(data stored in SCRATCH zone)

SWISSPROT: COMEA_BACSU

ID   COMEA_BACSU             Reviewed;         205 AA.
AC   P39694;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   11-DEC-2019, entry version 124.
DE   RecName: Full=ComE operon protein 1;
GN   Name=comEA; Synonyms=comE1; OrderedLocusNames=BSU25590;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX   PubMed=7968523; DOI=10.1111/j.1365-2958.1993.tb00907.x;
RA   Hahn J., Inamine G., Kozlov Y., Dubnau D.A.;
RT   "Characterization of comE, a late competence operon of Bacillus subtilis
RT   required for the binding and uptake of transforming DNA.";
RL   Mol. Microbiol. 10:99-110(1993).
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   CHARACTERIZATION.
RX   PubMed=7768800; DOI=10.1128/jb.177.11.3045-3051.1995;
RA   Inamine G.S., Dubnau D.;
RT   "ComEA, a Bacillus subtilis integral membrane protein required for genetic
RT   transformation, is needed for both DNA binding and transport.";
RL   J. Bacteriol. 177:3045-3051(1995).
RN   [5]
RP   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   [6]
RP   SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
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).
CC   -!- FUNCTION: Needed for both DNA binding and transport. It is absolutely
CC       required for the uptake of transforming DNA but not for binding. Its
CC       role in binding may be indirect. {ECO:0000269|PubMed:7968523}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane
CC       protein. Note=Localizes in a nonuniform, punctate manner in competent
CC       cells, unlike some other competence proteins is not localized to the
CC       cell poles (PubMed:16009133). {ECO:0000269|PubMed:16009133}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in cells competent for DNA
CC       transformation; that is 5-20% of the population (PubMed:16009133).
CC   -!- INDUCTION: Expression activated by ComK (PubMed:11918817).
CC       {ECO:0000269|PubMed:11918817}.
DR   EMBL; L15202; AAC36905.1; -; Unassigned_DNA.
DR   EMBL; D84432; BAA12452.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14501.1; -; Genomic_DNA.
DR   PIR; S39863; S39863.
DR   RefSeq; NP_390437.1; NC_000964.3.
DR   RefSeq; WP_004398514.1; NZ_JNCM01000036.1.
DR   SMR; P39694; -.
DR   STRING; 224308.BSU25590; -.
DR   TCDB; 3.A.11.1.1; the bacterial competence-related dna transformation transporter (dna-t) family.
DR   PaxDb; P39694; -.
DR   PRIDE; P39694; -.
DR   DNASU; 937827; -.
DR   EnsemblBacteria; CAB14501; CAB14501; BSU25590.
DR   GeneID; 937827; -.
DR   KEGG; bsu:BSU25590; -.
DR   PATRIC; fig|224308.179.peg.2782; -.
DR   eggNOG; ENOG4105KQC; Bacteria.
DR   eggNOG; COG1555; LUCA.
DR   HOGENOM; HOG000015829; -.
DR   InParanoid; P39694; -.
DR   KO; K02237; -.
DR   OMA; MVDIKGA; -.
DR   PhylomeDB; P39694; -.
DR   BioCyc; BSUB:BSU25590-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
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:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR   GO; GO:0030420; P:establishment of competence for transformation; IEA:UniProtKB-KW.
DR   InterPro; IPR004787; Competence_ComE.
DR   InterPro; IPR004509; Competence_ComEA_HhH.
DR   InterPro; IPR003583; Hlx-hairpin-Hlx_DNA-bd_motif.
DR   InterPro; IPR010994; RuvA_2-like.
DR   InterPro; IPR019554; Soluble_ligand-bd.
DR   Pfam; PF10531; SLBB; 1.
DR   SMART; SM00278; HhH1; 2.
DR   SUPFAM; SSF47781; SSF47781; 1.
DR   TIGRFAMs; TIGR01259; comE; 1.
DR   TIGRFAMs; TIGR00426; TIGR00426; 1.
PE   1: Evidence at protein level;
DR   PRODOM; P39694.
DR   SWISS-2DPAGE; P39694.
KW   Cell membrane; Competence; Membrane; Reference proteome; Repeat;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..205
FT                   /note="ComE operon protein 1"
FT                   /id="PRO_0000090008"
FT   TOPO_DOM        1..9
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        10..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        29..205
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          142..171
FT                   /note="HhH 1"
FT   DOMAIN          172..201
FT                   /note="HhH 2"
SQ   SEQUENCE   205 AA;  21769 MW;  4E3817FAF982F9DE CRC64;
     MNWLNQHKKA IILAASAAVF TAIMIFLATG KNKEPVKQAV PTETENTVVK QEANNDESNE
     TIVIDIKGAV QHPGVYEMRT GDRVSQAIEK AGGTSEQADE AQVNLAEILQ DGTVVYIPKK
     GEETAVQQGG GGSVQSDGGK GALVNINTAT LEELQGISGV GPSKAEAIIA YREENGRFQT
     IEDITKVSGI GEKSFEKIKS SITVK
//

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