FUTA1_SYNY3
ID FUTA1_SYNY3 Reviewed; 360 AA.
AC P72827;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Iron uptake protein A1;
DE Flags: Precursor;
GN Name=futA1; OrderedLocusNames=slr1295;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
RN [2]
RP ROLE IN IRON TRANSPORT (FE(3+)), DISRUPTION PHENOTYPE, AND INDUCTION.
RX PubMed=11292796; DOI=10.1128/jb.183.9.2779-2784.2001;
RA Katoh H., Hagino N., Grossman A.R., Ogawa T.;
RT "Genes essential to iron transport in the cyanobacterium Synechocystis sp.
RT strain PCC 6803.";
RL J. Bacteriol. 183:2779-2784(2001).
RN [3]
RP IRON-BINDING (FE(3+)).
RX PubMed=11522907; DOI=10.1093/pcp/pce106;
RA Katoh H., Hagino N., Ogawa T.;
RT "Iron-binding activity of FutA1 subunit of an ABC-type iron transporter in
RT the cyanobacterium Synechocystis sp. strain PCC 6803.";
RL Plant Cell Physiol. 42:823-827(2001).
RN [4]
RP PROBABLE ROLE IN PHOTOSYSTEM II PROTECTION, INDUCTION, DISRUPTION
RP PHENOTYPE, AND SUBCELLULAR LOCATION IN THYLAKOID LUMEN.
RX PubMed=12368463; DOI=10.1099/00221287-148-10-3293;
RA Toelle J., Michel K.-P., Kruip J., Kahmann U., Preisfeld A.,
RA Pistorius E.K.;
RT "Localization and function of the IdiA homologue Slr1295 in the
RT cyanobacterium Synechocystis sp. strain PCC 6803.";
RL Microbiology 148:3293-3305(2002).
RN [5]
RP SUBCELLULAR LOCATION IN THYLAKOID.
RX PubMed=16287171; DOI=10.1002/pmic.200500111;
RA Srivastava R., Pisareva T., Norling B.;
RT "Proteomic studies of the thylakoid membrane of Synechocystis sp. PCC
RT 6803.";
RL Proteomics 5:4905-4916(2005).
RN [6]
RP SUBCELLULAR LOCATION TO PLASMA MEMBRANE.
RX PubMed=16400685; DOI=10.1002/pmic.200500114;
RA Huang F., Fulda S., Hagemann M., Norling B.;
RT "Proteomic screening of salt-stress-induced changes in plasma membranes of
RT Synechocystis sp. strain PCC 6803.";
RL Proteomics 6:910-920(2006).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 30-360 IN THE PRESENCE AND ABSENCE
RP OF FE(2+).
RX PubMed=17626019; DOI=10.1074/jbc.m704136200;
RA Koropatkin N., Randich A.M., Bhattacharyya-Pakrasi M., Pakrasi H.B.,
RA Smith T.J.;
RT "The structure of the iron-binding protein, FutA1, from Synechocystis
RT 6803.";
RL J. Biol. Chem. 282:27468-27477(2007).
CC -!- FUNCTION: Plays an important role in protecting the acceptor side of
CC photosystem II (PSII) against oxidative damage, especially under iron-
CC limiting growth conditions (Probable). The differing subcellular
CC locations of futA1 (predominantly thylakoid lumen) and futA2
CC (predominantly periplasmic) suggest they may fulfill different roles.
CC {ECO:0000269|PubMed:11292796, ECO:0000305}.
CC -!- FUNCTION: A major iron-binding protein involved in Fe(3+) uptake,
CC probably part of a periplasmic ABC transporter complex futA1A2BC (TC
CC 3.A.1.10.2) involved in Fe(3+) ion import (ferric iron). This protein
CC and futA2 (slr0531) may be subunit proteins that have redundant or
CC overlapping substrate-binding functions (Probable).
CC {ECO:0000305|PubMed:11292796}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000305}; Lipid-
CC anchor {ECO:0000305}. Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}. Note=Localization to the periplasm was not detected in
CC PubMed:12368463. {ECO:0000269|PubMed:12368463,
CC ECO:0000269|PubMed:16287171, ECO:0000269|PubMed:16400685}.
CC -!- INDUCTION: Transcript levels increase when cells are grown in the
CC absence of iron. Protein levels increase when cells are grown in the
CC absence of iron. {ECO:0000269|PubMed:11292796,
CC ECO:0000269|PubMed:12368463}.
CC -!- DISRUPTION PHENOTYPE: Cells grow normally in the absence of iron but
CC have a reduced capacity for Fe(3+) uptake; double knockouts of this
CC gene and futA2 (slr0531) grow very poorly in the absence of iron and
CC have a marked reduction in their ability to take up Fe(3+).
CC {ECO:0000269|PubMed:11292796, ECO:0000269|PubMed:12368463}.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 1 family.
CC {ECO:0000305}.
CC -!- CAUTION: There is controversy as to whether this protein preferentially
CC binds Fe(2+) or Fe(3+), and also whether it is found associated with
CC the plasma membrane or not. {ECO:0000305}.
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DR EMBL; BA000022; BAA16842.1; -; Genomic_DNA.
DR PIR; S74691; S74691.
DR PDB; 2PT1; X-ray; 2.00 A; A=30-360.
