APCE_SYNY3
ID APCE_SYNY3 Reviewed; 896 AA.
AC Q55544;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Phycobiliprotein ApcE;
DE EC=4.-.-.-;
DE AltName: Full=Phycobilisome LCM core-membrane linker polypeptide;
DE AltName: Full=Phycobilisome core-membrane linker phycobiliprotein ApcE;
GN Name=apcE; OrderedLocusNames=slr0335;
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 [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).
CC -!- FUNCTION: This protein is postulated to act both as terminal energy
CC acceptor (by its phycobilin-like domains) and as a linker polypeptide
CC (by its repeats and arms) that stabilizes the phycobilisome core
CC architecture. Has intrinsic bilin lyase activity (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Heterodimer of ApcF (a variant beta-allophycocyanin).
CC Phycobilisomes of this organism are composed of a two cylinder core,
CC from which six rods radiate. The core is mainly composed of
CC allophycocyanin alpha and beta chains and of minor components (By
CC similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q55544; P52231: trxA; NbExp=4; IntAct=EBI-862826, EBI-862916;
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
CC {ECO:0000250}. Note=Anchors the phycobilisome perpendicularly to the
CC cytoplasmic surface of the thylakoid membrane. {ECO:0000250}.
CC -!- PTM: Contains one covalently linked bilin chromophore. This protein
CC autochromophorylates (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the phycobilisome linker protein family.
CC {ECO:0000255|PROSITE-ProRule:PRU00775}.
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DR EMBL; BA000022; BAA10042.1; -; Genomic_DNA.
DR PIR; S76064; S76064.
DR PDB; 2L06; NMR; -; A=254-401.
DR PDB; 3OHW; X-ray; 2.70 A; A/B=711-858.
DR PDB; 3OSJ; X-ray; 2.30 A; A/B/C/D=254-400.
DR PDBsum; 2L06; -.
DR PDBsum; 3OHW; -.
DR PDBsum; 3OSJ; -.
DR AlphaFoldDB; Q55544; -.
DR SMR; Q55544; -.
DR IntAct; Q55544; 7.
DR STRING; 1148.1001419; -.
DR PaxDb; Q55544; -.
DR PRIDE; Q55544; -.
DR EnsemblBacteria; BAA10042; BAA10042; BAA10042.
DR KEGG; syn:slr0335; -.
DR eggNOG; COG0237; Bacteria.
DR eggNOG; COG0448; Bacteria.
DR InParanoid; Q55544; -.
DR OMA; FYTPYPN; -.
DR PhylomeDB; Q55544; -.
DR EvolutionaryTrace; Q55544; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0030089; C:phycobilisome; IEA:UniProtKB-KW.
DR GO; GO:0031676; C:plasma membrane-derived thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR Gene3D; 1.10.3130.20; -; 3.
DR Gene3D; 1.10.490.20; -; 1.
DR InterPro; IPR009050; Globin-like_sf.
DR InterPro; IPR001297; PBS_linker_dom.
DR InterPro; IPR038255; PBS_linker_sf.
DR InterPro; IPR012128; Phycobilisome_asu/bsu.
DR InterPro; IPR038719; Phycobilisome_asu/bsu_sf.
DR Pfam; PF00427; PBS_linker_poly; 3.
DR Pfam; PF00502; Phycobilisome; 2.
DR SUPFAM; SSF46458; SSF46458; 1.
DR PROSITE; PS51445; PBS_LINKER; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Antenna complex; Bile pigment; Chromophore;
KW Electron transport; Lyase; Membrane; Photosynthesis; Phycobilisome;
KW Reference proteome; Repeat; Thylakoid; Transport.
