FUTA2_SYNY3
ID FUTA2_SYNY3 Reviewed; 346 AA.
AC Q55835;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Iron uptake protein A2;
DE AltName: Full=Iron deficiency-induced protein A;
DE AltName: Full=PP2;
DE Flags: Precursor;
GN Name=futA2; Synonyms=idiA; OrderedLocusNames=slr0513;
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 PROTEIN SEQUENCE OF 140-155 AND 178-188, AND SUBCELLULAR LOCATION IN
RP PERIPLASM.
RX PubMed=10201099; DOI=10.1007/s002030050702;
RA Fulda S., Mikkat S., Schroeder W., Hagemann M.;
RT "Isolation of salt-induced periplasmic proteins from Synechocystis sp.
RT strain PCC 6803.";
RL Arch. Microbiol. 171:214-217(1999).
RN [3]
RP SUBCELLULAR LOCATION IN PERIPLASM, AND INDUCTION.
RX PubMed=10998049; DOI=10.1046/j.1432-1327.2000.01642.x;
RA Fulda S., Huang F., Nilsson F., Hagemann M., Norling B.;
RT "Proteomics of Synechocystis sp. strain PCC 6803. Identification of
RT periplasmic proteins in cells grown at low and high salt concentrations.";
RL Eur. J. Biochem. 267:5900-5907(2000).
RN [4]
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 [5]
RP INDUCTION, AND SUBCELLULAR LOCATION IN PERIPLASM AND 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 [6]
RP SUBCELLULAR LOCATION IN THYLAKOID LUMEN.
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 [7]
RP IRON-BINDING IN THE PERIPLASM (FE(3+)), AND ROLE IN COPPER SUPPLY FOR
RP THYLAKOID PROTEINS.
RX PubMed=17148438; DOI=10.1074/jbc.m609916200;
RA Waldron K.J., Tottey S., Yanagisawa S., Dennison C., Robinson N.J.;
RT "A periplasmic iron-binding protein contributes toward inward copper
RT supply.";
RL J. Biol. Chem. 282:3837-3846(2007).
RN [8]
RP BINDING 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).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 32-346 IN THE PRESENCE AND ABSENCE
RP OF FE(3+), AND PREFERENCE FOR FE(3+) OVER FE(2+).
RX PubMed=18252722; DOI=10.1074/jbc.m709907200;
RA Badarau A., Firbank S.J., Waldron K.J., Yanagisawa S., Robinson N.J.,
RA Banfield M.J., Dennison C.;
RT "FutA2 is a ferric binding protein from Synechocystis PCC 6803.";
RL J. Biol. Chem. 283:12520-12527(2008).
CC -!- FUNCTION: Probably part of a periplasmic ABC transporter complex
CC futA1A2BC (TC 3.A.1.10.2) involved in Fe(3+) ion import (ferric iron).
CC This protein and futA1 (slr1295) are subunit proteins that have
CC redundant or overlapping substrate-binding functions (Probable). The
CC differing subcellular locations of futA1 (predominantly thylakoid
CC lumen) and futA2 (predominantly periplasmic) suggest they may fulfill
CC different roles. {ECO:0000305}.
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. {ECO:0000305}.
CC -!- FUNCTION: Plays an undefined role in copper supply to thylakoid
CC proteins.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000305};
CC Peripheral membrane protein {ECO:0000305}; Lumenal side {ECO:0000305}.
CC Periplasm. Note=Binds Fe(3+) in the periplasm.
CC -!- INDUCTION: Transcript levels increase when cells are grown in the
CC absence of iron. Periplasmic levels increase when cells are grown in
CC high NaCl or in the absence of iron. {ECO:0000269|PubMed:10998049,
CC ECO:0000269|PubMed:11292796, ECO:0000269|PubMed:12368463}.
CC -!- PTM: Predicted to be exported by the Tat system. The position of the
CC signal peptide cleavage has not been experimentally proven.
CC -!- DISRUPTION PHENOTYPE: Cells grow normally in the absence of iron;
CC double knockouts of this gene and futA1 (slr1295) grow very poorly in
CC the absence of iron and have a marked reduction in their ability to
CC take up Fe(3+). {ECO:0000269|PubMed:11292796}.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 1 family.
CC {ECO:0000305}.
CC -!- CAUTION: There is some controversy as to whether this protein
CC preferentially binds Fe(2+) or Fe(3+). {ECO:0000305}.
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DR EMBL; BA000022; BAA10591.1; -; Genomic_DNA.
DR PIR; S76647; S76647.
DR PDB; 2VOZ; X-ray; 1.70 A; A/B=1-346.
DR PDB; 2VP1; X-ray; 2.70 A; A/B=1-346.
DR PDBsum; 2VOZ; -.
DR PDBsum; 2VP1; -.
DR AlphaFoldDB; Q55835; -.
