IDIA_SYNP6
ID IDIA_SYNP6 Reviewed; 357 AA.
AC Q5N0R0; O06850;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Iron deficiency-induced protein A;
DE Flags: Precursor;
GN Name=idiA; OrderedLocusNames=syc1920_d;
OS Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) (Anacystis
OS nidulans).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=269084;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 37-82; 86-100;
RP 121-135; 142-161; 190-213; 254-273 AND 335-356, SUBCELLULAR LOCATION, AND
RP INDUCTION.
RX PubMed=8828233; DOI=10.1099/00221287-142-9-2635;
RA Michel K.-P., Thole H.H., Pistorius E.K.;
RT "IdiA, a 34 kDa protein in the cyanobacteria Synechococcus sp. strains PCC
RT 6301 and PCC 7942, is required for growth under iron and manganese
RT limitations.";
RL Microbiology 142:2635-2645(1996).
RN [2]
RP SEQUENCE REVISION.
RX PubMed=10411274; DOI=10.1099/13500872-145-6-1473;
RA Michel K.-P., Krueger F., Puehler A., Pistorius E.K.;
RT "Molecular characterization of idiA and adjacent genes in the cyanobacteria
RT Synechococcus sp. strains PCC 6301 and PCC 7942.";
RL Microbiology 145:1473-1484(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27144 / PCC 6301 / SAUG 1402/1;
RX PubMed=17211581; DOI=10.1007/s11120-006-9122-4;
RA Sugita C., Ogata K., Shikata M., Jikuya H., Takano J., Furumichi M.,
RA Kanehisa M., Omata T., Sugiura M., Sugita M.;
RT "Complete nucleotide sequence of the freshwater unicellular cyanobacterium
RT Synechococcus elongatus PCC 6301 chromosome: gene content and
RT organization.";
RL Photosyn. Res. 93:55-67(2007).
RN [4]
RP INDUCTION.
RX PubMed=9599805; DOI=10.1007/s004250050298;
RA Michel K.-P., Exss-Sonne P., Scholten-Beck G., Kahmann U., Ruppel H.G.,
RA Pistorius E.K.;
RT "Immunocytochemical localization of IdiA, a protein expressed under iron or
RT manganese limitation in the mesophilic cyanobacterium Synechococcus PCC
RT 6301 and the thermophilic cyanobacterium Synechococcus elongatus.";
RL Planta 205:73-81(1998).
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:0000250}.
CC -!- FUNCTION: May also be part of a periplasmic ABC transporter complex
CC involved in iron import. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane
CC {ECO:0000305|PubMed:8828233}; Peripheral membrane protein
CC {ECO:0000305|PubMed:8828233}; Lumenal side
CC {ECO:0000305|PubMed:8828233}.
CC -!- INDUCTION: By iron limitation and to a smaller extent by manganese
CC limitation. {ECO:0000269|PubMed:8828233, ECO:0000269|PubMed:9599805}.
CC -!- PTM: Predicted to be exported by the Tat system. The position of the
CC signal peptide cleavage has been experimentally proven.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 1 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD80110.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA88640.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; Z48754; CAA88640.1; ALT_INIT; Genomic_DNA.
DR EMBL; AP008231; BAD80110.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; Q5N0R0; -.
DR SMR; Q5N0R0; -.
DR STRING; 269084.syc1920_d; -.
DR EnsemblBacteria; BAD80110; BAD80110; syc1920_d.
DR KEGG; syc:syc1920_d; -.
DR eggNOG; COG1840; Bacteria.
DR Proteomes; UP000001175; 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; IPR006311; TAT_signal.
DR PIRSF; PIRSF002825; CfbpA; 1.
DR PROSITE; PS51318; TAT; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Ion transport; Iron; Iron transport; Membrane;
KW Metal-binding; Signal; Thylakoid; Transport.
FT SIGNAL 1..36
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648,
FT ECO:0000269|PubMed:8828233"
FT CHAIN 37..357
FT /note="Iron deficiency-induced protein A"
FT /id="PRO_0000345609"
FT BINDING 48
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 49
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 182
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 238
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 239
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT CONFLICT 75
FT /note="D -> T (in Ref. 1; CAA88640)"
FT /evidence="ECO:0000305"
FT CONFLICT 223
FT /note="L -> A (in Ref. 1; CAA88640)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 357 AA; 39243 MW; 209F41291845F14D CRC64;
MSESMFSRRD FLLGGTALAG TLLLDSFGDW RRRAEAAEGE VNLYSGRHYN TDNQIYREFT
QKTGIKVNLI EGEADALLAR LKSEGSRSPA DVFITVDAGR LWQATQANLL RPLTQAQAPK
LYQAVPANLR DPQGRWFALS KRARVIMYNR DRVNASQLST YEDLANPKWR NQILVRSSSN
VYNLSLTGEM IAADGAAKTE AWARGLVQNF ARQPQGGDTP QILACAAGVG SLAIANTYYL
VRLFKSKKAE EREAARKIKV FFPNQKGRGT HVNISGAGIV RTAPNPRAAQ LLLEYLLSSQ
AQAVFARGNG EYPVLRGVSL DPILAGFGQF KESKISASVF GANNAQALQL MDRAGWK
