="PRO_0000450703"
FT TRANSMEM 5..25
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 5
FT /note="N-methylleucine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01070"
SQ SEQUENCE 193 AA; 20564 MW; 2168844349136912 CRC64;
MRKGLTLVEV LVTLVIMGIA FAALLTSQLA NLRASAQARF ATDAKAAAVQ VLERRSAEVL
KSEIVPALSP YKDAPLDPDN PSGNWRSFYF VDYYFSCPTR VAPSPKQRGG SVANLRPGLT
CSGTETIFGI PVAWDIRGEN GILGEGVVTV VVTATHPRGP KVTLGRRVTC YDVYPSPTQD
QPAPCPPPGG GRP
