FEUA_BACSU
ID FEUA_BACSU Reviewed; 317 AA.
AC P40409;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Iron-uptake system-binding protein;
DE Flags: Precursor;
GN Name=feuA; OrderedLocusNames=BSU01630;
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, SUBCELLULAR LOCATION, POSSIBLE SUBUNIT, DISRUPTION PHENOTYPE, AND
RP INDUCTION.
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.
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, ECO:0000305|PubMed:16672620}; Lipid-anchor
CC {ECO:0000305|PubMed:16672620}. Cytoplasm {ECO:0000269|PubMed:16672620}.
CC Membrane raft {ECO:0000269|PubMed:20713508,
CC ECO:0000269|PubMed:22882210}; Lipid-anchor
CC {ECO:0000305|PubMed:16672620}. Note=Present in detergent-resistant
CC membrane (DRM) fractions that may be equivalent to eukaryotic membrane
CC rafts; these rafts include proteins involved in signaling, molecule
CC trafficking and protein secretion. {ECO:0000269|PubMed:20713508,
CC ECO:0000269|PubMed:22882210}.
CC -!- INDUCTION: Repressed by fur. Induced by Btr in iron-limited conditions.
CC {ECO:0000269|PubMed:16672620, ECO:0000269|PubMed:17725565}.
CC -!- DISRUPTION PHENOTYPE: Strains lacking this gene show a reduction in
CC growth stimulation by the catecholate siderophores enterobactin and
CC bacillibactin. {ECO:0000269|PubMed:16672620}.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 8 family.
CC {ECO:0000305}.
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DR EMBL; L19954; AAA64354.1; -; Genomic_DNA.
DR EMBL; AB002150; BAA19496.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB11939.1; -; Genomic_DNA.
DR PIR; I39842; I39842.
DR RefSeq; NP_388044.1; NC_000964.3.
DR RefSeq; WP_003234978.1; NZ_JNCM01000030.1.
DR PDB; 2PHZ; X-ray; 2.15 A; A=21-317.
DR PDB; 2WHY; X-ray; 1.70 A; A=21-317.
DR PDB; 2WI8; X-ray; 1.55 A; A=21-317.
DR PDB; 2XUZ; X-ray; 1.90 A; A=21-317.
DR PDB; 2XV1; X-ray; 2.15 A; A=21-317.
DR PDBsum; 2PHZ; -.
DR PDBsum; 2WHY; -.
DR PDBsum; 2WI8; -.
DR PDBsum; 2XUZ; -.
DR PDBsum; 2XV1; -.
DR AlphaFoldDB; P40409; -.
DR SMR; P40409; -.
DR STRING; 224308.BSU01630; -.
DR TCDB; 3.A.1.14.15; the atp-binding cassette (abc) superfamily.
DR PaxDb; P40409; -.
DR PRIDE; P40409; -.
DR DNASU; 938891; -.
DR EnsemblBacteria; CAB11939; CAB11939; BSU_01630.
DR GeneID; 938891; -.
DR KEGG; bsu:BSU01630; -.
DR PATRIC; fig|224308.179.peg.169; -.
DR eggNOG; COG0614; Bacteria.
DR InParanoid; P40409; -.
DR OMA; ENMMLLA; -.
DR PhylomeDB; P40409; -.
DR BioCyc; BSUB:BSU01630-MON; -.
DR EvolutionaryTrace; P40409; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR GO; GO:0055072; P:iron ion homeostasis; IEA:UniProtKB-KW.
DR InterPro; IPR002491; ABC_transptr_periplasmic_BD.
DR Pfam; PF01497; Peripla_BP_2; 1.
DR PROSITE; PS50983; FE_B12_PBP; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Cytoplasm; Ion transport; Iron;
KW Iron transport; Lipoprotein; Membrane; Palmitate; Reference proteome;
KW Signal; Transport.
FT SIGNAL 1..19
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 20..317
FT /note="Iron-uptake system-binding protein"
FT /id="PRO_0000031822"
FT DOMAIN 57..317
FT /note="Fe/B12 periplasmic-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00344"
FT LIPID 20
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 20
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT STRAND 37..43
FT /evidence="ECO:0007829|PDB:2WI8"
FT STRAND 46..53
FT /evidence="ECO:0007829|PDB:2WI8"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:2WI8"
FT HELIX 63..72
FT /evidence="ECO:0007829|PDB:2WI8"
FT STRAND 77..82
FT /evidence="ECO:0007829|PDB:2WI8"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:2WI8"
FT TURN 91..93
FT /evidence="ECO:0007829|PDB:2WI8"
FT STRAND 98..102
FT /evidence="ECO:0007829|PDB:2WI8"
FT HELIX 108..114
FT /evidence="ECO:0007829|PDB:2WI8"
FT STRAND 117..122
FT /evidence="ECO:0007829|PDB:2WI8"
FT HELIX 127..134
FT /evidence="ECO:0007829|PDB:2WI8"
FT STRAND 139..142
FT /evidence="ECO:0007829|PDB:2WI8"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:2WI8"
FT HELIX 149..160
FT /evidence="ECO:0007829|PDB:2WI8"
FT HELIX 163..183
FT /evidence="ECO:0007829|PDB:2WI8"
FT HELIX 186..189
FT /evidence="ECO:0007829|PDB:2WI8"
FT STRAND 193..199
FT /evidence="ECO:0007829|PDB:2WI8"
FT STRAND 202..205
FT /evidence="ECO:0007829|PDB:2WI8"
FT HELIX 213..216
FT /evidence="ECO:0007829|PDB:2WI8"
FT TURN 217..220
FT /evidence="ECO:0007829|PDB:2WI8"
FT HELIX 226..230
FT /evidence="ECO:0007829|PDB:2WI8"
FT STRAND 232..236
FT /evidence="ECO:0007829|PDB:2WI8"
FT HELIX 239..245
FT /evidence="ECO:0007829|PDB:2WI8"
FT STRAND 248..254
FT /evidence="ECO:0007829|PDB:2WI8"
FT HELIX 256..258
FT /evidence="ECO:0007829|PDB:2WI8"
FT HELIX 265..271
FT /evidence="ECO:0007829|PDB:2WI8"
FT HELIX 273..276
FT /evidence="ECO:0007829|PDB:2WI8"
FT HELIX 279..282
FT /evidence="ECO:0007829|PDB:2WI8"
FT STRAND 286..288
FT /evidence="ECO:0007829|PDB:2WI8"
FT STRAND 297..299
FT /evidence="ECO:0007829|PDB:2WI8"
FT HELIX 300..314
FT /evidence="ECO:0007829|PDB:2WI8"
SQ SEQUENCE 317 AA; 35108 MW; 57193CB61E835D25 CRC64;
MKKISLTLLI LLLALTAAAC GSKNESTASK ASGTASEKKK IEYLDKTYEV TVPTDKIAIT
GSVESMEDAK LLDVHPQGAI SFSGKFPDMF KDITDKAEPT GEKMEPNIEK ILEMKPDVIL
ASTKFPEKTL QKISTAGTTI PVSHISSNWK ENMMLLAQLT GKEKKAKKII ADYEQDLKEI
KTKINDKAKD SKALVIRIRQ GNIYIYPEQV YFNSTLYGDL GLKAPNEVKA AKAQELSSLE
KLSEMNPDHI FVQFSDDENA DKPDALKDLE KNPIWKSLKA VKEDHVYVNS VDPLAQGGTA
WSKVRFLKAA AEKLTQN
