FEUB_BACSU
ID FEUB_BACSU Reviewed; 334 AA.
AC P40410;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Iron-uptake system permease protein FeuB;
GN Name=feuB; OrderedLocusNames=BSU01620;
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=BD99 / MS94;
RX PubMed=8011666; DOI=10.1016/0005-2728(94)90131-7;
RA Quirk P.G., Guffanti A.A., Clejan S., Cheng J., Krulwich T.A.;
RT "Isolation of Tn917 insertional mutants of Bacillus subtilis that are
RT resistant to the protonophore carbonyl cyanide m-chlorophenylhydrazone.";
RL Biochim. Biophys. Acta 1186:27-34(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9274029; DOI=10.1099/00221287-143-8-2763;
RA Liu H., Haga K., Yasumoto K., Ohashi Y., Yoshikawa H., Takahashi H.;
RT "Sequence and analysis of a 31 kb segment of the Bacillus subtilis
RT chromosome in the area of the rrnH and rrnG operons.";
RL Microbiology 143:2763-2767(1997).
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 FUNCTION, AND POSSIBLE SUBUNIT.
RC STRAIN=168;
RX PubMed=16672620; DOI=10.1128/jb.188.10.3664-3673.2006;
RA Ollinger J., Song K.-B., Antelmann H., Hecker M., Helmann J.D.;
RT "Role of the Fur regulon in iron transport in Bacillus subtilis.";
RL J. Bacteriol. 188:3664-3673(2006).
RN [5]
RP INDUCTION.
RC STRAIN=168 / CU1065;
RX PubMed=17725565; DOI=10.1111/j.1365-2958.2007.05905.x;
RA Gaballa A., Helmann J.D.;
RT "Substrate induction of siderophore transport in Bacillus subtilis mediated
RT by a novel one-component regulator.";
RL Mol. Microbiol. 66:164-173(2007).
RN [6]
RP SUBCELLULAR LOCATION.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=20713508; DOI=10.1101/gad.1945010;
RA Lopez D., Kolter R.;
RT "Functional microdomains in bacterial membranes.";
RL Genes Dev. 24:1893-1902(2010).
RN [7]
RP SUBCELLULAR LOCATION.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=22882210; DOI=10.1111/j.1365-2958.2012.08205.x;
RA Yepes A., Schneider J., Mielich B., Koch G., Garcia-Betancur J.C.,
RA Ramamurthi K.S., Vlamakis H., Lopez D.;
RT "The biofilm formation defect of a Bacillus subtilis flotillin-defective
RT mutant involves the protease FtsH.";
RL Mol. Microbiol. 86:457-471(2012).
CC -!- FUNCTION: Involved in the uptake of iron. Probably responsible for the
CC translocation of the substrate across the membrane.
CC {ECO:0000269|PubMed:16672620}.
CC -!- FUNCTION: Part of the ABC transporter complex FeuABC/YusV involved in
CC import of the catecholate siderophores bacillibactin and enterobactin.
CC {ECO:0000305|PubMed:16672620}.
CC -!- SUBUNIT: The complex is composed of one ATP-binding protein (YusV), two
CC transmembrane proteins (FeuB and FeuC) and a solute-binding protein
CC (FeuA). {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20713508,
CC ECO:0000269|PubMed:22882210}; Multi-pass membrane protein. Membrane
CC raft {ECO:0000269|PubMed:20713508, ECO:0000269|PubMed:22882210}; Multi-
CC pass membrane protein {ECO:0000255}. Note=Present in detergent-
CC resistant membrane (DRM) fractions that may be equivalent to eukaryotic
CC membrane rafts; these rafts include proteins involved in signaling,
CC molecule trafficking and protein secretion.
CC {ECO:0000269|PubMed:20713508, ECO:0000269|PubMed:22882210}.
CC -!- INDUCTION: Induced by Btr in iron-limited conditions.
CC {ECO:0000269|PubMed:17725565}.
CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC permease family. FecCD subfamily. {ECO:0000305}.
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DR EMBL; L19954; AAA64355.1; -; Genomic_DNA.
DR EMBL; AB002150; BAA19495.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB11938.1; -; Genomic_DNA.
DR PIR; I39843; I39843.
DR RefSeq; NP_388043.1; NC_000964.3.
DR RefSeq; WP_003234979.1; NZ_JNCM01000030.1.
DR AlphaFoldDB; P40410; -.
DR SMR; P40410; -.
DR STRING; 224308.BSU01620; -.
DR TCDB; 3.A.1.14.15; the atp-binding cassette (abc) superfamily.
DR PaxDb; P40410; -.
DR PRIDE; P40410; -.
DR EnsemblBacteria; CAB11938; CAB11938; BSU_01620.
DR GeneID; 938884; -.
DR KEGG; bsu:BSU01620; -.
DR PATRIC; fig|224308.179.peg.168; -.
DR eggNOG; COG0609; Bacteria.
DR InParanoid; P40410; -.
DR OMA; WYSARLH; -.
DR PhylomeDB; P40410; -.
DR BioCyc; BSUB:BSU01620-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0006811; P:ion transport; IEP:CACAO.
DR GO; GO:0033214; P:siderophore-dependent iron import into cell; IBA:GO_Central.
DR Gene3D; 1.10.3470.10; -; 1.
DR InterPro; IPR037294; ABC_BtuC-like.
DR InterPro; IPR000522; ABC_transptr_permease_BtuC.
DR PANTHER; PTHR30472; PTHR30472; 1.
DR Pfam; PF01032; FecCD; 1.
DR SUPFAM; SSF81345; SSF81345; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Ion transport; Iron; Iron transport; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..334
FT /note="Iron-uptake system permease protein FeuB"
FT /id="PRO_0000060024"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 63..83
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 91..111
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 119..139
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 191..211
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 243..263
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 281..301
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 305..325
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 334 AA; 35897 MW; 5FD4CF983E51D9E3 CRC64;
MYSKQWTRII LITSPFAIAL SLLLSILYGA KHLSTDIVFT SLIHFDPGNT DHQIIWHSRI
PRAAGALLIG AALAVSGALM QGITRNYLAS PSIMGVSDGS AFIITLCMVL LPQSSSIEMM
IYSFIGSALG AVLVFGLAAM MPNGFTPVQL AIIGTVTSML LSSLSAAMSI YFQISQDLSF
WYSARLHQMS PDFLKLAAPF FLIGIIMAIS LSKKVTAVSL GDDISKSLGQ KKKTIKIMAM
LSVIILTGSA VALAGKIAFV GLVVPHITRF LVGSDYSRLI PCSCILGGIF LTLCDLASRF
INYPFETPIE VVTSIIGVPF FLYLIKRKGG EQNG
