FIU_ECOLI
ID FIU_ECOLI Reviewed; 760 AA.
AC P75780;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Catecholate siderophore receptor Fiu;
DE AltName: Full=Ferric iron uptake protein;
DE AltName: Full=TonB-dependent receptor Fiu;
DE Flags: Precursor;
GN Name=fiu; Synonyms=ybiL; OrderedLocusNames=b0805, JW0790;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP FUNCTION IN TRANSPORT OF CATECHOL-SUBSTITUTED CEPHALOSPORINS, AND
RP INDUCTION.
RC STRAIN=K12;
RX PubMed=3072926; DOI=10.1128/aac.32.12.1879;
RA Curtis N.A.C., Eisenstadt R.L., East S.J., Cornford R.J., Walker L.A.,
RA White A.J.;
RT "Iron-regulated outer membrane proteins of Escherichia coli K-12 and
RT mechanism of action of catechol-substituted cephalosporins.";
RL Antimicrob. Agents Chemother. 32:1879-1886(1988).
RN [5]
RP FUNCTION.
RC STRAIN=K12;
RX PubMed=2139424; DOI=10.1016/0378-1097(90)90158-m;
RA Hantke K.;
RT "Dihydroxybenzoylserine -- a siderophore for E. coli.";
RL FEMS Microbiol. Lett. 55:5-8(1990).
RN [6]
RP FUNCTION IN TRANSPORT OF CATECHOL-CONTAINING ANTIBIOTICS.
RC STRAIN=K12;
RX PubMed=2407721; DOI=10.1128/jb.172.3.1361-1367.1990;
RA Nikaido H., Rosenberg E.Y.;
RT "Cir and Fiu proteins in the outer membrane of Escherichia coli catalyze
RT transport of monomeric catechols: study with beta-lactam antibiotics
RT containing catechol and analogous groups.";
RL J. Bacteriol. 172:1361-1367(1990).
RN [7]
RP INDUCTION.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=1804764; DOI=10.1016/0378-1097(91)90376-l;
RA Niehaus F., Hantke K., Unden G.;
RT "Iron content and FNR-dependent gene regulation in Escherichia coli.";
RL FEMS Microbiol. Lett. 68:319-323(1991).
RN [8]
RP INDUCTION.
RC STRAIN=K12;
RX PubMed=10411720; DOI=10.1046/j.1365-2958.1999.01423.x;
RA Newman D.L., Shapiro J.A.;
RT "Differential fiu-lacZ fusion regulation linked to Escherichia coli colony
RT development.";
RL Mol. Microbiol. 33:18-32(1999).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND PUTATIVE FUNCTION.
RX PubMed=10806384; DOI=10.1046/j.1432-1327.2000.01296.x;
RA Molloy M.P., Herbert B.R., Slade M.B., Rabilloud T., Nouwens A.S.,
RA Williams K.L., Gooley A.A.;
RT "Proteomic analysis of the Escherichia coli outer membrane.";
RL Eur. J. Biochem. 267:2871-2881(2000).
RN [10]
RP FUNCTION.
RX PubMed=12949180; DOI=10.1099/mic.0.26396-0;
RA Patzer S.I., Baquero M.R., Bravo D., Moreno F., Hantke K.;
RT "The colicin G, H and X determinants encode microcins M and H47, which
RT might utilize the catecholate siderophore receptors FepA, Cir, Fiu and
RT IroN.";
RL Microbiology 149:2557-2570(2003).
RN [11]
RP FUNCTION.
RX PubMed=16718603; DOI=10.1007/s10534-005-4452-9;
RA Destoumieux-Garzon D., Peduzzi J., Thomas X., Djediat C., Rebuffat S.;
RT "Parasitism of iron-siderophore receptors of Escherichia coli by the
RT siderophore-peptide microcin E492m and its unmodified counterpart.";
RL BioMetals 19:181-191(2006).
CC -!- FUNCTION: Involved in the active transport across the outer membrane of
CC iron complexed with catecholate siderophores such as
CC dihydroxybenzoylserine and dihydroxybenzoate. It derives its energy for
CC transport by interacting with the trans-periplasmic membrane protein
CC TonB. Can also transport catechol-substituted cephalosporins. Receptor
CC for microcins M, H47 and E492. {ECO:0000269|PubMed:12949180,
CC ECO:0000269|PubMed:16718603, ECO:0000269|PubMed:2139424,
CC ECO:0000269|PubMed:2407721, ECO:0000269|PubMed:3072926}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane.
CC -!- INDUCTION: Repressed by iron. {ECO:0000269|PubMed:10411720,
CC ECO:0000269|PubMed:1804764, ECO:0000269|PubMed:3072926}.
CC -!- SIMILARITY: Belongs to the TonB-dependent receptor family.
CC {ECO:0000305}.
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DR EMBL; U00096; AAC73892.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35471.1; -; Genomic_DNA.
DR PIR; E64817; E64817.
DR RefSeq; NP_415326.1; NC_000913.3.
DR RefSeq; WP_000430057.1; NZ_STEB01000019.1.
