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ISIA_SYNE7
ID   ISIA_SYNE7              Reviewed;         342 AA.
AC   P15347; Q31MZ7;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 3.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Iron stress-induced chlorophyll-binding protein;
DE   AltName: Full=CP43';
GN   Name=isiA; OrderedLocusNames=Synpcc7942_1542;
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], AND INDUCTION.
RX   PubMed=3141374; DOI=10.1128/jb.170.11.5018-5026.1988;
RA   Laudenbach D.E., Straus N.A.;
RT   "Characterization of a cyanobacterial iron stress-induced gene similar to
RT   psbC.";
RL   J. Bacteriol. 170:5018-5026(1988).
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   FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX   PubMed=8022940; DOI=10.1104/pp.103.3.893;
RA   Burnap R.L., Troyan T., Sherman L.A.;
RT   "The highly abundant chlorophyll-protein complex of iron-deficient
RT   Synechococcus sp. PCC7942 (CP43') is encoded by the isiA gene.";
RL   Plant Physiol. 103:893-902(1993).
RN   [4]
RP   FUNCTION, AND SUGGESTED TO PROTECT PHOTOSYSTEM II DURING IRON-DEPRIVATION.
RX   PubMed=10216865; DOI=10.1046/j.1365-2958.1999.01332.x;
RA   Park Y.-I., Sandstroem S., Gustafsson P., Oequist G.;
RT   "Expression of the isiA gene is essential for the survival of the
RT   cyanobacterium Synechococcus sp. PCC 7942 by protecting photosystem II from
RT   excess light under iron limitation.";
RL   Mol. Microbiol. 32:123-129(1999).
RN   [5]
RP   STRUCTURAL ASSOCIATION WITH PHOTOSYSTEM I TRIMERS, AND SUBUNIT.
RX   PubMed=11507644; DOI=10.1038/35089104;
RA   Boekema E.J., Hifney A., Yakushevska A.E., Piotrowski M., Keegstra W.,
RA   Berry S., Michel K.-P., Pistorius E.K., Kruip J.;
RT   "A giant chlorophyll-protein complex induced by iron deficiency in
RT   cyanobacteria.";
RL   Nature 412:745-748(2001).
RN   [6]
RP   FUNCTION, AND OVEREXPRESSION.
RX   PubMed=11594057; DOI=10.1562/0031-8655(2001)074<0431:ctigpf>2.0.co;2;
RA   Sandstroem S., Park Y.-I., Oequist G., Gustafsson P.;
RT   "CP43', the isiA gene product, functions as an excitation energy dissipator
RT   in the cyanobacterium Synechococcus sp. PCC 7942.";
RL   Photochem. Photobiol. 74:431-437(2001).
RN   [7]
RP   SUBCELLULAR LOCATION, COFACTOR, AND SPECTROSCOPIC PROPERTIES.
RX   PubMed=12460685; DOI=10.1016/s0005-2728(02)00371-7;
RA   Andrizhiyevskaya E.G., Schwabe T.M.E., Germano M., D'Haene S., Kruip J.,
RA   van Grondelle R., Dekker J.P.;
RT   "Spectroscopic properties of PSI-IsiA supercomplexes from the
RT   cyanobacterium Synechococcus PCC 7942.";
RL   Biochim. Biophys. Acta 1556:265-272(2002).
RN   [8]
RP   INDUCTION BY OXIDATIVE STRESS.
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: Functions as an antenna for photosystem I (PSI) under iron-
CC       limiting conditions, when phycobilisomes disappear. Also functions as a
CC       dissipator of light energy, protecting cells from excessive light under
CC       iron-deficient conditions. Sequesters chlorophyll when cells are
CC       growing in iron-deficient conditions; it may bind up to 50% of the
CC       chlorophyll in iron-starved cells. {ECO:0000269|PubMed:10216865,
CC       ECO:0000269|PubMed:8022940, ECO:0000303|PubMed:11594057}.
CC   -!- COFACTOR:
CC       Name=chlorophyll a; Xref=ChEBI:CHEBI:58416;
CC         Evidence={ECO:0000269|PubMed:12460685};
CC       Note=Binds 16-17 chlorophyll a molecules per subunit.
CC       {ECO:0000269|PubMed:12460685};
CC   -!- COFACTOR:
CC       Name=all-trans-beta-carotene; Xref=ChEBI:CHEBI:17579;
CC         Evidence={ECO:0000269|PubMed:12460685};
CC   -!- SUBUNIT: Under iron-starvation forms a complex with PSI trimers, where
CC       the trimer is surrounded by a ring composed of 18 IsiA subunits.
