FECA_ECOLI
ID FECA_ECOLI Reviewed; 774 AA.
AC P13036; Q2M624;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Fe(3+) dicitrate transport protein FecA;
DE AltName: Full=Iron(III) dicitrate transport protein FecA;
DE Flags: Precursor;
GN Name=fecA; OrderedLocusNames=b4291, JW4251;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 34-40.
RC STRAIN=B;
RX PubMed=2836368; DOI=10.1128/jb.170.6.2716-2724.1988;
RA Pressler U., Staudenmaier H., Zimmermann L., Braun V.;
RT "Genetics of the iron dicitrate transport system of Escherichia coli.";
RL J. Bacteriol. 170:2716-2724(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-428.
RX PubMed=2254251; DOI=10.1128/jb.172.12.6749-6758.1990;
RA van Hove B., Staudenmaier H., Braun V.;
RT "Novel two-component transmembrane transcription control: regulation of
RT iron dicitrate transport in Escherichia coli K-12.";
RL J. Bacteriol. 172:6749-6758(1990).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 731-774.
RC STRAIN=K12;
RX PubMed=2651410; DOI=10.1128/jb.171.5.2626-2633.1989;
RA Staudenmaier H., van Hove B., Yaraghi Z., Braun V.;
RT "Nucleotide sequences of the fecBCDE genes and locations of the proteins
RT suggest a periplasmic-binding-protein-dependent transport mechanism for
RT iron(III) dicitrate in Escherichia coli.";
RL J. Bacteriol. 171:2626-2633(1989).
RN [7]
RP INDUCTION BY HYDROXYUREA.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=20005847; DOI=10.1016/j.molcel.2009.11.024;
RA Davies B.W., Kohanski M.A., Simmons L.A., Winkler J.A., Collins J.J.,
RA Walker G.C.;
RT "Hydroxyurea induces hydroxyl radical-mediated cell death in Escherichia
RT coli.";
RL Mol. Cell 36:845-860(2009).
CC -!- FUNCTION: FecA is the outer membrane receptor protein in the Fe(3+)
CC dicitrate transport system.
CC -!- INTERACTION:
CC P13036; P02929: tonB; NbExp=3; IntAct=EBI-1131517, EBI-6399993;
CC -!- SUBCELLULAR LOCATION: Cell outer membrane.
CC -!- INDUCTION: For induction, the TonB and the ExbB proteins have to be
CC active. Regulation by the iron level mediated by the Fur protein and
CC induction by citrate plus iron suggest that the Fe(3+) dicitrate
CC complex must enter the periplasm where it binds to a transmembrane
CC protein, which regulates transcription of the fec genes directly or via
CC a further inductor. Induced 2-fold by hydroxyurea (PubMed:20005847).
CC {ECO:0000269|PubMed:20005847}.
CC -!- SIMILARITY: Belongs to the TonB-dependent receptor family.
CC {ECO:0000305}.
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DR EMBL; M20981; AAA23760.1; -; Genomic_DNA.
DR EMBL; U14003; AAA97187.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77247.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78282.1; -; Genomic_DNA.
DR EMBL; M63115; AAA23768.1; -; Genomic_DNA.
DR EMBL; M26397; AAA23761.1; -; Genomic_DNA.
DR PIR; E65242; QRECFA.
DR RefSeq; NP_418711.1; NC_000913.3.
DR RefSeq; WP_000188283.1; NZ_LN832404.1.
DR PDB; 1KMO; X-ray; 2.00 A; A=1-774.
DR PDB; 1KMP; X-ray; 2.50 A; A=1-774.
DR PDB; 1PNZ; X-ray; 2.50 A; A=34-774.
DR PDB; 1PO0; X-ray; 2.15 A; A=34-774.
DR PDB; 1PO3; X-ray; 3.40 A; A/B=34-774.
DR PDB; 1ZZV; NMR; -; A=34-113.
DR PDB; 2D1U; NMR; -; A=34-129.
DR PDBsum; 1KMO; -.
DR PDBsum; 1KMP; -.