DR PDB; 6BPM; X-ray; 2.50 A; A/C=34-760.
DR PDB; 6BPN; X-ray; 2.10 A; A=34-760.
DR PDB; 6BPO; X-ray; 2.90 A; A/B/C/D=34-760.
DR PDBsum; 6BPM; -.
DR PDBsum; 6BPN; -.
DR PDBsum; 6BPO; -.
DR AlphaFoldDB; P75780; -.
DR SMR; P75780; -.
DR BioGRID; 4259972; 125.
DR ComplexPortal; CPX-3580; fiu outer membrane transporter complex.
DR DIP; DIP-11432N; -.
DR IntAct; P75780; 4.
DR STRING; 511145.b0805; -.
DR DrugBank; DB14879; Cefiderocol.
DR TCDB; 1.B.14.1.9; the outer membrane receptor (omr) family.
DR PaxDb; P75780; -.
DR PRIDE; P75780; -.
DR EnsemblBacteria; AAC73892; AAC73892; b0805.
DR EnsemblBacteria; BAA35471; BAA35471; BAA35471.
DR GeneID; 946246; -.
DR KEGG; ecj:JW0790; -.
DR KEGG; eco:b0805; -.
DR PATRIC; fig|1411691.4.peg.1473; -.
DR EchoBASE; EB3101; -.
DR eggNOG; COG4774; Bacteria.
DR HOGENOM; CLU_008287_9_1_6; -.
DR InParanoid; P75780; -.
DR OMA; TWGSDQT; -.
DR PhylomeDB; P75780; -.
DR BioCyc; EcoCyc:G6414-MON; -.
DR BioCyc; MetaCyc:G6414-MON; -.
DR PRO; PR:P75780; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IBA:GO_Central.
DR GO; GO:0045203; C:integral component of cell outer membrane; IDA:EcoCyc.
DR GO; GO:0016020; C:membrane; IC:ComplexPortal.
DR GO; GO:1902495; C:transmembrane transporter complex; IC:ComplexPortal.
DR GO; GO:0015344; F:siderophore uptake transmembrane transporter activity; IDA:EcoCyc.
DR GO; GO:0038023; F:signaling receptor activity; IEA:InterPro.
DR GO; GO:0055072; P:iron ion homeostasis; IC:ComplexPortal.
DR GO; GO:0042884; P:microcin transport; IMP:EcoliWiki.
DR GO; GO:0015891; P:siderophore transport; IMP:EcoliWiki.
DR GO; GO:0033214; P:siderophore-dependent iron import into cell; IDA:EcoCyc.
DR Gene3D; 2.170.130.10; -; 1.
DR Gene3D; 2.40.170.20; -; 1.
DR InterPro; IPR030148; Fiu.
DR InterPro; IPR012910; Plug_dom.
DR InterPro; IPR037066; Plug_dom_sf.
DR InterPro; IPR039423; TonB-dep_rcpt.
DR InterPro; IPR000531; TonB-dep_rcpt_b-brl.
DR InterPro; IPR010916; TonB_box_CS.
DR InterPro; IPR036942; TonB_rcpt_b-brl_sf.
DR InterPro; IPR010105; TonB_sidphr_rcpt.
DR PANTHER; PTHR32552; PTHR32552; 1.
DR PANTHER; PTHR32552:SF68; PTHR32552:SF68; 1.
DR Pfam; PF07715; Plug; 1.
DR Pfam; PF00593; TonB_dep_Rec; 1.
DR TIGRFAMs; TIGR01783; TonB-siderophor; 1.
DR PROSITE; PS00430; TONB_DEPENDENT_REC_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell outer membrane; Ion transport; Iron; Iron transport;
KW Membrane; Receptor; Reference proteome; Signal; TonB box; Transmembrane;
KW Transmembrane beta strand; Transport.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..760
FT /note="Catecholate siderophore receptor Fiu"
FT /id="PRO_0000034790"
FT MOTIF 743..760
FT /note="TonB C-terminal box"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:6BPN"
FT STRAND 71..79
FT /evidence="ECO:0007829|PDB:6BPN"
FT HELIX 80..85
FT /evidence="ECO:0007829|PDB:6BPN"
FT HELIX 91..94
FT /evidence="ECO:0007829|PDB:6BPN"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:6BPN"
FT STRAND 102..105
FT /evidence="ECO:0007829|PDB:6BPN"
FT STRAND 117..120
FT /evidence="ECO:0007829|PDB:6BPN"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:6BPN"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:6BPN"
FT STRAND 147..155
