YXEB_BACSU
ID YXEB_BACSU Reviewed; 321 AA.
AC P54941;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Iron(3+)-hydroxamate-binding protein YxeB;
DE AltName: Full=Ferric hydroxamate uptake protein YxeB;
DE AltName: Full=Iron(III)-hydroxamate-binding protein YxeB;
DE Flags: Precursor;
GN Name=yxeB; OrderedLocusNames=BSU39610; ORFNames=HS74BR;
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 / BGSC1A1;
RX PubMed=8867804; DOI=10.1093/dnares/2.6.295;
RA Yoshida K., Fujimyra M., Yanai N., Fujita Y.;
RT "Cloning and sequencing of a 23-kb region of the Bacillus subtilis genome
RT between the iol and hut operons.";
RL DNA Res. 2:295-301(1995).
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 SEQUENCE REVISION TO C-TERMINUS.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [4]
RP FUNCTION IN DESFERRIOXAMINE TRANSPORT.
RC STRAIN=168 / CU1065;
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 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 [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=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: Part of the ABC transporter complex FhuCBGD involved in
CC iron(3+)-hydroxamate import. Binds the iron(3+)-hydroxamate complex and
CC transfers it to the membrane-bound permease. Partially required for the
CC transport of desferrioxamine. {ECO:0000269|PubMed:16672620}.
CC -!- SUBUNIT: The complex is composed of an ATP-binding protein (FhuC), two
CC transmembrane proteins (FhuB and FhuG) and a solute-binding protein
CC (FhuD or YxeB). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20713508,
CC ECO:0000269|PubMed:22882210}; Lipid-anchor {ECO:0000305}. Membrane raft
CC {ECO:0000269|PubMed:20713508, ECO:0000269|PubMed:22882210}; Peripheral
CC membrane protein {ECO:0000305}. 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 -!- SIMILARITY: Belongs to the bacterial solute-binding protein 8 family.
CC {ECO:0000305}.
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DR EMBL; D45912; BAA08318.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15997.2; -; Genomic_DNA.
DR PIR; D70074; D70074.
DR RefSeq; NP_391840.2; NC_000964.3.
DR RefSeq; WP_003243725.1; NZ_JNCM01000034.1.
DR AlphaFoldDB; P54941; -.
DR SMR; P54941; -.
DR STRING; 224308.BSU39610; -.
DR jPOST; P54941; -.
DR PaxDb; P54941; -.
DR PRIDE; P54941; -.
DR EnsemblBacteria; CAB15997; CAB15997; BSU_39610.
DR GeneID; 937581; -.
DR KEGG; bsu:BSU39610; -.
DR PATRIC; fig|224308.179.peg.4286; -.
DR eggNOG; COG0614; Bacteria.
DR InParanoid; P54941; -.
DR OMA; YAADYMF; -.
DR PhylomeDB; P54941; -.
DR BioCyc; BSUB:BSU39610-MON; -.
DR Proteomes; UP000001570; Chromosome.
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 Cell membrane; Ion transport; Iron; Iron transport; Lipoprotein; Membrane;
KW Palmitate; Reference proteome; Signal; Transport.
FT SIGNAL 1..20
FT /evidence="ECO:0000305"
FT CHAIN 21..321
FT /note="Iron(3+)-hydroxamate-binding protein YxeB"
FT /id="PRO_0000031825"
FT DOMAIN 58..316
FT /note="Fe/B12 periplasmic-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00344"
FT REGION 24..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 21
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000305"
FT LIPID 21
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000305"
FT CONFLICT 320..321
FT /note="Missing (in Ref. 1; BAA08318)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 321 AA; 35507 MW; 656D4044AE6CD561 CRC64;
MKKNILLVGM LVLLLMFVSA CSGTASKGSS SDSASEKTEM RTYKSPKGNV NIPAHPKRIV
TDFYAGELLS VGANVVGSGS WSFDNPFLKS KLKNVKDVGD PISVEKVMEL QPDLIVVMNE
ENVDKLKKIA PTVVIPYNTA KNVEDTVSMF GDIAGAKDQA KSFMADFNKK AEAAKKKIAG
VIDKDATFGI YENTDKGEFW VFNDNGGRGG QAVYNALGLK APEKIEQDVI KKGEMKQLSQ
EVIPEYAADY MFITDYNPKG ESKTLDKLEN SSIWKNLDAV KHNRVFINDF DSFYPYDPIS
VSKQVDIITD MLIKRAEENK K
