ID   PILC_MYXXD              Reviewed;         417 AA.
AC   Q1D0A0;
DT   17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Type IV pilus assembly protein PilC;
GN   Name=pilC; OrderedLocusNames=MXAN_5786;
OS   Myxococcus xanthus (strain DK1622).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Myxococcaceae; Myxococcus.
OX   NCBI_TaxID=246197;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DK1622;
RX   PubMed=17015832; DOI=10.1073/pnas.0607335103;
RA   Goldman B.S., Nierman W.C., Kaiser D., Slater S.C., Durkin A.S., Eisen J.,
RA   Ronning C.M., Barbazuk W.B., Blanchard M., Field C., Halling C., Hinkle G.,
RA   Iartchuk O., Kim H.S., Mackenzie C., Madupu R., Miller N., Shvartsbeyn A.,
RA   Sullivan S.A., Vaudin M., Wiegand R., Kaplan H.B.;
RT   "Evolution of sensory complexity recorded in a myxobacterial genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15200-15205(2006).
RN   [2]
RP   FUNCTION, INTERACTION WITH PILB, AND SUBCELLULAR LOCATION.
RC   STRAIN=DK1622;
RX   PubMed=26851283; DOI=10.1074/jbc.m115.701284;
RA   Bischof L.F., Friedrich C., Harms A., Soegaard-Andersen L.,
RA   van der Does C.;
RT   "The Type IV Pilus assembly ATPase PilB of Myxococcus xanthus interacts
RT   with the inner membrane platform protein PilC and the nucleotide-binding
RT   protein PilM.";
RL   J. Biol. Chem. 291:6946-6957(2016).
RN   [3] {ECO:0007744|PDB:3JC8, ECO:0007744|PDB:3JC9}
RP   STRUCTURE BY NMR, AND DISRUPTION PHENOTYPE.
RX   PubMed=26965631; DOI=10.1126/science.aad2001;
RA   Chang Y.W., Rettberg L.A., Treuner-Lange A., Iwasa J., Sogaard-Andersen L.,
RA   Jensen G.J.;
RT   "Architecture of the type IVa pilus machine.";
RL   Science 351:aad2001-aad2001(2016).
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 (By similarity). Controls both pilus assembly
CC       and disassembly and plays an important role in PilB localization to the
CC       complex and ATPase activity (PubMed:26851283).
CC       {ECO:0000250|UniProtKB:P22609, ECO:0000269|PubMed:26851283}.
CC   -!- SUBUNIT: Homotetramer (By similarity). Interacts with PilB
CC       (PubMed:26851283). {ECO:0000250|UniProtKB:Q5SK58,
CC       ECO:0000269|PubMed:26851283}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000269|PubMed:26851283}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P22609}.
CC   -!- DISRUPTION PHENOTYPE: Deletion mutant show missing type IV cytoplasmic
CC       dome and disc but the cytoplasmic ring is still present.
CC       {ECO:0000269|PubMed:26965631}.
CC   -!- SIMILARITY: Belongs to the GSP F family.
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DR   EMBL; CP000113; ABF92576.1; -; Genomic_DNA.
DR   RefSeq; WP_011555737.1; NC_008095.1.
DR   PDB; 3JC8; EM; -; Ca/Cb=1-417.
DR   PDB; 3JC9; EM; -; Ca/Cb=1-417.
DR   PDBsum; 3JC8; -.
DR   PDBsum; 3JC9; -.
DR   AlphaFoldDB; Q1D0A0; -.
DR   SMR; Q1D0A0; -.
DR   STRING; 246197.MXAN_5786; -.
DR   EnsemblBacteria; ABF92576; ABF92576; MXAN_5786.
DR   GeneID; 41363029; -.
DR   KEGG; mxa:MXAN_5786; -.
DR   eggNOG; COG1459; Bacteria.
DR   HOGENOM; CLU_035032_2_1_7; -.
DR   OMA; TRQMATM; -.
DR   OrthoDB; 1268170at2; -.
DR   Proteomes; UP000002402; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   Gene3D; 1.20.81.30; -; 2.
DR   InterPro; IPR003004; GspF/PilC.
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.
PE   1: Evidence at protein level;
KW   3D-structure; Cell inner membrane; Cell membrane; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..417
FT                   /note="Type IV pilus assembly protein PilC"
FT                   /id="PRO_0000450274"
FT   TRANSMEM        141..161
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        182..202
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        235..255
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        390..410
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   417 AA;  45142 MW;  EC2255D134E5FE6E CRC64;
     MAAPAVKSAS TPKKATAQFL WEAKTKSGES KKGEMEAMDV EAVNARLKSL GLNPVKVRKK
     SMLDGDITIP GFGGVEGKDI LVFTRQFATM IDAGLPLVQC LDILASQMDN PSFKKVLFAI
     KSKVEQGSTF ADALKEHPKV FDELYVQLCA AGEVGGILDA ILNRLAAYRE KNEKLKSKVK
     SAMTYPIIVI LVAIGVTAVL LLKVTPVFEK MFADFGSELP GPTQMIVNFS HMAQEYFFHV
     AGSIVAVVMS FTWSYRQPRG RKFWDKVFLF MPVFGPVLRK VAVARFTRTL GTMISSGVPI
     LDALDVTAKT AGNRTVEDAI IYVRGKIAEG KNIAGPLAET KVFPSMVVQM IGVGEATGAM
     DTMLNKIADF YDDEVDAAIN SLTAMIEPVL MVFLGGVVGG FLIGMYLPIF SLAGAIQ