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Database: UniProt
Entry: Q55835
LinkDB: Q55835
Original site: Q55835 
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   27-MAR-2024, entry version 135.
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; Cyanobacteriota; Cyanophyceae; Synechococcales; Merismopediaceae;
OC   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.gene:10500095; -.
DR   TCDB; 3.A.1.10.2; the atp-binding cassette (abc) superfamily.
DR   PaxDb; 1148-1001753; -.
DR   EnsemblBacteria; BAA10591; BAA10591; BAA10591.
DR   KEGG; syn:slr0513; -.
DR   eggNOG; COG1840; Bacteria.
DR   InParanoid; Q55835; -.
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:0006826; P:iron ion transport; IEA:UniProtKB-KW.
DR   CDD; cd13542; PBP2_FutA1_ilke; 1.
DR   Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR   InterPro; IPR026045; Ferric-bd.
DR   InterPro; IPR006059; SBP.
DR   InterPro; IPR006311; TAT_signal.
DR   PANTHER; PTHR30006:SF15; IRON-UTILIZATION PERIPLASMIC PROTEIN; 1.
DR   PANTHER; PTHR30006; THIAMINE-BINDING PERIPLASMIC PROTEIN-RELATED; 1.
DR   Pfam; PF13416; SBP_bac_8; 1.
DR   PIRSF; PIRSF002825; CfbpA; 1.
DR   SUPFAM; SSF53850; Periplasmic binding protein-like II; 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
//
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