FT CHAIN 1..896
FT /note="Phycobiliprotein ApcE"
FT /id="PRO_0000403185"
FT DOMAIN 247..427
FT /note="PBS-linker 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00775"
FT DOMAIN 508..684
FT /note="PBS-linker 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00775"
FT DOMAIN 703..881
FT /note="PBS-linker 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00775"
FT BINDING 190
FT /ligand="(2R,3E)-phycocyanobilin"
FT /ligand_id="ChEBI:CHEBI:85275"
FT /note="covalent, via 1 link"
FT /evidence="ECO:0000250"
FT TURN 255..257
FT /evidence="ECO:0007829|PDB:2L06"
FT HELIX 275..290
FT /evidence="ECO:0007829|PDB:3OSJ"
FT HELIX 296..298
FT /evidence="ECO:0007829|PDB:3OSJ"
FT HELIX 300..310
FT /evidence="ECO:0007829|PDB:3OSJ"
FT HELIX 316..325
FT /evidence="ECO:0007829|PDB:3OSJ"
FT HELIX 327..333
FT /evidence="ECO:0007829|PDB:3OSJ"
FT TURN 334..336
FT /evidence="ECO:0007829|PDB:3OSJ"
FT HELIX 339..351
FT /evidence="ECO:0007829|PDB:3OSJ"
FT HELIX 358..382
FT /evidence="ECO:0007829|PDB:3OSJ"
FT HELIX 384..389
FT /evidence="ECO:0007829|PDB:3OSJ"
FT TURN 390..393
FT /evidence="ECO:0007829|PDB:3OSJ"
FT HELIX 732..747
FT /evidence="ECO:0007829|PDB:3OHW"
FT HELIX 753..759
FT /evidence="ECO:0007829|PDB:3OHW"
FT HELIX 761..768
FT /evidence="ECO:0007829|PDB:3OHW"
FT HELIX 774..782
FT /evidence="ECO:0007829|PDB:3OHW"
FT HELIX 785..791
FT /evidence="ECO:0007829|PDB:3OHW"
FT STRAND 793..795
FT /evidence="ECO:0007829|PDB:3OHW"
FT HELIX 797..808
FT /evidence="ECO:0007829|PDB:3OHW"
FT STRAND 809..811
FT /evidence="ECO:0007829|PDB:3OHW"
FT HELIX 816..829
FT /evidence="ECO:0007829|PDB:3OHW"
FT HELIX 831..839
FT /evidence="ECO:0007829|PDB:3OHW"
FT HELIX 842..847
FT /evidence="ECO:0007829|PDB:3OHW"
FT STRAND 850..852
FT /evidence="ECO:0007829|PDB:3OHW"
SQ SEQUENCE 896 AA; 100296 MW; 05D4358C5F0BCD8C CRC64;
MSVKASGGSS LARPQLYQTV PVSAISQAEQ QDRFLEGSEL NELTAYFQSG ALRLEIAETL
TQNADLIVSR AANRIFTGGS PLSYLEKPVE RQPALVGASS DSRNGSVTYA ESNGSGGLFG
GLRSVFSSTG PIPPGFRPIN IARYGPSNMQ KSLRDMSWFL RYTTYAIVAG DPNIIVVNTR
GLKEVIENAC SIDATIVAIQ EMRAASADYF RNNAQAKEIV LQYFDILLSE FKAPTPANKV
RQGPSNDIQG LELPQSYFNA AAKRQKYAMK PGLSALEKNA VIKAAYRQIF ERDITKAYSQ
SISYLESQVR NGDISMKEFV RRLAKSPLYR KQFFEPFINS RALELAFRHI LGRGPSSREE
VQKYFSIVSS GGLPALVDAL VDSQEYADYF GEETVPYLRG LGVEAQECRN WGMQQDLFSY
SAPFRKVPQF ITTFAQYDRP LPDQHVYGSG NDPLEIQFGA IFPKETRNPS KRPAPFNKDT
KRILIHRGPA VNNQVGNPSA VGEFPGSLGA KVFRLNGGLP GAKVGKNTGT SVKFGESSTQ
ALIRAAYRQV FGRDLYEGQR LSVAEIQLEN GDISVREFIK RLAKSELFLK LYWAPHYVCK
AIEYMHRRLL GRPTYGRQEM NQYFDIASKQ GFYAVVEAMI DSKEYSDAFG EDTVPYERYL
TPGGLQMRSA RVGSLREDIG QRVDKEVTPR FVELGQVSAI RTEPEIAYRS NQGVTRQRQQ
TKVFKLVSTY DKVAVKNAIR AAYRQVFERD LEPYIINSEF TALESKLSNN EINVKEFIEG
LGTSELYMKE FYAPYPNTKV IEMGTKHFLG RAPLNQKEIQ QYNQILASQG LKAFIGAMVN
GMEYLQTFGE DTVPYRRFPT LPAANFPNTE RLYNKLTKQD KELVVPSFTP VVKVGG