DR PDBsum; 1PNZ; -.
DR PDBsum; 1PO0; -.
DR PDBsum; 1PO3; -.
DR PDBsum; 1ZZV; -.
DR PDBsum; 2D1U; -.
DR AlphaFoldDB; P13036; -.
DR BMRB; P13036; -.
DR SMR; P13036; -.
DR BioGRID; 4261554; 298.
DR ComplexPortal; CPX-3576; Ferric-citrate outer membrane transporter complex.
DR DIP; DIP-9583N; -.
DR IntAct; P13036; 4.
DR STRING; 511145.b4291; -.
DR DrugBank; DB04147; Dodecyldimethylamine N-oxide.
DR DrugBank; DB04079; Heptane-1,2,3-Triol.
DR TCDB; 1.B.14.1.20; the outer membrane receptor (omr) family.
DR jPOST; P13036; -.
DR PaxDb; P13036; -.
DR PRIDE; P13036; -.
DR EnsemblBacteria; AAC77247; AAC77247; b4291.
DR EnsemblBacteria; BAE78282; BAE78282; BAE78282.
DR GeneID; 946427; -.
DR KEGG; ecj:JW4251; -.
DR KEGG; eco:b4291; -.
DR PATRIC; fig|1411691.4.peg.2408; -.
DR EchoBASE; EB0282; -.
DR eggNOG; COG4772; Bacteria.
DR HOGENOM; CLU_008287_17_1_6; -.
DR InParanoid; P13036; -.
DR OMA; IREDGPN; -.
DR PhylomeDB; P13036; -.
DR BioCyc; EcoCyc:EG10286-MON; -.
DR BioCyc; MetaCyc:EG10286-MON; -.
DR EvolutionaryTrace; P13036; -.
DR PHI-base; PHI:8006; -.
DR PRO; PR:P13036; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IDA:EcoCyc.
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; IEA:InterPro.
DR GO; GO:0038023; F:signaling receptor activity; IDA:EcoCyc.
DR GO; GO:0055072; P:iron ion homeostasis; IC:ComplexPortal.
DR GO; GO:0006826; P:iron ion transport; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:EcoCyc.
DR GO; GO:1990641; P:response to iron ion starvation; IMP:EcoCyc.
DR GO; GO:0033214; P:siderophore-dependent iron import into cell; IMP:EcoCyc.
DR GO; GO:0023019; P:signal transduction involved in regulation of gene expression; TAS:EcoCyc.
DR Gene3D; 2.170.130.10; -; 1.
DR Gene3D; 2.40.170.20; -; 1.
DR InterPro; IPR012910; Plug_dom.
DR InterPro; IPR037066; Plug_dom_sf.
DR InterPro; IPR011662; Secretin/TonB_short_N.
DR InterPro; IPR000531; TonB-dep_rcpt_b-brl.
DR InterPro; IPR010916; TonB_box_CS.
DR InterPro; IPR036942; TonB_rcpt_b-brl_sf.
DR InterPro; IPR010917; TonB_rcpt_CS.
DR InterPro; IPR010105; TonB_sidphr_rcpt.
DR Pfam; PF07715; Plug; 1.
DR Pfam; PF07660; STN; 1.
DR Pfam; PF00593; TonB_dep_Rec; 1.
DR SMART; SM00965; STN; 1.
DR TIGRFAMs; TIGR01783; TonB-siderophor; 1.
DR PROSITE; PS00430; TONB_DEPENDENT_REC_1; 1.
DR PROSITE; PS01156; TONB_DEPENDENT_REC_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell outer membrane; Direct protein sequencing;
KW Ion transport; Iron; Iron transport; Membrane; Receptor;
KW Reference proteome; Signal; TonB box; Transmembrane;
KW Transmembrane beta strand; Transport.
