BCEB_BACSU
ID BCEB_BACSU Reviewed; 646 AA.
AC O34741;
DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Bacitracin export permease protein BceB;
GN Name=bceB; Synonyms=barD, ytsD; OrderedLocusNames=BSU30370;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9387221; DOI=10.1099/00221287-143-11-3431;
RA Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.;
RT "Sequencing and functional annotation of the Bacillus subtilis genes in the
RT 200 kb rrnB-dnaB region.";
RL Microbiology 143:3431-3441(1997).
RN [2]
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 [3]
RP INDUCTION, AND PROBABLE FUNCTION.
RC STRAIN=168;
RX PubMed=14612242; DOI=10.1016/s0378-1097(03)00738-9;
RA Bernard R., Joseph P., Guiseppi A., Chippaux M., Denizot F.;
RT "YtsCD and YwoA, two independent systems that confer bacitracin resistance
RT to Bacillus subtilis.";
RL FEMS Microbiol. Lett. 228:93-97(2003).
RN [4]
RP INDUCTION, AND PROBABLE FUNCTION.
RC STRAIN=168;
RX PubMed=12890034; DOI=10.1046/j.1365-2958.2003.03653.x;
RA Ohki R., Giyanto X., Tateno K., Masuyama W., Moriya S., Kobayashi K.,
RA Ogasawara N.;
RT "The BceRS two-component regulatory system induces expression of the
RT bacitracin transporter, BceAB, in Bacillus subtilis.";
RL Mol. Microbiol. 49:1135-1144(2003).
RN [5]
RP INDUCTION.
RC STRAIN=168 / CU1065;
RX PubMed=14651641; DOI=10.1046/j.1365-2958.2003.03786.x;
RA Mascher T., Margulis N.G., Wang T., Ye R.W., Helmann J.D.;
RT "Cell wall stress responses in Bacillus subtilis: the regulatory network of
RT the bacitracin stimulon.";
RL Mol. Microbiol. 50:1591-1604(2003).
CC -!- FUNCTION: Part of the ABC transporter complex BceAB (TC 3.A.1.123.5)
CC involved in bacitracin export.
CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins (BceA) and
CC two transmembrane proteins (BceB). {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- INDUCTION: Expression is induced by bacitracin, via the two-component
CC regulatory system BceS/BceR. {ECO:0000269|PubMed:12890034,
CC ECO:0000269|PubMed:14612242, ECO:0000269|PubMed:14651641}.
CC -!- SIMILARITY: Belongs to the ABC-4 integral membrane protein family.
CC {ECO:0000305}.
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DR EMBL; AF008220; AAC00256.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15015.1; -; Genomic_DNA.
DR PIR; B70001; B70001.
DR RefSeq; NP_390915.1; NC_000964.3.
DR RefSeq; WP_003229139.1; NZ_JNCM01000036.1.
DR PDB; 7TCG; EM; 3.80 A; A=1-646.
DR PDB; 7TCH; EM; 3.70 A; A=1-646.
DR PDBsum; 7TCG; -.
DR PDBsum; 7TCH; -.
DR AlphaFoldDB; O34741; -.
DR STRING; 224308.BSU30370; -.
DR TCDB; 3.A.1.134.3; the atp-binding cassette (abc) superfamily.
DR PaxDb; O34741; -.
DR PRIDE; O34741; -.
DR EnsemblBacteria; CAB15015; CAB15015; BSU_30370.
DR GeneID; 938178; -.
DR KEGG; bsu:BSU30370; -.
DR PATRIC; fig|224308.179.peg.3294; -.
DR eggNOG; COG0577; Bacteria.
DR OMA; SFMPVII; -.
DR PhylomeDB; O34741; -.
DR BioCyc; BSUB:BSU30370-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:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR InterPro; IPR003838; ABC3_permease_dom.
DR InterPro; IPR027022; ABC_permease_BceB-typ.
DR Pfam; PF02687; FtsX; 1.
DR PIRSF; PIRSF018968; ABC_permease_BceB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic resistance; Cell membrane; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..646
FT /note="Bacitracin export permease protein BceB"
FT /id="PRO_0000064868"
FT TRANSMEM 18..38
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 115..135
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 152..172
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 232..252
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 290..310
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 526..546
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 588..608
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 616..636
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 646 AA; 72186 MW; 99527B771C2D9D22 CRC64;
MNINQLILRN LKKNLRNYYL YVFALIFSVA LYFAFVTLQY DPAINEVKAS IKGAAAIKTA
SILLVAVVAI FILYANTIFI KRRSKEIGLF QLIGMTKHKI FRILSAENVM LYFGSLAIGV
AAGFSISKLV LMILFKIVDV KADAKLHFSE QALVQTVIVF CGIYLLIMIM NYTFIKKQSI
LSLFKVTSST EDKVKKISFF QMLIGALGIV LILTGYYVSS ELFGGKFKTI NELFVAMSFI
LGSVIIGTFL FYKGSVTFIS NIIRKSKGGY LNISEVLSLS SIMFRMKSNA LLLTIITTVS
ALAIGLLSLA YISYYSSEKT AEQNVAADFS FMNEKDAKLF ENKLRESNIS FVKKATPVLQ
ANVDIANIMD GTPKEMQGDP GNMQLAVVSD KDVKGVDVAA GEAVFSGYTD LLQKIMVFKD
SGVIKVKSKH ETQPLKYKGL REEFLVSYTF TSGGMPAVIV DDSLFKQLDK DKDPRIQLAQ
STFIGVNVKH DDQMEKANEL FQQVNKKNEH LSRLDTSAAQ KSLFGMVMFI VGFLGLTFLI
TSGCILYFKQ MGESEDEKPS YTILRKLGFT QGDLIKGIRI KQMYNFGIPL VVGLFHSYFA
VQSGWFLFGS EVWAPMIMVM VLYTALYSIF GFLSVLYYKK VIKSSL