DR SMR; Q55835; -.
DR IntAct; Q55835; 1.
DR STRING; 1148.1001753; -.
DR TCDB; 3.A.1.10.2; the atp-binding cassette (abc) superfamily.
DR PaxDb; Q55835; -.
DR EnsemblBacteria; BAA10591; BAA10591; BAA10591.
DR KEGG; syn:slr0513; -.
DR eggNOG; COG1840; Bacteria.
DR InParanoid; Q55835; -.
DR OMA; HPYNVSL; -.
DR PhylomeDB; Q55835; -.
DR EvolutionaryTrace; Q55835; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; HDA:UniProtKB.
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 InterPro; IPR006311; TAT_signal.
DR Pfam; PF13416; SBP_bac_8; 1.
DR PIRSF; PIRSF002825; CfbpA; 1.
DR PROSITE; PS51318; TAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Ion transport; Iron;
KW Iron transport; Membrane; Metal-binding; Periplasm; Reference proteome;
KW Signal; Thylakoid; Transport.
FT SIGNAL 1..31
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT CHAIN 32..346
FT /note="Iron uptake protein A2"
FT /id="PRO_0000352736"
FT BINDING 43
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT BINDING 44
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT BINDING 169
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT BINDING 225
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT BINDING 226
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT STRAND 35..41
FT /evidence="ECO:0007829|PDB:2VOZ"
FT HELIX 47..54
FT /evidence="ECO:0007829|PDB:2VOZ"
FT STRAND 55..61
FT /evidence="ECO:0007829|PDB:2VOZ"
FT HELIX 64..73
FT /evidence="ECO:0007829|PDB:2VOZ"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:2VOZ"
FT STRAND 81..87
FT /evidence="ECO:0007829|PDB:2VOZ"
FT HELIX 88..96
FT /evidence="ECO:0007829|PDB:2VOZ"
FT HELIX 106..111
FT /evidence="ECO:0007829|PDB:2VOZ"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:2VOZ"
FT STRAND 124..136
FT /evidence="ECO:0007829|PDB:2VOZ"
FT TURN 137..139
FT /evidence="ECO:0007829|PDB:2VOZ"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:2VOZ"
FT HELIX 149..152
FT /evidence="ECO:0007829|PDB:2VOZ"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:2VOZ"
FT TURN 157..159
FT /evidence="ECO:0007829|PDB:2VOZ"
FT HELIX 168..181
FT /evidence="ECO:0007829|PDB:2VOZ"
FT HELIX 183..195
FT /evidence="ECO:0007829|PDB:2VOZ"
FT STRAND 197..200
FT /evidence="ECO:0007829|PDB:2VOZ"
FT HELIX 205..213
FT /evidence="ECO:0007829|PDB:2VOZ"
FT STRAND 218..223
FT /evidence="ECO:0007829|PDB:2VOZ"
FT HELIX 224..232
FT /evidence="ECO:0007829|PDB:2VOZ"
FT HELIX 236..244
FT /evidence="ECO:0007829|PDB:2VOZ"
FT STRAND 245..248
FT /evidence="ECO:0007829|PDB:2VOZ"
FT STRAND 261..269
FT /evidence="ECO:0007829|PDB:2VOZ"
FT HELIX 275..285
FT /evidence="ECO:0007829|PDB:2VOZ"
FT HELIX 288..296
FT /evidence="ECO:0007829|PDB:2VOZ"
FT TURN 297..299
FT /evidence="ECO:0007829|PDB:2VOZ"
FT STRAND 301..304
FT /evidence="ECO:0007829|PDB:2VOZ"
FT HELIX 311..314
FT /evidence="ECO:0007829|PDB:2VOZ"
FT HELIX 327..331
FT /evidence="ECO:0007829|PDB:2VOZ"
FT HELIX 333..342
FT /evidence="ECO:0007829|PDB:2VOZ"
SQ SEQUENCE 346 AA; 38156 MW; 921000C065E5CD3E CRC64;
MTTKISRRTF FVGGTALTAL VVANLPRRAS AQSRTINLYS SRHYNTDDAL YDAFGEVNLI
EASAEELIER IQSEGANSPG DILFTVDAGM LWRAEQAGLF QPVRSGKLNE RIPENLRHPD
GLWYGFTQRA RVLYYSRDRV NPADLSTYEA LADPQWRGKI LVRPSSNVYN LSLTASRIAI
HGEPETRRWL QGLVGNFARQ PEGNDTAQIR AIAAGIGDVA IANSYYYIRL QKSTDPADQE
VVEKVSLFFP NTGSGERGTH VNVSGAGVLK NAPNRDAAIA FLEYLASDDA QRYFAEGNNE
YPVIPGVPID PVLAAHGQLK GDPLNVSNLG RYQPDSARLM NEVGWQ
