ISIA_SYNY3
ID ISIA_SYNY3 Reviewed; 342 AA.
AC Q55274; P73884;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Iron stress-induced chlorophyll-binding protein;
DE AltName: Full=CP43';
GN Name=isiA; OrderedLocusNames=sll0247;
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 [GENOMIC DNA].
RA Ferreira F., Straus N.A.;
RT "Sequence of isiS from Synechocystis PCC 6803.";
RL Submitted (DEC-1993) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
RP INDUCTION BY HIGH SALT AND IRON-DEFICIENCY.
RX PubMed=9868777; DOI=10.1111/j.1574-6968.1998.tb13336.x;
RA Vinnemeier J., Kunert A., Hagemann M.;
RT "Transcriptional analysis of the isiAB operon in salt-stressed cells of the
RT cyanobacterium Synechocystis sp. PCC 6803.";
RL FEMS Microbiol. Lett. 169:323-330(1998).
RN [4]
RP FUNCTION, STRUCTURAL ASSOCIATION WITH PHOTOSYSTEM I TRIMERS, AND SUBUNIT.
RX PubMed=11507643; DOI=10.1038/35089098;
RA Bibby T.S., Nield J., Barber J.;
RT "Iron deficiency induces the formation of an antenna ring around trimeric
RT photosystem I in cyanobacteria.";
RL Nature 412:743-745(2001).
RN [5]
RP SUBCELLULAR LOCATION, RING STRUCTURE IN THE ABSENCE OF PSAF AND PSAJ, AND
RP SUBUNIT.
RX PubMed=14556907; DOI=10.1016/j.bbabio.2003.08.002;
RA Kouril R., Yeremenko N., D'Haene S., Yakushevska A.E., Keegstra W.,
RA Matthijs H.C.P., Dekker J.P., Boekema E.J.;
RT "Photosystem I trimers from Synechocystis PCC 6803 lacking the PsaF and
RT PsaJ subunits bind an IsiA ring of 17 units.";
RL Biochim. Biophys. Acta 1607:1-4(2003).
RN [6]
RP SUBCELLULAR LOCATION, PIGMENT-BINDING, FUNCTION IN LIGHT PROTECTION,
RP COFACTOR, AND SUBUNIT.
RX PubMed=16086587; DOI=10.1021/bi0510680;
RA Ihalainen J.A., D'Haene S., Yeremenko N., van Roon H., Arteni A.A.,
RA Boekema E.J., van Grondelle R., Matthijs H.C.P., Dekker J.P.;
RT "Aggregates of the chlorophyll-binding protein IsiA (CP43') dissipate
RT energy in cyanobacteria.";
RL Biochemistry 44:10846-10853(2005).
RN [7]
RP RING STRUCTURE IN THE ABSENCE OF PSAL, AND SUBUNIT.
RX PubMed=15694354; DOI=10.1016/j.bbabio.2004.11.008;
RA Kouril R., Yeremenko N., D'Haene S., Oostergetel G.T., Matthijs H.C.P.,
RA Dekker J.P., Boekema E.J.;
RT "Supercomplexes of IsiA and photosystem I in a mutant lacking subunit
RT PsaL.";
RL Biochim. Biophys. Acta 1706:262-266(2005).
RN [8]
RP REVIEW.
RX PubMed=15943969; DOI=10.1016/j.febslet.2005.03.051;
RA Kouril R., Arteni A.A., Lax J., Yeremenko N., D'Haene S., Rogner M.,
RA Matthijs H.C., Dekker J.P., Boekema E.J.;
RT "Structure and functional role of supercomplexes of IsiA and Photosystem I
RT in cyanobacterial photosynthesis.";
RL FEBS Lett. 579:3253-3257(2005).
CC -!- FUNCTION: Functions as an antenna for photosystem I (PSI) under iron-
CC limiting conditions, when phycobilisomes disappear. In the
CC (PSI)3(Isi3)18 complex most of the harvested energy is probably used by
CC PSI; in other PSI-containing supercomplexes a large part of the energy
CC will probably not be used for light harvesting, but rather is
CC dissipated to protect the organism from light damage.
CC {ECO:0000269|PubMed:11507643, ECO:0000269|PubMed:16086587}.
CC -!- COFACTOR:
CC Name=chlorophyll a; Xref=ChEBI:CHEBI:58416;
CC Evidence={ECO:0000269|PubMed:16086587};
CC Note=Binds 16 chlorophyll a molecules per subunit.
