ID   COMGC_BACSU             Reviewed;          98 AA.
AC   P25955;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   03-AUG-2022, entry version 132.
DE   RecName: Full=ComG operon protein 3;
DE   Flags: Precursor;
GN   Name=comGC; Synonyms=comG3; OrderedLocusNames=BSU24710;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2507524; DOI=10.1128/jb.171.10.5386-5404.1989;
RA   Albano M., Breitling R., Dubnau D.A.;
RT   "Nucleotide sequence and genetic organization of the Bacillus subtilis comG
RT   operon.";
RL   J. Bacteriol. 171:5386-5404(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / JH642;
RX   PubMed=8969508; DOI=10.1099/13500872-142-11-3103;
RA   Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M.,
RA   Kobayashi Y.;
RT   "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the
RT   Bacillus subtilis genome containing the skin element and many sporulation
RT   genes.";
RL   Microbiology 142:3103-3111(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [4]
RP   CHARACTERIZATION.
RX   PubMed=1968455; DOI=10.1128/jb.172.3.1499-1508.1990;
RA   Breitling R., Dubnau D.A.;
RT   "A membrane protein with similarity to N-methylphenylalanine pilins is
RT   essential for DNA binding by competent Bacillus subtilis.";
RL   J. Bacteriol. 172:1499-1508(1990).
RN   [5]
RP   FUNCTION.
RX   PubMed=9422590; DOI=10.1128/jb.180.1.41-45.1998;
RA   Chung Y.S., Dubnau D.A.;
RT   "All seven comG open reading frames are required for DNA binding during
RT   transformation of competent Bacillus subtilis.";
RL   J. Bacteriol. 180:41-45(1998).
RN   [6]
RP   SUBCELLULAR LOCATION, AND DISULFIDE BOND.
RC   STRAIN=168;
RX   PubMed=9723928; DOI=10.1046/j.1365-2958.1998.00989.x;
RA   Chung Y.S., Breidt F., Dubnau D.A.;
RT   "Cell surface localization and processing of the ComG proteins, required
RT   for DNA binding during transformation of Bacillus subtilis.";
RL   Mol. Microbiol. 29:905-913(1998).
RN   [7]
RP   REQUIREMENT FOR BDBDC OPERON FOR COMGC PRODUCTION.
RC   STRAIN=168;
RX   PubMed=11744713; DOI=10.1074/jbc.m111380200;
RA   Meima R., Eschevins C., Fillinger S., Bolhuis A., Hamoen L.W., Dorenbos R.,
RA   Quax W.J., van Dijl J.M., Provvedi R., Chen I., Dubnau D., Bron S.;
RT   "The bdbDC operon of Bacillus subtilis encodes thiol-disulfide
RT   oxidoreductases required for competence development.";
RL   J. Biol. Chem. 277:6994-7001(2002).
CC   -!- FUNCTION: Required for transformation and DNA binding.
CC       {ECO:0000269|PubMed:9422590}.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9723928};
CC       Single-pass membrane protein {ECO:0000269|PubMed:9723928}. Cell surface
CC       {ECO:0000269|PubMed:9723928}. Note=The unprocessed form is an integral
CC       membrane protein with its C-terminus outside the membrane. Upon
CC       cleavage, it is translocated to the outer face of the membrane.
CC   -!- PTM: Processing of ComGC in competent cells requires ComC, while
CC       stabilization, possibly by formation of a disulfide bond, requires BdbC
CC       and BdbD.
CC   -!- SIMILARITY: Belongs to the ComGC family. {ECO:0000305}.
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DR   EMBL; M29691; AAA83369.1; -; Genomic_DNA.
DR   EMBL; D84432; BAA12535.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14402.1; -; Genomic_DNA.
DR   PIR; D30338; D30338.
DR   RefSeq; NP_390351.1; NC_000964.3.
DR   RefSeq; WP_003230162.1; NZ_JNCM01000036.1.
DR   AlphaFoldDB; P25955; -.
DR   SMR; P25955; -.
DR   STRING; 224308.BSU24710; -.
DR   PaxDb; P25955; -.
DR   PRIDE; P25955; -.
DR   EnsemblBacteria; CAB14402; CAB14402; BSU_24710.
DR   GeneID; 938526; -.
DR   KEGG; bsu:BSU24710; -.
DR   PATRIC; fig|224308.179.peg.2689; -.
DR   eggNOG; COG4537; Bacteria.
DR   OMA; PNVTKHN; -.
DR   PhylomeDB; P25955; -.
DR   BioCyc; BSUB:BSU24710-MON; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
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:0030420; P:establishment of competence for transformation; IEA:UniProtKB-KW.
DR   InterPro; IPR016940; ComGC.
DR   InterPro; IPR012902; N_methyl_site.
DR   InterPro; IPR045584; Pilin-like.
DR   Pfam; PF07963; N_methyl; 1.
DR   PIRSF; PIRSF029928; Late_competence_ComGC; 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   Cell membrane; Competence; Disulfide bond; Membrane; Methylation;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT   PROPEP          1..5
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000024266"
FT   CHAIN           6..98
FT                   /note="ComG operon protein 3"
FT                   /id="PRO_0000024267"
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   DISULFID        41..81
FT                   /evidence="ECO:0000305|PubMed:9723928"
SQ   SEQUENCE   98 AA;  10850 MW;  17B8152CAFE2E4C9 CRC64;
     MNEKGFTLVE MLIVLFIISI LLLITIPNVT KHNQTIQKKG CEGLQNMVKA QMTAFELDHE
     GQTPSLADLQ SEGYVKKDAV CPNGKRIIIT GGEVKVEH