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IDIA_SYNE7
ID   IDIA_SYNE7              Reviewed;         357 AA.
AC   Q31L64; Q93IP4;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 2.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Iron deficiency-induced protein A;
DE   Flags: Precursor;
GN   Name=idiA; OrderedLocusNames=Synpcc7942_2175;
OS   Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS   R2).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX   NCBI_TaxID=1140;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Toelle J.;
RL   Thesis (2001), University of Bielefeld, Germany.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7942 / FACHB-805;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Lykidis A., Richardson P.;
RT   "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   MUTANT STUDIES, AND 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   [4]
RP   INDUCTION, AND REGULATION BY IDIB AND DPSA.
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   [5]
RP   FUNCTION IN PSII PROTECTION.
RX   PubMed=16228425; DOI=10.1023/a:1006322925324;
RA   Exss-Sonne P., Toelle J., Bader K.P., Pistorius E.K., Michel K.-P.;
RT   "The IdiA protein of Synechococcus sp. PCC 7942 functions in protecting the
RT   acceptor side of Photosystem II under oxidative stress.";
RL   Photosyn. Res. 63:145-157(2000).
RN   [6]
RP   REGULATION BY IDIB AND FUR.
RX   PubMed=11489854; DOI=10.1128/jb.183.17.5015-5024.2001;
RA   Michel K.-P., Pistorius E.K., Golden S.S.;
RT   "Unusual regulatory elements for iron deficiency induction of the idiA gene
RT   of Synechococcus elongatus PCC 7942.";
RL   J. Bacteriol. 183:5015-5024(2001).
RN   [7]
RP   REGULATION BY IDIB.
RX   PubMed=14605795; DOI=10.1007/s00203-003-0618-4;
RA   Yousef N., Pistorius E.K., Michel K.-P.;
RT   "Comparative analysis of idiA and isiA transcription under iron starvation
RT   and oxidative stress in Synechococcus elongatus PCC 7942 wild-type and
RT   selected mutants.";
RL   Arch. Microbiol. 180:471-483(2003).
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:0000269|PubMed:16228425}.
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 {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}; Lumenal side {ECO:0000250}.
CC   -!- INDUCTION: By iron limitation and to a smaller extent by manganese
CC       limitation. Regulated by IdiB. May also be indirectly regulated by DpsA
CC       and Fur. {ECO:0000269|PubMed:10411274, ECO:0000269|PubMed:8828233}.
CC   -!- PTM: Predicted to be exported by the Tat system. The position of the
CC       signal peptide cleavage has not been experimentally proven.
CC   -!- SIMILARITY: Belongs to the bacterial solute-binding protein 1 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABB58205.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AJ319672; CAC40996.1; -; Genomic_DNA.
DR   EMBL; CP000100; ABB58205.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q31L64; -.
DR   SMR; Q31L64; -.
DR   STRING; 1140.Synpcc7942_2175; -.
DR   PRIDE; Q31L64; -.
DR   EnsemblBacteria; ABB58205; ABB58205; Synpcc7942_2175.
DR   KEGG; syf:Synpcc7942_2175; -.
DR   eggNOG; COG1840; Bacteria.
DR   HOGENOM; CLU_026974_2_1_3; -.
DR   BioCyc; SYNEL:SYNPCC7942_2175-MON; -.
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   Ion transport; Iron; Iron transport; Membrane; Metal-binding; Signal;
KW   Thylakoid; Transport.
FT   SIGNAL          1..36
FT                   /note="Tat-type signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT   CHAIN           37..357
FT                   /note="Iron deficiency-induced protein A"
FT                   /id="PRO_5000067709"
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"
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
 
 
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