FT SIGNAL 1..33
FT /evidence="ECO:0000269|PubMed:2836368"
FT CHAIN 34..774
FT /note="Fe(3+) dicitrate transport protein FecA"
FT /id="PRO_0000034746"
FT MOTIF 56..63
FT /note="TonB box"
FT MOTIF 757..774
FT /note="TonB C-terminal box"
FT CONFLICT 16
FT /note="T -> A (in Ref. 1; AAA23760)"
FT /evidence="ECO:0000305"
FT CONFLICT 190
FT /note="A -> T (in Ref. 1; AAA23760)"
FT /evidence="ECO:0000305"
FT CONFLICT 300
FT /note="T -> M (in Ref. 1; AAA23760 and 5)"
FT /evidence="ECO:0000305"
FT CONFLICT 357
FT /note="W -> R (in Ref. 1; AAA23760)"
FT /evidence="ECO:0000305"
FT CONFLICT 444
FT /note="L -> V (in Ref. 1; AAA23760)"
FT /evidence="ECO:0000305"
FT CONFLICT 749
FT /note="R -> A (in Ref. 1; AAA23760)"
FT /evidence="ECO:0000305"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:1ZZV"
FT HELIX 43..54
FT /evidence="ECO:0007829|PDB:1ZZV"
FT TURN 62..65
FT /evidence="ECO:0007829|PDB:1ZZV"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:1ZZV"
FT HELIX 79..86
FT /evidence="ECO:0007829|PDB:1ZZV"
FT TURN 87..89
FT /evidence="ECO:0007829|PDB:1ZZV"
FT STRAND 93..98
FT /evidence="ECO:0007829|PDB:1ZZV"
FT STRAND 101..105
FT /evidence="ECO:0007829|PDB:1ZZV"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:1ZZV"
FT HELIX 127..131
FT /evidence="ECO:0007829|PDB:1KMO"
FT STRAND 137..141
FT /evidence="ECO:0007829|PDB:1KMO"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:1KMO"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:1KMO"
FT HELIX 153..157
FT /evidence="ECO:0007829|PDB:1KMO"
FT STRAND 174..177
FT /evidence="ECO:0007829|PDB:1KMP"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:1KMO"
FT STRAND 192..197
FT /evidence="ECO:0007829|PDB:1KMO"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:1KMO"
FT TURN 206..208
FT /evidence="ECO:0007829|PDB:1KMO"
FT HELIX 219..221
FT /evidence="ECO:0007829|PDB:1KMO"
FT STRAND 222..228
FT /evidence="ECO:0007829|PDB:1KMO"
FT TURN 233..235
FT /evidence="ECO:0007829|PDB:1KMO"
FT HELIX 240..242
FT /evidence="ECO:0007829|PDB:1KMO"
FT STRAND 244..249
FT /evidence="ECO:0007829|PDB:1KMO"
FT STRAND 257..266
FT /evidence="ECO:0007829|PDB:1KMO"
FT STRAND 276..286
FT /evidence="ECO:0007829|PDB:1KMO"
FT STRAND 290..302
FT /evidence="ECO:0007829|PDB:1KMO"
FT STRAND 305..308
FT /evidence="ECO:0007829|PDB:1KMO"
FT STRAND 311..322
FT /evidence="ECO:0007829|PDB:1KMO"
FT STRAND 324..342
FT /evidence="ECO:0007829|PDB:1KMO"
FT HELIX 349..354
FT /evidence="ECO:0007829|PDB:1KMO"
FT STRAND 365..379
FT /evidence="ECO:0007829|PDB:1KMO"
FT STRAND 385..404
FT /evidence="ECO:0007829|PDB:1KMO"