CC {ECO:0000269|PubMed:16086587};
CC -!- COFACTOR:
CC Name=all-trans-beta-carotene; Xref=ChEBI:CHEBI:17579;
CC Evidence={ECO:0000269|PubMed:16086587};
CC Note=Binds 2 beta-carotene molecules per subunit.
CC {ECO:0000269|PubMed:16086587};
CC -!- COFACTOR:
CC Name=echinenone; Xref=ChEBI:CHEBI:4746;
CC Evidence={ECO:0000269|PubMed:16086587};
CC Note=Binds 1 echinenone molecule per subunit.
CC {ECO:0000269|PubMed:16086587};
CC -!- COFACTOR:
CC Name=all-trans-zeaxanthin; Xref=ChEBI:CHEBI:27547;
CC Evidence={ECO:0000269|PubMed:16086587};
CC Note=Binds 1 zeaxanthin molecule per subunit.
CC {ECO:0000269|PubMed:16086587};
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. When
CC the PSI subunits PsaF and PsaJ are missing the ring is composed of 17
CC IsiA subunits, indicating that each IsiA subunit has a different
CC interaction with the trimer. This suggests that the size of the PSI
CC complex determines the number of IsiA units in the surrounding ring. In
CC the absence of PsaL has a tendency to form incomplete rings with PSI
CC monomers, suggesting PsaL helps form the rings. Also forms other
CC aggregates of varying sizes depending on the level of iron-deprivation.
CC {ECO:0000269|PubMed:11507643, ECO:0000269|PubMed:14556907,
CC ECO:0000269|PubMed:15694354, ECO:0000269|PubMed:16086587}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane
CC {ECO:0000269|PubMed:14556907, ECO:0000269|PubMed:16086587}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:14556907,
CC ECO:0000269|PubMed:16086587}.
CC -!- INDUCTION: By iron stress, salt stress and to a lesser extent by heat
CC shock. {ECO:0000269|PubMed:9868777}.
CC -!- SIMILARITY: Belongs to the PsbB/PsbC family. IsiA/Pcb subfamily.
CC {ECO:0000305}.
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DR EMBL; L26530; AAA27291.1; -; Genomic_DNA.
DR EMBL; BA000022; BAA17948.1; -; Genomic_DNA.
DR PIR; S75086; S75086.
DR PDB; 6NWA; EM; 3.48 A; W/X/Y/Z/g/h/n/o/p/q/r/s/t/u/v/w/x/y=1-342.
DR PDBsum; 6NWA; -.
DR AlphaFoldDB; Q55274; -.
DR SMR; Q55274; -.
DR IntAct; Q55274; 11.
DR STRING; 1148.1653031; -.
DR PaxDb; Q55274; -.
DR EnsemblBacteria; BAA17948; BAA17948; BAA17948.
DR KEGG; syn:sll0247; -.
DR eggNOG; ENOG502Z92X; Bacteria.
DR OMA; FGEYTEF; -.
DR PhylomeDB; Q55274; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030094; C:plasma membrane-derived photosystem I; IDA:UniProtKB.
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:0010106; P:cellular response to iron ion starvation; IDA:UniProtKB.
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; Reference proteome; Stress response; Thylakoid;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..342
FT /note="Iron stress-induced chlorophyll-binding protein"
FT /id="PRO_0000077562"
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 208..228
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 240..260
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 303..323
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CONFLICT 94
FT /note="S -> R (in Ref. 1; AAA27291)"
FT /evidence="ECO:0000305"
FT CONFLICT 334..342
FT /note="EQAFDSLQT -> NKRLIPCKPSH (in Ref. 1; AAA27291)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 342 AA; 37221 MW; 3510C9D4F6EADC4C CRC64;
MQTYGNDTVQ YEWWAGNARF ADQSGLFIAA HVAQAALTAF WAGAFTLFEI SRFDPTQAMG
DQGLILLPHL ATLGWGVGDG GQIVDTYPYF VIGSIHLIAS AVLGAGALFH TLRAPADLST
LKGQGKKFHF TWENPQQLGI ILGHHLLFLG AGALLLAGKA MYWGGLYDAT TQTVRLVSQP
TLDPLVIYGY QTHFASISSL EDLVGGHIFV GFLLIGGGIW HILVPPLGWA KKVLLFSGEA
ILSYSLGGIA LAGFVAAYFC AVNTLAYPPE FYGPPLAIKL GIFPYFADTV ELPMHAHTSR
AWLANAHFFL AFFFLQGHLW HALRALGFDF KRVEQAFDSL QT
