COMGA_BACSU
ID COMGA_BACSU Reviewed; 356 AA.
AC P25953;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=ComG operon protein 1;
GN Name=comGA; Synonyms=comG1; OrderedLocusNames=BSU24730;
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.
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 [6]
RP DEVELOPMENTAL STAGE, AND INDUCTION.
RC STRAIN=168;
RX PubMed=11918817; DOI=10.1046/j.1365-2958.2002.02833.x;
RA Berka R.M., Hahn J., Albano M., Draskovic I., Persuh M., Cui X., Sloma A.,
RA Widner W., Dubnau D.;
RT "Microarray analysis of the Bacillus subtilis K-state: genome-wide
RT expression changes dependent on ComK.";
RL Mol. Microbiol. 43:1331-1345(2002).
RN [7]
RP INDUCTION.
RC STRAIN=168 / CU741;
RX PubMed=11948146; DOI=10.1128/jb.184.9.2344-2351.2002;
RA Ogura M., Yamaguchi H., Kobayashi K., Ogasawara N., Fujita Y., Tanaka T.;
RT "Whole-genome analysis of genes regulated by the Bacillus subtilis
RT competence transcription factor ComK.";
RL J. Bacteriol. 184:2344-2351(2002).
RN [8]
RP SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, INDUCTION, DISRUPTION PHENOTYPE,
RP AND MUTAGENESIS OF LYS-150.
RC STRAIN=168;
RX PubMed=16009133; DOI=10.1016/j.cell.2005.04.035;
RA Hahn J., Maier B., Haijema B.J., Sheetz M., Dubnau D.;
RT "Transformation proteins and DNA uptake localize to the cell poles in
RT Bacillus subtilis.";
RL Cell 122:59-71(2005).
RN [9]
RP SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RC STRAIN=168;
RX PubMed=17630974; DOI=10.1111/j.1365-2958.2007.05799.x;
RA Kramer N., Hahn J., Dubnau D.;
RT "Multiple interactions among the competence proteins of Bacillus
RT subtilis.";
RL Mol. Microbiol. 65:454-464(2007).
CC -!- FUNCTION: Required for uptake of DNA by competent cells.
CC {ECO:0000269|PubMed:9422590}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9723928};
CC Peripheral membrane protein {ECO:0000269|PubMed:9723928}; Cytoplasmic
CC side {ECO:0000269|PubMed:9723928}. Note=Localizes mostly to the cell
CC poles during the development of competence, this depends on comK.
CC During competence a number of proteins (at least CoiA, ComFA, ComGA,
CC DprA, RecA and SsbB) are thought to colocalize at the cell pole, when
CC comFA is disrupted ComGA no longer accumulates (PubMed:16009133).
CC Colocalizes with CoiA and DprA (PubMed:17630974). During development of
CC competence ComGA and SsbB colocalize in discrete foci which accumulate
CC at the cell poles and then delocalize without the overall levels of
CC proteins decreasing, these processes are coincident with the timing of
CC transformability and the site of DNA uptake (PubMed:16009133).
CC {ECO:0000269|PubMed:16009133, ECO:0000269|PubMed:17630974}.
CC -!- DEVELOPMENTAL STAGE: Expressed in cells competent for DNA
CC transformation; that is 5-15% of the population (PubMed:11918817,
CC PubMed:16009133, PubMed:17630974). {ECO:0000269|PubMed:11918817,
CC ECO:0000269|PubMed:16009133, ECO:0000269|PubMed:17630974}.
CC -!- INDUCTION: Expression activated by ComK (PubMed:11918817,
CC PubMed:11948146). {ECO:0000269|PubMed:11918817,
CC ECO:0000269|PubMed:11948146}.
CC -!- DISRUPTION PHENOTYPE: Transformation deficient (PubMed:16009133).
CC {ECO:0000269|PubMed:16009133}.
CC -!- SIMILARITY: Belongs to the GSP E family. {ECO:0000305}.
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DR EMBL; M29691; AAA83367.1; -; Genomic_DNA.
DR EMBL; D84432; BAA12533.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14404.1; -; Genomic_DNA.
DR PIR; B30338; B30338.
DR RefSeq; NP_390353.1; NC_000964.3.
DR RefSeq; WP_004399124.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; P25953; -.
DR SMR; P25953; -.
DR STRING; 224308.BSU24730; -.
DR TCDB; 3.A.14.1.1; the fimbrilin/protein exporter (fpe) family.
DR PaxDb; P25953; -.
DR PRIDE; P25953; -.
DR EnsemblBacteria; CAB14404; CAB14404; BSU_24730.
DR GeneID; 938516; -.
DR KEGG; bsu:BSU24730; -.
DR PATRIC; fig|224308.179.peg.2691; -.
DR eggNOG; COG2804; Bacteria.
DR InParanoid; P25953; -.
DR OMA; AKGAIYR; -.
DR PhylomeDB; P25953; -.
DR BioCyc; BSUB:BSU24730-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0030420; P:establishment of competence for transformation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001482; T2SS/T4SS.
DR Pfam; PF00437; T2SSE; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00662; T2SP_E; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Competence; Membrane; Nucleotide-binding;
KW Reference proteome; Transport.
FT CHAIN 1..356
FT /note="ComG operon protein 1"
FT /id="PRO_0000207293"
FT BINDING 144..151
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MUTAGEN 150
FT /note="K->Q: Cells no longer transformable but still
FT undergo competence-associated growth arrest; protein
FT localizes to the cell pole."
FT /evidence="ECO:0000269|PubMed:16009133"
SQ SEQUENCE 356 AA; 40459 MW; C15840FFB734E266 CRC64;
MDSIEKVSKN LIEEAYLTKA SDIHIVPRER DAIIHFRVDH ALLKKRDMKK EECVRLISHF
KFLSAMDIGE RRKPQNGSLT LKLKEGNVHL RMSTLPTINE ESLVIRVMPQ YNIPSIDKLS
LFPKTGATLL SFLKHSHGML IFTGPTGSGK TTTLYSLVQY AKKHFNRNIV TLEDPVETRD
EDVLQVQVNE KAGVTYSAGL KAILRHDPDM IILGEIRDAE TAEIAVRAAM TGHLVLTSLH
TRDAKGAIYR LLEFGINMNE IEQTVIAIAA QRLVDLACPF CENGCSSVYC RQSRNTRRAS
VYELLYGKNL QQCIQEAKGN HANYQYQTLR QIIRKGIALG YLTTNNYDRW VYHEKD
