ID   PILC_THET8              Reviewed;         406 AA.
AC   Q5SK58;
DT   17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 100.
DE   RecName: Full=Type IV pilus assembly protein PilC;
GN   OrderedLocusNames=TTHA0794;
OS   Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX   NCBI_TaxID=300852;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27634 / DSM 579 / HB8;
RA   Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA   Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT   "Complete genome sequence of Thermus thermophilus HB8.";
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0007744|PDB:2WHN}
RP   X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 53-168, AND SUBUNIT.
RX   PubMed=20455262; DOI=10.1002/prot.22720;
RA   Karuppiah V., Hassan D., Saleem M., Derrick J.P.;
RT   "Structure and oligomerization of the PilC type IV pilus biogenesis protein
RT   from Thermus thermophilus.";
RL   Proteins 78:2049-2057(2010).
CC   -!- FUNCTION: Essential inner membrane component of the type IV pilus (T4P)
CC       that plays a role in surface and host cell adhesion, colonization,
CC       biofilm maturation, virulence, and twitching, a form of surface-
CC       associated motility facilitated by cycles of extension, adhesion, and
CC       retraction of T4P fibers. Controls both pilus assembly and disassembly
CC       and plays an important role in PilB localization to the complex and
CC       ATPase activity. {ECO:0000250|UniProtKB:P22609}.
CC   -!- SUBUNIT: Homotetramer (PubMed:20455262). Interacts with PilB (By
CC       similarity). {ECO:0000250|UniProtKB:P22609,
CC       ECO:0000269|PubMed:20455262}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000250|UniProtKB:P22609}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P22609}.
CC   -!- SIMILARITY: Belongs to the GSP F family.
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DR   EMBL; AP008226; BAD70617.1; -; Genomic_DNA.
DR   RefSeq; WP_011228203.1; NC_006461.1.
DR   RefSeq; YP_144060.1; NC_006461.1.
DR   PDB; 2WHN; X-ray; 2.05 A; A/B=53-168.
DR   PDBsum; 2WHN; -.
DR   AlphaFoldDB; Q5SK58; -.
DR   SMR; Q5SK58; -.
DR   STRING; 300852.55772176; -.
DR   EnsemblBacteria; BAD70617; BAD70617; BAD70617.
DR   GeneID; 3168277; -.
DR   KEGG; ttj:TTHA0794; -.
DR   PATRIC; fig|300852.9.peg.787; -.
DR   eggNOG; COG1459; Bacteria.
DR   HOGENOM; CLU_035032_2_1_0; -.
DR   OMA; VAEQCEK; -.
DR   PhylomeDB; Q5SK58; -.
DR   Proteomes; UP000000532; 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:0009306; P:protein secretion; IEA:InterPro.
DR   Gene3D; 1.20.81.30; -; 2.
DR   InterPro; IPR003004; GspF/PilC.
DR   InterPro; IPR001992; T2SS_GspF/T4SS_PilC_CS.
DR   InterPro; IPR018076; T2SS_GspF_dom.
DR   InterPro; IPR042094; T2SS_GspF_sf.
DR   PANTHER; PTHR30012; PTHR30012; 1.
DR   Pfam; PF00482; T2SSF; 2.
DR   PRINTS; PR00812; BCTERIALGSPF.
DR   PROSITE; PS00874; T2SP_F; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell inner membrane; Cell membrane; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..406
FT                   /note="Type IV pilus assembly protein PilC"
FT                   /id="PRO_0000450275"
FT   TRANSMEM        69..91
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        171..191
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        211..231
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        377..397
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   HELIX           55..58
FT                   /evidence="ECO:0007829|PDB:2WHN"
FT   HELIX           64..80
FT                   /evidence="ECO:0007829|PDB:2WHN"
FT   HELIX           84..91
FT                   /evidence="ECO:0007829|PDB:2WHN"
FT   HELIX           98..112
FT                   /evidence="ECO:0007829|PDB:2WHN"
FT   HELIX           117..122
FT                   /evidence="ECO:0007829|PDB:2WHN"
FT   HELIX           129..141
FT                   /evidence="ECO:0007829|PDB:2WHN"
FT   HELIX           144..161
FT                   /evidence="ECO:0007829|PDB:2WHN"
SQ   SEQUENCE   406 AA;  44688 MW;  B3AAAEE4203F6D87 CRC64;
     MPVYQYKARD RQGRLVEATI EAEDLRTAAR LLRDRGLFVA EIKEPGKGLQ AEVRIPALER
     GPGLKDLAIF SRQLATMLGA GLTLLQALAI LERQTENRKF REILKQVRTD VEGGMAFSEA
     LSKHKIFSRL YVNLVRAGET SGGLDLILDR LASFLEKELE LRGKIRSAMT YPVIVFVFAV
     GVAYFLLTGI VPQFAQILTD LGSELPLLTR FLIAVSDLLR AATLPLLLLA VALFFAYRWY
     YGTPQGRRVI DRLKLRLPVF GNLNRKTAVA RFSRTLALLL SSGVNIVEAL DITKGTAGNS
     VVEEIVEAAK LKIQQGDPLN LTLAQHPFVF PPMVSSMVAI GEETGALDTM LSKVADFYER
     EVDEAVASLT AAIEPLMIIF LGVIVGMIVA GMFLPLFKII GTLSVQ