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 03-AUG-2022, entry version 131.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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 AlphaFoldDB; 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; BSU_25590.
DR GeneID; 937827; -.
DR KEGG; bsu:BSU25590; -.
DR PATRIC; fig|224308.179.peg.2782; -.
DR eggNOG; COG1555; Bacteria.
DR eggNOG; COG1596; Bacteria.
DR InParanoid; P39694; -.
DR OMA; MVDIKGA; -.
DR PhylomeDB; P39694; -.
DR BioCyc; BSUB:BSU25590-MON; -.
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:0015627; C:type II protein secretion system complex; IBA:GO_Central.
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 GO; GO:0015628; P:protein secretion by the type II secretion system; IBA:GO_Central.
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;
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
