FHUD_BACSU
ID FHUD_BACSU Reviewed; 315 AA.
AC P37580;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Iron(3+)-hydroxamate-binding protein FhuD;
DE AltName: Full=Ferric hydroxamate uptake protein D;
DE AltName: Full=Ferrichrome-binding protein;
DE AltName: Full=Iron(III)-hydroxamate-binding protein FhuD;
DE Flags: Precursor;
GN Name=fhuD; OrderedLocusNames=BSU33320;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION IN IRON(3+)-HYDROXAMATE
RP TRANSPORT.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=8388528; DOI=10.1111/j.1365-2958.1993.tb01208.x;
RA Schneider R., Hantke K.;
RT "Iron-hydroxamate uptake systems in Bacillus subtilis: identification of a
RT lipoprotein as part of a binding protein-dependent transport system.";
RL Mol. Microbiol. 8:111-121(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RA Schneider R., Hantke K.;
RL Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9639930; DOI=10.1099/00221287-144-6-1593;
RA Wipat A., Brignell C.S., Guy J.B., Rose M., Emmerson P.T., Harwood C.R.;
RT "The yvsA-yvqA (293 degrees - 289 degrees) region of the Bacillus subtilis
RT chromosome containing genes involved in metal ion uptake and a putative
RT sigma factor.";
RL Microbiology 144:1593-1600(1998).
RN [4]
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 [5]
RP FUNCTION IN IRON(3+)-HYDROXAMATE 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 [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 INTERACTION WITH FLOT, AND SUBCELLULAR LOCATION.
RC STRAIN=168;
RX PubMed=23651456; DOI=10.1111/mmi.12252;
RA Bach J.N., Bramkamp M.;
RT "Flotillins functionally organize the bacterial membrane.";
RL Mol. Microbiol. 88:1205-1217(2013).
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. Required for the transport
CC of ferrichrome and coprogen. {ECO:0000269|PubMed:16672620,
CC ECO:0000269|PubMed:8388528}.
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 Lipid-anchor {ECO:0000305}. Membrane raft {ECO:0000269|PubMed:20713508,
CC ECO:0000269|PubMed:23651456}; Lipid-anchor {ECO:0000305}. Note=Present
CC in detergent-resistant membrane (DRM) fractions that may be equivalent
CC to eukaryotic membrane rafts; these rafts include proteins involved in
CC signaling, molecule trafficking and protein secretion.
CC {ECO:0000269|PubMed:20713508, ECO:0000269|PubMed:23651456}.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 8 family.
CC {ECO:0000305}.
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DR EMBL; M87283; AAA22424.1; -; Genomic_DNA.
DR EMBL; X93092; CAA63642.1; -; Genomic_DNA.
DR EMBL; AJ223978; CAA11719.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15338.1; -; Genomic_DNA.
DR PIR; S32930; S32930.
DR RefSeq; NP_391213.1; NC_000964.3.
DR RefSeq; WP_003243220.1; NZ_JNCM01000033.1.
DR PDB; 3G9Q; X-ray; 2.60 A; A=45-315.
DR PDB; 3HXP; X-ray; 3.20 A; A=25-315.
DR PDBsum; 3G9Q; -.
DR PDBsum; 3HXP; -.
DR AlphaFoldDB; P37580; -.
DR SMR; P37580; -.
DR STRING; 224308.BSU33320; -.
DR PaxDb; P37580; -.
DR PRIDE; P37580; -.
DR EnsemblBacteria; CAB15338; CAB15338; BSU_33320.
DR GeneID; 935996; -.
DR KEGG; bsu:BSU33320; -.
DR PATRIC; fig|224308.179.peg.3616; -.
DR eggNOG; COG0614; Bacteria.
DR InParanoid; P37580; -.
DR OMA; SIMQTNG; -.
DR PhylomeDB; P37580; -.
DR BioCyc; BSUB:BSU33320-MON; -.
DR EvolutionaryTrace; P37580; -.