FT /evidence="ECO:0007829|PDB:6BPN"
FT HELIX 158..161
FT /evidence="ECO:0007829|PDB:6BPN"
FT STRAND 168..174
FT /evidence="ECO:0007829|PDB:6BPN"
FT STRAND 182..190
FT /evidence="ECO:0007829|PDB:6BPN"
FT HELIX 191..193
FT /evidence="ECO:0007829|PDB:6BPN"
FT STRAND 194..204
FT /evidence="ECO:0007829|PDB:6BPN"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:6BPN"
FT STRAND 210..221
FT /evidence="ECO:0007829|PDB:6BPN"
FT STRAND 225..227
FT /evidence="ECO:0007829|PDB:6BPN"
FT STRAND 229..242
FT /evidence="ECO:0007829|PDB:6BPN"
FT STRAND 245..261
FT /evidence="ECO:0007829|PDB:6BPN"
FT HELIX 279..285
FT /evidence="ECO:0007829|PDB:6BPN"
FT STRAND 302..319
FT /evidence="ECO:0007829|PDB:6BPN"
FT STRAND 322..343
FT /evidence="ECO:0007829|PDB:6BPN"
FT HELIX 346..348
FT /evidence="ECO:0007829|PDB:6BPN"
FT STRAND 352..355
FT /evidence="ECO:0007829|PDB:6BPN"
FT HELIX 356..358
FT /evidence="ECO:0007829|PDB:6BPN"
FT STRAND 360..387
FT /evidence="ECO:0007829|PDB:6BPN"
FT STRAND 390..407
FT /evidence="ECO:0007829|PDB:6BPN"
FT STRAND 418..422
FT /evidence="ECO:0007829|PDB:6BPN"
FT STRAND 439..455
FT /evidence="ECO:0007829|PDB:6BPN"
FT STRAND 457..480
FT /evidence="ECO:0007829|PDB:6BPN"
FT STRAND 485..487
FT /evidence="ECO:0007829|PDB:6BPN"
FT STRAND 500..538
FT /evidence="ECO:0007829|PDB:6BPN"
FT TURN 540..544
FT /evidence="ECO:0007829|PDB:6BPM"
FT STRAND 552..554
FT /evidence="ECO:0007829|PDB:6BPM"
FT STRAND 564..577
FT /evidence="ECO:0007829|PDB:6BPN"
FT TURN 578..581
FT /evidence="ECO:0007829|PDB:6BPN"
FT STRAND 582..594
FT /evidence="ECO:0007829|PDB:6BPN"
FT STRAND 601..603
FT /evidence="ECO:0007829|PDB:6BPM"
FT STRAND 611..625
FT /evidence="ECO:0007829|PDB:6BPN"
FT STRAND 628..640
FT /evidence="ECO:0007829|PDB:6BPN"
FT STRAND 651..654
FT /evidence="ECO:0007829|PDB:6BPM"
FT STRAND 660..670
FT /evidence="ECO:0007829|PDB:6BPN"
FT STRAND 672..684
FT /evidence="ECO:0007829|PDB:6BPN"
FT STRAND 695..697
FT /evidence="ECO:0007829|PDB:6BPM"
FT STRAND 699..701
FT /evidence="ECO:0007829|PDB:6BPN"
FT STRAND 704..716
FT /evidence="ECO:0007829|PDB:6BPN"
FT STRAND 719..727
FT /evidence="ECO:0007829|PDB:6BPN"
FT STRAND 734..737
FT /evidence="ECO:0007829|PDB:6BPN"
FT STRAND 739..746
FT /evidence="ECO:0007829|PDB:6BPN"
FT STRAND 751..759
FT /evidence="ECO:0007829|PDB:6BPN"
SQ SEQUENCE 760 AA; 81960 MW; 1B66B9C2EF68C7CA CRC64;
MENNRNFPAR QFHSLTFFAG LCIGITPVAQ ALAAEGQTNA DDTLVVEAST PSLYAPQQSA
DPKFSRPVAD TTRTMTVISE QVIKDQGATN LTDALKNVPG VGAFFAGENG NSTTGDAIYM
RGADTSNSIY IDGIRDIGSV SRDTFNTEQV EVIKGPSGTD YGRSAPTGSI NMISKQPRND
SGIDASASIG SAWFRRGTLD VNQVIGDTTA VRLNVMGEKT HDAGRDKVKN ERYGVAPSVA
FGLGTANRLY LNYLHVTQHN TPDGGIPTIG LPGYSAPSAG TAALNHSGKV DTHNFYGTDS
DYDDSTTDTA TMRFEHDIND NTTIRNTTRW SRVKQDYLMT AIMGGASNIT QPTSDVNSWT
WSRTANTKDV SNKILTNQTN LTSTFYTGSI GHDVSTGVEF TRETQTNYGV NPVTLPAVNI
YHPDSSIHPG GLTRNGANAN GQTDTFAIYA FDTLQITRDF ELNGGIRLDN YHTEYDSATA
CGGSGRGAIT CPTGVAKGSP VTTVDTAKSG NLMNWKAGAL YHLTENGNVY INYAVSQQPP
GGNNFALAQS GSGNSANRTD FKPQKANTSE IGTKWQVLDK RLLLTAALFR TDIENEVEQN
DDGTYSQYGK KRVEGYEISV AGNITPAWQV IGGYTQQKAT IKNGKDVAQD GSSSLPYTPE
HAFTLWSQYQ ATDDISVGAG ARYIGSMHKG SDGAVGTPAF TEGYWVADAK LGYRVNRNLD
FQLNVYNLFD TDYVASINKS GYRYHPGEPR TFLLTANMHF