DR PDB; 2PT2; X-ray; 2.00 A; A=30-360.
DR PDB; 3F11; X-ray; 2.00 A; A=30-360.
DR PDBsum; 2PT1; -.
DR PDBsum; 2PT2; -.
DR PDBsum; 3F11; -.
DR AlphaFoldDB; P72827; -.
DR SMR; P72827; -.
DR STRING; 1148.1651916; -.
DR TCDB; 3.A.1.10.2; the atp-binding cassette (abc) superfamily.
DR PaxDb; P72827; -.
DR EnsemblBacteria; BAA16842; BAA16842; BAA16842.
DR KEGG; syn:slr1295; -.
DR eggNOG; COG1840; Bacteria.
DR InParanoid; P72827; -.
DR OMA; TLPYNTE; -.
DR PhylomeDB; P72827; -.
DR EvolutionaryTrace; P72827; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0031676; C:plasma membrane-derived thylakoid membrane; 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 InterPro; IPR026045; Ferric-bd.
DR InterPro; IPR006059; SBP.
DR Pfam; PF13416; SBP_bac_8; 1.
DR PIRSF; PIRSF002825; CfbpA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Ion transport; Iron; Iron transport;
KW Lipoprotein; Membrane; Metal-binding; Palmitate; Reference proteome;
KW Signal; Thylakoid; Transport.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..360
FT /note="Iron uptake protein A1"
FT /id="PRO_0000352735"
FT BINDING 54
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT BINDING 55
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT BINDING 185
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT BINDING 241
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT BINDING 242
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT LIPID 29
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT LIPID 29
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255"
FT STRAND 46..52
FT /evidence="ECO:0007829|PDB:2PT1"
FT HELIX 58..69
FT /evidence="ECO:0007829|PDB:2PT1"
FT STRAND 72..77
FT /evidence="ECO:0007829|PDB:2PT1"
FT HELIX 80..90
FT /evidence="ECO:0007829|PDB:2PT1"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:2PT1"
FT STRAND 98..103
FT /evidence="ECO:0007829|PDB:2PT1"
FT HELIX 104..112
FT /evidence="ECO:0007829|PDB:2PT1"
FT HELIX 122..127
FT /evidence="ECO:0007829|PDB:2PT1"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:2PT1"
FT STRAND 140..152
FT /evidence="ECO:0007829|PDB:2PT1"
FT TURN 153..155
FT /evidence="ECO:0007829|PDB:2PT1"
FT HELIX 158..160
FT /evidence="ECO:0007829|PDB:2PT1"
FT HELIX 165..168
FT /evidence="ECO:0007829|PDB:2PT1"
FT HELIX 170..172
FT /evidence="ECO:0007829|PDB:2PT1"
FT HELIX 184..197
FT /evidence="ECO:0007829|PDB:2PT1"
FT HELIX 199..211
FT /evidence="ECO:0007829|PDB:2PT1"
FT STRAND 213..215
FT /evidence="ECO:0007829|PDB:2PT1"
FT HELIX 221..230
FT /evidence="ECO:0007829|PDB:2PT1"
FT STRAND 234..239
FT /evidence="ECO:0007829|PDB:2PT1"
FT HELIX 240..247
FT /evidence="ECO:0007829|PDB:2PT1"
FT HELIX 252..259
FT /evidence="ECO:0007829|PDB:2PT1"
FT STRAND 261..264
FT /evidence="ECO:0007829|PDB:2PT1"
FT TURN 268..271
FT /evidence="ECO:0007829|PDB:2PT1"
FT STRAND 275..283
FT /evidence="ECO:0007829|PDB:2PT1"
FT HELIX 289..299
FT /evidence="ECO:0007829|PDB:2PT1"
FT HELIX 302..312
FT /evidence="ECO:0007829|PDB:2PT1"
FT STRAND 315..318
FT /evidence="ECO:0007829|PDB:2PT1"
FT HELIX 325..328
FT /evidence="ECO:0007829|PDB:2PT1"
FT HELIX 340..342
FT /evidence="ECO:0007829|PDB:2PT1"
FT HELIX 344..346
FT /evidence="ECO:0007829|PDB:2PT1"
FT HELIX 347..357
FT /evidence="ECO:0007829|PDB:2PT1"
SQ SEQUENCE 360 AA; 39370 MW; E2748CB06E3765C7 CRC64;
MVQKLSRRLF LSIGTAFTVV VGSQLLSSCG QSPDAPIADT PGEQQEINLY SSRHYNTDNE
LYAKFTAETG IKVNLIEGKA DELLERIKSE GANSPADVLL TVDLARLWRA EEDGIFQPVQ
SEILETNVPE YLRSPDGMWF GFTKRARVIM YNKGKVKPEE LSTYEELADP KWKGRVIIRS
SSNEYNQSLV ASLVVADGEE STLAWAKGFV SNFAREPQGN DTAQIEAVSS GEADLTLANT
YYMGRLLESE DPAQKAIAEN VGVFFPNQEG RGTHVNVSGV GVVKTAPNRE GAVKFIEFLV
SEPAQAFLAQ NNYEYPVLAG VPLNKSVASF GEFKSDTTSL DKLGPALAPA TKIMNEAGWK