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 3D-structure; Cell membrane; Ion transport; Iron; Iron transport;
KW Lipoprotein; Membrane; Palmitate; Reference proteome; Signal; Transport.
FT SIGNAL 1..23
FT /evidence="ECO:0000305"
FT CHAIN 24..315
FT /note="Iron(3+)-hydroxamate-binding protein FhuD"
FT /id="PRO_0000031823"
FT DOMAIN 60..315
FT /note="Fe/B12 periplasmic-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00344"
FT LIPID 24
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000305"
FT LIPID 24
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000305"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:3G9Q"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:3G9Q"
FT HELIX 69..75
FT /evidence="ECO:0007829|PDB:3G9Q"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:3G9Q"
FT HELIX 84..87
FT /evidence="ECO:0007829|PDB:3G9Q"
FT TURN 90..95
FT /evidence="ECO:0007829|PDB:3G9Q"
FT HELIX 108..112
FT /evidence="ECO:0007829|PDB:3G9Q"
FT STRAND 117..122
FT /evidence="ECO:0007829|PDB:3G9Q"
FT STRAND 125..127
FT /evidence="ECO:0007829|PDB:3HXP"
FT HELIX 129..135
FT /evidence="ECO:0007829|PDB:3G9Q"
FT STRAND 138..141
FT /evidence="ECO:0007829|PDB:3G9Q"
FT TURN 143..145
FT /evidence="ECO:0007829|PDB:3HXP"
FT HELIX 150..159
FT /evidence="ECO:0007829|PDB:3G9Q"
FT HELIX 162..187
FT /evidence="ECO:0007829|PDB:3G9Q"
FT STRAND 191..198
FT /evidence="ECO:0007829|PDB:3G9Q"
FT STRAND 201..205
FT /evidence="ECO:0007829|PDB:3G9Q"
FT STRAND 207..210
FT /evidence="ECO:0007829|PDB:3G9Q"
FT HELIX 213..217
FT /evidence="ECO:0007829|PDB:3G9Q"
FT TURN 218..220
FT /evidence="ECO:0007829|PDB:3HXP"
FT HELIX 226..232
FT /evidence="ECO:0007829|PDB:3G9Q"
FT TURN 233..235
FT /evidence="ECO:0007829|PDB:3G9Q"
FT STRAND 236..242
FT /evidence="ECO:0007829|PDB:3G9Q"
FT STRAND 244..246
FT /evidence="ECO:0007829|PDB:3HXP"
FT HELIX 247..250
FT /evidence="ECO:0007829|PDB:3G9Q"
FT STRAND 253..260
FT /evidence="ECO:0007829|PDB:3G9Q"
FT TURN 269..271
FT /evidence="ECO:0007829|PDB:3G9Q"
FT HELIX 273..276
FT /evidence="ECO:0007829|PDB:3G9Q"
FT HELIX 279..282
FT /evidence="ECO:0007829|PDB:3G9Q"
FT STRAND 286..288
FT /evidence="ECO:0007829|PDB:3G9Q"
FT HELIX 293..295
FT /evidence="ECO:0007829|PDB:3G9Q"
FT HELIX 299..314
FT /evidence="ECO:0007829|PDB:3G9Q"
SQ SEQUENCE 315 AA; 34426 MW; D5102CBD8F114EF1 CRC64;
MTHIYKKLGA AFFALLLIAA LAACGNNSES KGSASDSKGA ETFTYKAENG NVKIPKHPKR
VVVMADGYYG YFKTLGINVV GAPENVFKNP YYKGKTNGVE NIGDGTSVEK VIDLNPDLII
VWTTQGADIK KLEKIAPTVA VKYDKLDNIE QLKEFAKMTG TEDKAEKWLA KWDKKVAAAK
TKIKKAVGDK TISIMQTNGK DIYVFGKDFG RGGSIIYKDL GLQATKLTKE KAIDQGPGYT
SISLEKLPDF AGDYIFAGPW QSGGDDGGVF ESSIWKNLNA VKNGHVYKMD PIGFYFTDPI
SLEGQLEFIT ESLTK
