(data stored in SCRATCH zone)

SWISSPROT: 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   11-DEC-2019, entry version 128.
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;
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}.
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   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; BSU24730.
DR   GeneID; 938516; -.
DR   KEGG; bsu:BSU24730; -.
DR   PATRIC; fig|224308.179.peg.2691; -.
DR   eggNOG; COG2804; LUCA.
DR   HOGENOM; HOG000008426; -.
DR   InParanoid; P25953; -.
DR   KO; K02243; -.
DR   OMA; AKGAIYR; -.
DR   PhylomeDB; P25953; -.
DR   BioCyc; BSUB:BSU24730-MONOMER; -.
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   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;
DR   PRODOM; P25953.
DR   SWISS-2DPAGE; P25953.
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   NP_BIND         144..151
FT                   /note="ATP"
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
//

If you have problems or comments...

PBIL Back to PBIL home page