COMEC_BACSU
ID COMEC_BACSU Reviewed; 776 AA.
AC P39695;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 04-AUG-2003, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=ComE operon protein 3;
GN Name=comEC; Synonyms=comE3; OrderedLocusNames=BSU25570;
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 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 [5]
RP DISRUPTION PHENOTYPE.
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: The comE operon is required for the binding and uptake of
CC transforming DNA. ComEC is required for internalization but is
CC dispensable for DNA binding. {ECO:0000269|PubMed:7968523}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- INDUCTION: Expression activated by ComK (PubMed:11948146).
CC {ECO:0000269|PubMed:11948146}.
CC -!- DISRUPTION PHENOTYPE: Destabilization of ComFA (PubMed:17630974).
CC {ECO:0000269|PubMed:17630974}.
CC -!- SIMILARITY: To H.influenzae REC2, N.gonorrhoeae ComA and E.coli YcaI.
CC {ECO:0000305}.
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DR EMBL; L15202; AAC36907.1; -; Unassigned_DNA.
DR EMBL; D84432; BAA12454.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14499.1; -; Genomic_DNA.
DR PIR; S39865; S39865.
DR RefSeq; NP_390435.1; NC_000964.3.
DR RefSeq; WP_009967776.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; P39695; -.
DR SMR; P39695; -.
DR IntAct; P39695; 2.
DR STRING; 224308.BSU25570; -.
DR TCDB; 3.A.11.1.1; the bacterial competence-related dna transformation transporter (dna-t) family.
DR PaxDb; P39695; -.
DR PRIDE; P39695; -.
DR EnsemblBacteria; CAB14499; CAB14499; BSU_25570.
DR GeneID; 937839; -.
DR KEGG; bsu:BSU25570; -.
DR PATRIC; fig|224308.179.peg.2780; -.
DR eggNOG; COG0658; Bacteria.
DR eggNOG; COG2333; Bacteria.
DR InParanoid; P39695; -.
DR OMA; RTDKQGA; -.
DR PhylomeDB; P39695; -.
DR BioCyc; BSUB:BSU25570-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:0030420; P:establishment of competence for transformation; IEA:UniProtKB-KW.
DR CDD; cd07731; ComA-like_MBL-fold; 1.
DR Gene3D; 3.60.15.10; -; 1.
DR InterPro; IPR035681; ComA-like_MBL.
DR InterPro; IPR004477; ComEC_N.
DR InterPro; IPR004797; Competence_ComEC/Rec2.
DR InterPro; IPR025405; DUF4131.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR Pfam; PF03772; Competence; 1.
DR Pfam; PF13567; DUF4131; 1.
DR Pfam; PF00753; Lactamase_B; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
DR TIGRFAMs; TIGR00360; ComEC_N-term; 1.
DR TIGRFAMs; TIGR00361; ComEC_Rec2; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Competence; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..776
FT /note="ComE operon protein 3"
FT /id="PRO_0000090009"
FT TRANSMEM 19..39
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 45..65
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 232..252
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 263..283
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 308..328
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 352..372
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 387..407
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 416..436
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 443..463
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 475..495
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CONFLICT 451
FT /note="V -> I (in Ref. 1; AAC36907)"
FT /evidence="ECO:0000305"
FT CONFLICT 639
FT /note="P -> K (in Ref. 1; AAC36907)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 776 AA; 86701 MW; 90F50E1EECEEFB2A CRC64;
MRNSRLLLPM AAASATAGIT AAAYFPAIFL FILFLLIILI KTRHAFLIIV CFFSFILFFV
LYAVTDSQNV SSYRQGTYQF KAVIDTIPKI DGDRMSMMVE TPDKEKWAAA YRIQSAGEKE
QLLYIEPGMS CELTGTLEEP NHATVPGAFD YNEYLYRQHI HWNYSVTSIQ NCSEPENFKY
KVLSLRKHII SFTNSLLPPD STGIVQALTV GDRFYVEDEV LTAYQKLGVV HLLAISGLHV
GILTAGLFYI MIRLGITREK ASILLLLFLP LYVMLTGAAP SVLRAALMSG VYLAGSLVKW
RVRSATAICL SYIVLLLFNP YHLFEAGFQL SFAVSFSLIL SSSIFQQVKT SLGQLTIVSL
IAQLGSLPIL LYHFHQFSII SVPMNMLMVP FYTFCILPGA VAGVLLLSLS ASFGRLFFSW
FDLLISWINR LITNIADVDV FTIMIAHPAP VLLFLFTVTI ILLLMAIEKR SLSQLMVTGG
ICCTVMFLLF IYPCLSSEGE VDMIDIGQGD SMFVGAPHQR GRVLIDTGGT LSYSSEPWRE
KQHPFSLGEK VLIPFLTAKG IKQLDALILT HADQDHIGEA EILLKHHKVK RLVIPKGFVS
EPKDEKVLQA AREEGVAIEE VKRGDVLQIK DLQFHVLSPE APDPASKNNS SLVLWMETGG
MSWILTGDLE KEGEQEVMNV FPNIKADVLK VGHHGSKGST GEEFIQQLQP KTAIISAGKN
NRYHHPHQKV LQLLQRHSIR VLRTDQNGTI QYRYKNRVGT FSVYPPYDTS DITETN
