COMGG_BACSU
ID COMGG_BACSU Reviewed; 124 AA.
AC P25959;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=ComG operon protein 7;
DE Flags: Precursor;
GN Name=comGG; Synonyms=comG7; OrderedLocusNames=BSU24670;
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; 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 [5]
RP SUBCELLULAR LOCATION, AND PROBABLE DISULFIDE BOND.
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 -!- SUBUNIT: Homodimer; disulfide-linked. A minor fraction of ComGG is
CC found as a disulfide-bonded homodimer.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9723928};
CC Peripheral membrane protein {ECO:0000269|PubMed:9723928}. Cell membrane
CC {ECO:0000269|PubMed:9723928}; Peptidoglycan-anchor
CC {ECO:0000269|PubMed:9723928}. Secreted {ECO:0000269|PubMed:9723928}.
CC Note=About half of pre-ComGG is present as a peripheral membrane
CC protein and the other half as an integral protein. Upon (partial)
CC processing ComGG is translocated to a position outside the membrane.
CC -!- PTM: Partial processing of ComGG in competent cells requires ComC.
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DR EMBL; M29691; AAA83373.1; -; Genomic_DNA.
DR EMBL; D84432; BAA12538.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14398.1; -; Genomic_DNA.
DR PIR; H30338; H30338.
DR RefSeq; NP_390347.1; NC_000964.3.
DR RefSeq; WP_003230170.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; P25959; -.
DR STRING; 224308.BSU24670; -.
DR PaxDb; P25959; -.
DR PRIDE; P25959; -.
DR DNASU; 938538; -.
DR EnsemblBacteria; CAB14398; CAB14398; BSU_24670.
DR GeneID; 938538; -.
DR KEGG; bsu:BSU24670; -.
DR PATRIC; fig|224308.179.peg.2685; -.
DR OMA; ISRCMFE; -.
DR BioCyc; BSUB:BSU24670-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; IPR020372; Competence_ComGG.
DR Pfam; PF14173; ComGG; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Competence; Disulfide bond; Membrane; Peptidoglycan-anchor;
KW Reference proteome; Secreted; Signal; Transport.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..124
FT /note="ComG operon protein 7"
FT /id="PRO_0000020970"
FT DISULFID 34
FT /note="Interchain"
FT /evidence="ECO:0000305"
SQ SEQUENCE 124 AA; 14540 MW; B3968089A6049421 CRC64;
MYRTRGFIYP AVLFVSALVL LIVNFVAAQY ISRCMFEKET KELYIGENLL QNGVLLSIRH
VLEERKGQEG TQQFLYGRVS YYIHDTSIKE QKEINLRVST DSGTERTAQI VFDQKQKKLL
RWTE