FT STRAND 407..410
FT /evidence="ECO:0007829|PDB:1KMO"
FT STRAND 413..430
FT /evidence="ECO:0007829|PDB:1KMO"
FT STRAND 433..456
FT /evidence="ECO:0007829|PDB:1KMO"
FT STRAND 459..461
FT /evidence="ECO:0007829|PDB:1KMO"
FT STRAND 465..467
FT /evidence="ECO:0007829|PDB:1KMP"
FT STRAND 469..490
FT /evidence="ECO:0007829|PDB:1KMO"
FT STRAND 493..510
FT /evidence="ECO:0007829|PDB:1KMO"
FT TURN 511..513
FT /evidence="ECO:0007829|PDB:1KMO"
FT STRAND 516..535
FT /evidence="ECO:0007829|PDB:1KMO"
FT STRAND 538..549
FT /evidence="ECO:0007829|PDB:1KMO"
FT HELIX 553..555
FT /evidence="ECO:0007829|PDB:1KMO"
FT HELIX 556..561
FT /evidence="ECO:0007829|PDB:1KMO"
FT STRAND 568..580
FT /evidence="ECO:0007829|PDB:1KMO"
FT STRAND 582..600
FT /evidence="ECO:0007829|PDB:1KMO"
FT STRAND 603..605
FT /evidence="ECO:0007829|PDB:1KMO"
FT STRAND 612..626
FT /evidence="ECO:0007829|PDB:1KMO"
FT HELIX 627..629
FT /evidence="ECO:0007829|PDB:1KMO"
FT HELIX 632..634
FT /evidence="ECO:0007829|PDB:1KMO"
FT STRAND 637..650
FT /evidence="ECO:0007829|PDB:1KMO"
FT STRAND 652..654
FT /evidence="ECO:0007829|PDB:1KMO"
FT TURN 655..658
FT /evidence="ECO:0007829|PDB:1KMO"
FT STRAND 666..675
FT /evidence="ECO:0007829|PDB:1KMO"
FT STRAND 680..689
FT /evidence="ECO:0007829|PDB:1KMO"
FT STRAND 706..709
FT /evidence="ECO:0007829|PDB:1KMO"
FT STRAND 714..724
FT /evidence="ECO:0007829|PDB:1KMO"
FT TURN 727..730
FT /evidence="ECO:0007829|PDB:1KMO"
FT STRAND 733..740
FT /evidence="ECO:0007829|PDB:1KMO"
FT STRAND 747..750
FT /evidence="ECO:0007829|PDB:1KMO"
FT STRAND 757..760
FT /evidence="ECO:0007829|PDB:1KMO"
FT STRAND 764..774
FT /evidence="ECO:0007829|PDB:1KMO"
SQ SEQUENCE 774 AA; 85322 MW; 16B5B510276C3B09 CRC64;
MTPLRVFRKT TPLVNTIRLS LLPLAGLSFS AFAAQVNIAP GSLDKALNQY AAHSGFTLSV
DASLTRGKQS NGLHGDYDVE SGLQQLLDGS GLQVKPLGNN SWTLEPAPAP KEDALTVVGD
WLGDARENDV FEHAGARDVI RREDFAKTGA TTMREVLNRI PGVSAPENNG TGSHDLAMNF
GIRGLNPRLA SRSTVLMDGI PVPFAPYGQP QLSLAPVSLG NMDAIDVVRG GGAVRYGPQS
VGGVVNFVTR AIPQDFGIEA GVEGQLSPTS SQNNPKETHN LMVGGTADNG FGTALLYSGT
RGSDWREHSA TRIDDLMLKS KYAPDEVHTF NSLLQYYDGE ADMPGGLSRA DYDADRWQST
RPYDRFWGRR KLASLGYQFQ PDSQHKFNIQ GFYTQTLRSG YLEQGKRITL SPRNYWVRGI
EPRYSQIFMI GPSAHEVGVG YRYLNESTHE MRYYTATSSG QLPSGSSPYD RDTRSGTEAH
AWYLDDKIDI GNWTITPGMR FEHIESYQNN AITGTHEEVS YNAPLPALNV LYHLTDSWNL
YANTEGSFGT VQYSQIGKAV QSGNVEPEKA RTWELGTRYD DGALTAEMGL FLINFNNQYD
SNQTNDTVTA RGKTRHTGLE TQARYDLGTL TPTLDNVSIY ASYAYVNAEI REKGDTYGNL
VPFSPKHKGT LGVDYKPGNW TFNLNSDFQS SQFADNANTV KESADGSTGR IPGFMLWGAR
VAYDFGPQMA DLNLAFGVKN IFDQDYFIRS YDDNNKGIYA GQPRTLYMQG SLKF