CC       {ECO:0000269|PubMed:11507644}.
CC   -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane
CC       {ECO:0000269|PubMed:12460685, ECO:0000269|PubMed:8022940}; Multi-pass
CC       membrane protein {ECO:0000269|PubMed:12460685,
CC       ECO:0000269|PubMed:8022940}. Note=Probably the major component of the
CC       CPVI-4 chlorophyll-protein complex.
CC   -!- INDUCTION: By iron stress, and also by exposure to oxidative stress
CC       such as hydrogen peroxide and methylviologen treatment.
CC       {ECO:0000269|PubMed:14605795, ECO:0000269|PubMed:3141374}.
CC   -!- DISRUPTION PHENOTYPE: In cells lacking isiA under iron-deficient
CC       conditions, approximately 2-fold less chlorophyll is found per cell.
CC       {ECO:0000269|PubMed:8022940}.
CC   -!- SIMILARITY: Belongs to the PsbB/PsbC family. IsiA/Pcb subfamily.
CC       {ECO:0000305}.
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DR   EMBL; M23639; AAC64212.1; -; Genomic_DNA.
DR   EMBL; CP000100; ABB57572.1; -; Genomic_DNA.
DR   PIR; A30189; A30189.
DR   RefSeq; WP_011242315.1; NC_007604.1.
DR   PDB; 6KIF; EM; 3.30 A; 1/2/3/4/5/6/Y/Z/a/b/c/d/q/r/s/t/u/v=1-342.
DR   PDB; 6KIG; EM; 2.90 A; 1/2/3/4/5/6/Y/Z/a/b/c/d/q/r/s/t/u/v=1-342.
DR   PDBsum; 6KIF; -.
DR   PDBsum; 6KIG; -.
DR   AlphaFoldDB; P15347; -.
DR   SMR; P15347; -.
DR   STRING; 1140.Synpcc7942_1542; -.
DR   PRIDE; P15347; -.
DR   EnsemblBacteria; ABB57572; ABB57572; Synpcc7942_1542.
DR   KEGG; syf:Synpcc7942_1542; -.
DR   eggNOG; ENOG502Z92X; Bacteria.
DR   HOGENOM; CLU_028310_0_0_3; -.
DR   OMA; FGEYTEF; -.
DR   OrthoDB; 417558at2; -.
DR   BioCyc; MetaCyc:SYNPCC7942_1542-MON; -.
DR   BioCyc; SYNEL:SYNPCC7942_1542-MON; -.
DR   BRENDA; 3.4.19.12; 3474.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0009522; C:photosystem I; IEA:UniProtKB-KW.
DR   GO; GO:0031676; C:plasma membrane-derived thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016168; F:chlorophyll binding; IEA:UniProtKB-KW.
DR   GO; GO:0009767; P:photosynthetic electron transport chain; IEA:InterPro.
DR   InterPro; IPR000932; PS_antenna-like.
DR   InterPro; IPR036001; PS_II_antenna-like_sf.
DR   PANTHER; PTHR33180; PTHR33180; 1.
DR   Pfam; PF00421; PSII; 1.
DR   SUPFAM; SSF161077; SSF161077; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Chlorophyll; Chromophore; Membrane; Photosynthesis;
KW   Photosystem I; Stress response; Thylakoid; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..342
FT                   /note="Iron stress-induced chlorophyll-binding protein"
FT                   /id="PRO_0000077561"
FT   TRANSMEM        25..45
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        89..109
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        138..158
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        204..224
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        240..260
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        308..328
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        179
FT                   /note="E -> Q (in Ref. 1; AAC64212)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   342 AA;  36976 MW;  ACE889338C0F44ED CRC64;
     MQTYNNPEVT YDWWAGNARF ANLSGLFIAA HVAQAALIMF WAGAFTLYEI SWLTADQSMG
     EQGLILLPHL ATLGLGVGDG GQVTDTYPLF VVGAVHLIAS AVLGAGALFH TFRAPSDLAA
     ASGAAKRFHF DWNDPKQLGL ILGHHLLFLG VGALLLVAKA TTWGGLYDAA SQTVRLVTEP
     TLNPAVIYGY QTHFASIDNL EDLVGGHVYV GVMLIAGGIW HILVPPFQWT KKVLIYSGEA
     ILSYSLGGIA LAGFVAAYFC AVNTLAYPVE FYGAPLEIKL GVTPYFADTV QLPFGAHTPR
     AWLSNAHFFL AFFCLQGHLW HALRAMGFDF RRVEKALSSV EA
 
 
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