BCEA_BACSU
ID BCEA_BACSU Reviewed; 253 AA.
AC O34697;
DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Bacitracin export ATP-binding protein BceA;
GN Name=bceA; Synonyms=barC, ytsC; OrderedLocusNames=BSU30380;
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. Responsible for energy coupling to the
CC transport system.
CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins (BceA) and
CC two transmembrane proteins (BceB). {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 transporter superfamily. {ECO:0000305}.
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DR EMBL; AF008220; AAC00255.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15016.1; -; Genomic_DNA.
DR PIR; A70001; A70001.
DR RefSeq; NP_390916.1; NC_000964.3.
DR RefSeq; WP_003229137.1; NZ_JNCM01000036.1.
DR PDB; 7TCG; EM; 3.80 A; B/C=2-253.
DR PDB; 7TCH; EM; 3.70 A; B/C=2-253.
DR PDBsum; 7TCG; -.
DR PDBsum; 7TCH; -.
DR AlphaFoldDB; O34697; -.
DR SMR; O34697; -.
DR STRING; 224308.BSU30380; -.
DR TCDB; 3.A.1.134.3; the atp-binding cassette (abc) superfamily.
DR PaxDb; O34697; -.
DR EnsemblBacteria; CAB15016; CAB15016; BSU_30380.
DR GeneID; 937246; -.
DR KEGG; bsu:BSU30380; -.
DR PATRIC; fig|224308.179.peg.3295; -.
DR eggNOG; COG1136; Bacteria.
DR InParanoid; O34697; -.
DR OMA; WKEYGDQ; -.
DR PhylomeDB; O34697; -.
DR BioCyc; BSUB:BSU30380-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR CDD; cd03255; ABC_MJ0796_LolCDE_FtsE; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017911; MacB_ATP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic resistance; ATP-binding; Nucleotide-binding;
KW Reference proteome; Transport.
FT CHAIN 1..253
FT /note="Bacitracin export ATP-binding protein BceA"
FT /id="PRO_0000091945"
FT DOMAIN 4..243
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 40..47
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 253 AA; 28234 MW; 95D28581A96627AA CRC64;
MVILEANKIR KSYGNKLNKQ EVLKGIDIHI EKGEFVSIMG ASGSGKTTLL NVLSSIDQVS
HGTIHINGND MTAMKEKQLA EFRKQHLGFI FQDYNLLDTL TVKENILLPL SITKLSKKEA
NRKFEEVAKE LGIYELRDKY PNEISGGQKQ RTSAGRAFIH DPSIIFADEP TGALDSKSAS
DLLNKLSQLN QKRNATIIMV THDPVAASYC GRVIFIKDGQ MYTQLNKGGQ DRQTFFQDIM
KTQGVLGGVQ HEH
