(data stored in SCRATCH zone)

SWISSPROT: COMGD_BACSU

ID   COMGD_BACSU             Reviewed;         143 AA.
AC   P25956;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   11-DEC-2019, entry version 113.
DE   RecName: Full=ComG operon protein 4;
DE   Flags: Precursor;
GN   Name=comGD; Synonyms=comG4; OrderedLocusNames=BSU24700;
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   FUNCTION.
RX   PubMed=9422590;
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   [5]
RP   SUBCELLULAR LOCATION.
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).
CC   -!- FUNCTION: Required for transformation and DNA binding.
CC       {ECO:0000269|PubMed:9422590}.
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. Upon cleavage, it is translocated to the outer face
CC       of the membrane.
CC   -!- PTM: Processing of ComGD in competent cells requires ComC.
DR   EMBL; M29691; AAA83370.1; -; Genomic_DNA.
DR   EMBL; D84432; BAA12536.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14401.1; -; Genomic_DNA.
DR   PIR; E30338; E30338.
DR   RefSeq; NP_390350.1; NC_000964.3.
DR   RefSeq; WP_004398628.1; NZ_JNCM01000036.1.
DR   SMR; P25956; -.
DR   STRING; 224308.BSU24700; -.
DR   PaxDb; P25956; -.
DR   PRIDE; P25956; -.
DR   EnsemblBacteria; CAB14401; CAB14401; BSU24700.
DR   GeneID; 938531; -.
DR   KEGG; bsu:BSU24700; -.
DR   PATRIC; fig|224308.179.peg.2688; -.
DR   eggNOG; COG2165; LUCA.
DR   HOGENOM; HOG000262062; -.
DR   KO; K02246; -.
DR   OMA; EFNEKGH; -.
DR   BioCyc; BSUB:BSU24700-MONOMER; -.
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: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; IPR016785; ComGD.
DR   InterPro; IPR012902; N_methyl_site.
DR   InterPro; IPR002416; T2SS_protein-H.
DR   Pfam; PF07963; N_methyl; 1.
DR   PIRSF; PIRSF021292; Competence_ComGD; 1.
DR   PRINTS; PR00885; BCTERIALGSPH.
DR   TIGRFAMs; TIGR02532; IV_pilin_GFxxxE; 1.
DR   PROSITE; PS00409; PROKAR_NTER_METHYL; 1.
PE   3: Inferred from homology;
DR   PRODOM; P25956.
DR   SWISS-2DPAGE; P25956.
KW   Cell membrane; Competence; Membrane; Methylation; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport.
FT   PROPEP          1..10
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000024268"
FT   CHAIN           11..143
FT                   /note="ComG operon protein 4"
FT                   /id="PRO_0000024269"
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"
SQ   SEQUENCE   143 AA;  16009 MW;  8E9D2928EC4DA3D2 CRC64;
     MNIKLNEEKG FTLLESLLVL SLASILLVAV FTTLPPAYDN TAVRQAASQL KNDIMLTQQT
     AISRQQRTKI LFHKKEYQLV IGDTVIERPY ATGLSIELLT LKDRLEFNEK GHPNAGGKIR
     VKGHAVYDIT VYLGSGRVNV ERK
//

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