ID   APCE_SYNY4              Reviewed;         896 AA.
AC   Q02907;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Phycobiliprotein ApcE;
DE            EC=4.-.-.-;
DE   AltName: Full=Anchor polypeptide;
DE   AltName: Full=L-CM 100.5;
DE   AltName: Full=Phycobilisome 100.5 kDa core-membrane linker polypeptide;
GN   Name=apcE;
OS   Synechocystis sp. (strain PCC 6714) (Aphanocapsa sp. (strain PCC 6714)).
OC   Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC   unclassified Synechocystis.
OX   NCBI_TaxID=1147;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8467079; DOI=10.1007/bf00027115;
RA   Dimagno L.M., Haselkorn R.;
RT   "Isolation and characterization of the genes encoding allophycocyanin
RT   subunits and two linker proteins from Synechocystis 6714.";
RL   Plant Mol. Biol. 21:835-846(1993).
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   -!- 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; L02309; AAA69685.1; -; Genomic_DNA.
DR   PIR; S59990; S59990.
DR   AlphaFoldDB; Q02907; -.
DR   SMR; Q02907; -.
DR   STRING; 1147.D082_24510; -.
DR   eggNOG; COG0237; Bacteria.
DR   eggNOG; COG0448; Bacteria.
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   3: Inferred from homology;
KW   Antenna complex; Bile pigment; Chromophore; Electron transport; Lyase;
KW   Membrane; Photosynthesis; Phycobilisome; Repeat; Thylakoid; Transport.
FT   CHAIN           1..896
FT                   /note="Phycobiliprotein ApcE"
FT                   /id="PRO_0000199265"
FT   DOMAIN          247..427
FT                   /note="PBS-linker 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00775"
FT   DOMAIN          508..689
FT                   /note="PBS-linker 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00775"
FT   DOMAIN          704..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"
SQ   SEQUENCE   896 AA;  100461 MW;  BD1D14C2923E32A3 CRC64;
     MSVKASGGSS LARPQLYQTF AVSAISQAEQ QDRFLEGSEL NELTRIFQSG SLRLEIAETL
     TENADLIVSR AANRIFTGGS PLSYLEKPVE RQPALVGASS DSRNGSVTYA ESNGGGGLFG
     GLRSVFSSTG PIPPGFRPIN IARYGPSNMQ KSLRDMSWFL RYTTYAIVAG GPNIIVVNTR
     GLKEVIENAC SIDATIVRIQ EMRAASADYF RANAQAKEIV LQYFDILLSE FKAPTPANKV
     RQGPSNDIQG LELPQSYFNA SAKRQKYAMK PGLSALEKNA VIKAAYRQIF ERDITKAYSQ
     SISYLESQVR NGDISMKEFV RRLAKSPLYR KQFFEPFINS RALELAFRHI LGRGPSSREE
     VQKYFAIVSN GGLPALVDAL VDSQEYSDYF GEETVPYLRG LGVEAQECRN WGMQQDLFSY
     SAPFRKVPQF ITTFAQYDRP LPDQHVYGSG NDPLEIQFGA IFPKETRNPS KRPAPFNKDT
     KRILIHRGPA VNNQVGNPSA VGEFPGSLGA KVFRLNGGLP GAKVGKNTGT SVKFGESSTQ
     ALIRAAYRQV FGRDLYEGQR LSVAEIQLEN GDISVREFIK RLAKSELFLK LYWAPHYVCK
     AIEYMHRRLL NRPTYGRQEM NQYFDIASKQ GFYAVVEAMI DSKEYSDAFG EDTVPYERYL
     TPGGLQMRSA RVGSIREDIG QRVDKEVTPR FVELGQVSNL RTEPEIAYRS NQGVYRQRQQ
     TKVFKLTSNY DKVAVKNAIR AAHRQVFERD LEPYIINSEF TALESKLSNG EINVKEFIEG
     LGTSELYMKE FYAPYPNTKV IEMGTKHFLG RAPLNQKEIQ QYNQILASQG LKAFIGAMVN
     GMEYLQTFGE DTVPYRRFPT LPAANFPNTE RLYNKLTKQD KELVVPSFTP VVKVGG