ID   COMGC_ALKHC             Reviewed;         102 AA.
AC   Q9K923;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=ComG operon protein 3 homolog;
DE   Flags: Precursor;
GN   Name=comGC; OrderedLocusNames=BH2827;
OS   Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS   / JCM 9153 / C-125) (Bacillus halodurans).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX   NCBI_TaxID=272558;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX   PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA   Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA   Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT   "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT   and genomic sequence comparison with Bacillus subtilis.";
RL   Nucleic Acids Res. 28:4317-4331(2000).
CC   -!- FUNCTION: Required for transformation and DNA binding. {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein. Cell
CC       surface. Note=The unprocessed form is an integral membrane protein with
CC       its C-terminus outside the membrane. Upon cleavage, it is translocated
CC       to the outer face of the membrane (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ComGC family. {ECO:0000305}.
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DR   EMBL; BA000004; BAB06546.1; -; Genomic_DNA.
DR   PIR; C84003; C84003.
DR   RefSeq; WP_010898975.1; NC_002570.2.
DR   AlphaFoldDB; Q9K923; -.
DR   SMR; Q9K923; -.
DR   STRING; 272558.10175448; -.
DR   EnsemblBacteria; BAB06546; BAB06546; BAB06546.
DR   KEGG; bha:BH2827; -.
DR   eggNOG; COG4537; Bacteria.
DR   HOGENOM; CLU_091705_9_0_9; -.
DR   OMA; PNVTKHN; -.
DR   OrthoDB; 2044924at2; -.
DR   Proteomes; UP000001258; 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:0015627; C:type II protein secretion system complex; IEA:InterPro.
DR   GO; GO:0030420; P:establishment of competence for transformation; IEA:UniProtKB-KW.
DR   GO; GO:0015628; P:protein secretion by the type II secretion system; IEA:InterPro.
DR   InterPro; IPR000983; Bac_GSPG_pilin.
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   PRINTS; PR00813; BCTERIALGSPG.
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 membrane; Competence; Disulfide bond; Membrane; Methylation;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT   PROPEP          1..10
FT                   /note="Leader sequence"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01070"
FT                   /id="PRO_0000024262"
FT   CHAIN           11..102
FT                   /note="ComG operon protein 3 homolog"
FT                   /id="PRO_0000024263"
FT   TRANSMEM        11..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         11
FT                   /note="N-methylphenylalanine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01070"
FT   DISULFID        46..85
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   102 AA;  11368 MW;  3C4BD89B08564A43 CRC64;
     MKKPFHHQAG FTLVEMMIVL MIISILLLVA LPSMTKNNEV AGDKGCEATV KLLQTQVHAY
     EIDHDRLPTN LDALKREGYV EHTECPNGKK LTLRNGVVAI SE