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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
 
 
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