FBP_NEIGO
ID FBP_NEIGO Reviewed; 330 AA.
AC P17259;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Major ferric iron-binding protein;
DE Short=FBP;
DE AltName: Full=Major iron-regulated protein;
DE Short=MIRP;
DE Flags: Precursor;
GN Name=fbp;
OS Neisseria gonorrhoeae.
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=485;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=ATCC 33084 / F62 / M-1914;
RX PubMed=2110241; DOI=10.1084/jem.171.5.1535;
RA Berish S.A., Mietzner T.A., Mayer L.W., Genco C.A., Holloway B.P.,
RA Morse S.A.;
RT "Molecular cloning and characterization of the structural gene for the
RT major iron-regulated protein expressed by Neisseria gonorrhoeae.";
RL J. Exp. Med. 171:1535-1546(1990).
RN [2]
RP PROTEIN SEQUENCE OF 23-69.
RX PubMed=3559476; DOI=10.1084/jem.165.4.1041;
RA Mietzner T.A., Bolan G., Schoolnik G.K., Morse S.A.;
RT "Purification and characterization of the major iron-regulated protein
RT expressed by pathogenic Neisseriae.";
RL J. Exp. Med. 165:1041-1057(1987).
CC -!- FUNCTION: This protein may be a central component in the iron-
CC acquisition system.
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- INDUCTION: By iron deprivation.
CC -!- MISCELLANEOUS: Iron co-purifies with FBP and is bound by the protein as
CC a Fe(3+) ion at an approximate molar ratio of 1:1.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 1 family.
CC {ECO:0000305}.
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DR EMBL; X51901; CAA36182.1; -; Genomic_DNA.
DR PIR; S10256; S10256.
DR PDB; 1R1N; X-ray; 1.74 A; A/B/C/D/E/F/G/H/I=23-330.
DR PDB; 1XC1; X-ray; 1.51 A; A/B/C/D/E/F/G/H/I=23-330.
DR PDB; 3TYH; X-ray; 2.10 A; A/B/C/D/E/F/G/H/I=23-330.
DR PDBsum; 1R1N; -.
DR PDBsum; 1XC1; -.
DR PDBsum; 3TYH; -.
DR AlphaFoldDB; P17259; -.
DR SMR; P17259; -.
DR EvolutionaryTrace; P17259; -.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR GO; GO:0055072; P:iron ion homeostasis; IEA:UniProtKB-KW.
DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR InterPro; IPR026045; Ferric-bd.
DR InterPro; IPR006059; SBP.
DR InterPro; IPR006061; SBP_1_CS.
DR Pfam; PF01547; SBP_bac_1; 1.
DR PIRSF; PIRSF002825; CfbpA; 1.
DR PROSITE; PS01037; SBP_BACTERIAL_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Ion transport; Iron;
KW Iron transport; Metal-binding; Periplasm; Signal; Transport.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:3559476"
FT CHAIN 23..330
FT /note="Major ferric iron-binding protein"
FT /id="PRO_0000031690"
FT BINDING 31
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 79
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 217
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 218
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT STRAND 24..28
FT /evidence="ECO:0007829|PDB:1XC1"
FT HELIX 32..46
FT /evidence="ECO:0007829|PDB:1XC1"
FT STRAND 50..54
FT /evidence="ECO:0007829|PDB:1XC1"
FT HELIX 57..65
FT /evidence="ECO:0007829|PDB:1XC1"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:1R1N"
FT STRAND 74..79
FT /evidence="ECO:0007829|PDB:1XC1"
FT HELIX 81..89
FT /evidence="ECO:0007829|PDB:1XC1"
FT HELIX 98..103
FT /evidence="ECO:0007829|PDB:1XC1"
FT STRAND 118..130
FT /evidence="ECO:0007829|PDB:1XC1"
FT TURN 131..133
FT /evidence="ECO:0007829|PDB:1XC1"
FT HELIX 136..138
FT /evidence="ECO:0007829|PDB:1XC1"
FT HELIX 143..146
FT /evidence="ECO:0007829|PDB:1XC1"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:1XC1"
FT TURN 152..154
FT /evidence="ECO:0007829|PDB:1XC1"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:1XC1"
FT HELIX 162..175
FT /evidence="ECO:0007829|PDB:1XC1"
FT HELIX 177..190
FT /evidence="ECO:0007829|PDB:1XC1"
FT STRAND 191..193
FT /evidence="ECO:0007829|PDB:1XC1"
FT HELIX 197..205
FT /evidence="ECO:0007829|PDB:1XC1"
FT STRAND 208..215
FT /evidence="ECO:0007829|PDB:1XC1"
FT HELIX 216..226
FT /evidence="ECO:0007829|PDB:1XC1"
FT HELIX 228..230
FT /evidence="ECO:0007829|PDB:1XC1"
FT STRAND 233..236
FT /evidence="ECO:0007829|PDB:1XC1"
FT HELIX 243..245
FT /evidence="ECO:0007829|PDB:1XC1"
FT STRAND 247..254
FT /evidence="ECO:0007829|PDB:1XC1"
FT HELIX 260..271
FT /evidence="ECO:0007829|PDB:1XC1"
FT HELIX 273..279
FT /evidence="ECO:0007829|PDB:1XC1"
FT TURN 280..282
FT /evidence="ECO:0007829|PDB:1XC1"
FT STRAND 286..289
FT /evidence="ECO:0007829|PDB:1XC1"
FT HELIX 301..303
FT /evidence="ECO:0007829|PDB:1XC1"
FT HELIX 314..327
FT /evidence="ECO:0007829|PDB:1XC1"
SQ SEQUENCE 330 AA; 35769 MW; 2BE257D269CA1C28 CRC64;
MKTSIRYALL AAALTAATPA LADITVYNGQ HKEAAQAVAD AFTRATGIKV KLNSAKGDQL
AGQIKEEGSR SPADVFYSEQ IPALATLSAA NLLEPLPAST INETRGKGVP VAAKKDWVAL
SGRSRVVVYD TRKLSEKDLE KSVLNYATPK WKNRIGYVPT SGAFLEQIVA IVKLKGEAAA
LKWLKGLKEY GKPYAKNSVA LQAVENGEID AALINNYYWH AFAREKGVQN VHTRLNFVRH
RDPGALVTYS GAVLKSSQNK DEAKKFVAFL AGKEGQRALT AVRAEYPLNP HVVSTFNLEP
IAKLEAPQVS ATTVSEKEHA TRLLEQAGMK
