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APCE_NOSS1
ID   APCE_NOSS1              Reviewed;        1132 AA.
AC   P80559; O05712;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Phycobiliprotein ApcE;
DE            EC=4.-.-.-;
DE   AltName: Full=Anchor polypeptide;
DE   AltName: Full=PBS-anchor protein;
DE   AltName: Full=Phycobilisome linker polypeptide;
GN   Name=apcE; OrderedLocusNames=alr0020;
OS   Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=103690;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Cai Y.A., Lantoine F.L., Glazer A.N.;
RT   "Characterization of Anabaena sp. PCC 7120 mutants defective in the large
RT   core-membrane linker protein of the light-harvesting phycobilisomes.";
RL   Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX   PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA   Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA   Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA   Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT   "Complete genomic sequence of the filamentous nitrogen-fixing
RT   cyanobacterium Anabaena sp. strain PCC 7120.";
RL   DNA Res. 8:205-213(2001).
RN   [3]
RP   PROTEIN SEQUENCE OF 2-31.
RX   PubMed=8665889; DOI=10.1111/j.1432-1033.1996.01010.x;
RA   Ducret A., Sidler W., Wehrli E., Frank G., Zuber H.;
RT   "Isolation, characterization and electron microscopy analysis of a
RT   hemidiscoidal phycobilisome type from the cyanobacterium Anabaena sp. PCC
RT   7120.";
RL   Eur. J. Biochem. 236:1010-1024(1996).
RN   [4]
RP   STRUCTURE BY NMR OF 727-867.
RG   Northeast structural genomics consortium (NESG);
RT   "Solution NMR structure of the PBS linker domain of phycobilisome linker
RT   polypeptide from Anabaena sp. Northeast structural genomics consortium
RT   (NESG) target nsr123e.";
RL   Submitted (JUL-2010) to the PDB data bank.
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; U96137; AAC97589.1; -; Genomic_DNA.
DR   EMBL; BA000019; BAB77544.1; -; Genomic_DNA.
DR   PIR; AD1809; AD1809.
DR   RefSeq; WP_010994197.1; NZ_RSCN01000016.1.
DR   PDB; 2KY4; NMR; -; A=727-867.
DR   PDB; 4XXI; X-ray; 2.20 A; A/B=20-76, A/B=154-240.
DR   PDB; 4XXK; X-ray; 2.97 A; A/B=20-76, A/B=154-240.
DR   PDB; 7EYD; EM; 3.90 A; 09/19=1-1132.
DR   PDBsum; 2KY4; -.
DR   PDBsum; 4XXI; -.
DR   PDBsum; 4XXK; -.
DR   PDBsum; 7EYD; -.
DR   AlphaFoldDB; P80559; -.
DR   SMR; P80559; -.
DR   STRING; 103690.17134998; -.
DR   EnsemblBacteria; BAB77544; BAB77544; BAB77544.
DR   KEGG; ana:alr0020; -.
DR   eggNOG; COG0237; Bacteria.
DR   eggNOG; COG0448; Bacteria.
DR   OMA; FYTPYPN; -.
DR   OrthoDB; 20391at2; -.
DR   EvolutionaryTrace; P80559; -.
DR   Proteomes; UP000002483; 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; -; 4.
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; 4.
DR   Pfam; PF00502; Phycobilisome; 2.
DR   SUPFAM; SSF46458; SSF46458; 1.
DR   PROSITE; PS51445; PBS_LINKER; 4.
PE   1: Evidence at protein level;
KW   3D-structure; Antenna complex; Bile pigment; Chromophore;
KW   Direct protein sequencing; Electron transport; Lyase; Membrane;
KW   Photosynthesis; Phycobilisome; Reference proteome; Repeat; Thylakoid;
KW   Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:8665889"
FT   CHAIN           2..1132
FT                   /note="Phycobiliprotein ApcE"
FT                   /id="PRO_0000199257"
FT   DOMAIN          253..433
FT                   /note="PBS-linker 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00775"
FT   DOMAIN          514..692
FT                   /note="PBS-linker 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00775"
FT   DOMAIN          709..887
FT                   /note="PBS-linker 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00775"
FT   DOMAIN          940..1121
FT                   /note="PBS-linker 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00775"
FT   BINDING         196
FT                   /ligand="(2R,3E)-phycocyanobilin"
FT                   /ligand_id="ChEBI:CHEBI:85275"
FT                   /note="covalent, via 1 link"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        29
FT                   /note="E -> D (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        221
FT                   /note="E -> D (in Ref. 1; AAC97589)"
FT                   /evidence="ECO:0000305"
FT   HELIX           21..30
FT                   /evidence="ECO:0007829|PDB:4XXI"
FT   HELIX           37..48
FT                   /evidence="ECO:0007829|PDB:4XXI"
FT   HELIX           50..62
FT                   /evidence="ECO:0007829|PDB:4XXI"
FT   HELIX           64..74
FT                   /evidence="ECO:0007829|PDB:4XXI"
FT   HELIX           155..175
FT                   /evidence="ECO:0007829|PDB:4XXI"
FT   HELIX           179..185
FT                   /evidence="ECO:0007829|PDB:4XXI"
FT   HELIX           188..195
FT                   /evidence="ECO:0007829|PDB:4XXI"
FT   HELIX           198..213
FT                   /evidence="ECO:0007829|PDB:4XXI"
FT   HELIX           214..216
FT                   /evidence="ECO:0007829|PDB:4XXI"
FT   HELIX           220..235
FT                   /evidence="ECO:0007829|PDB:4XXI"
FT   HELIX           738..752
FT                   /evidence="ECO:0007829|PDB:2KY4"
FT   HELIX           759..765
FT                   /evidence="ECO:0007829|PDB:2KY4"
FT   HELIX           767..774
FT                   /evidence="ECO:0007829|PDB:2KY4"
FT   HELIX           780..789
FT                   /evidence="ECO:0007829|PDB:2KY4"
FT   HELIX           791..797
FT                   /evidence="ECO:0007829|PDB:2KY4"
FT   STRAND          799..801
FT                   /evidence="ECO:0007829|PDB:2KY4"
FT   HELIX           803..814
FT                   /evidence="ECO:0007829|PDB:2KY4"
FT   HELIX           822..834
FT                   /evidence="ECO:0007829|PDB:2KY4"
FT   HELIX           837..845
FT                   /evidence="ECO:0007829|PDB:2KY4"
FT   HELIX           848..853
FT                   /evidence="ECO:0007829|PDB:2KY4"
FT   STRAND          856..858
FT                   /evidence="ECO:0007829|PDB:2KY4"
FT   TURN            864..866
FT                   /evidence="ECO:0007829|PDB:2KY4"
SQ   SEQUENCE   1132 AA;  126888 MW;  C241FAE6DB1140E6 CRC64;
     MSVKASGGSS VARPQLYQTL AVATITQAEQ QDRFLGRGEL DELASYFASG AKRLEIAQLL
     TENSEIIVSR AANRIFVGGS PMAFLEKPRE PELAMAAVGG GGDVRESMKL GTVTYVETRG
     GFLENLRSIF NTSPSGPTPP GFRPINIARY GPSNMAKSLR DLSWFLRYAT YAIVAGDPNI
     IVVNTRGLRE IIENACSGEA TIVALQEIKA ASLSYFRKDP EAAEIVSQYM DVLITEFKAP
     TPSNKLRQRP SGDQQGLQLP QIYFSAAERR PKFVMKTGLS ATEKNEVIKA AYRQIFERDI
     TRAYSLSISD LESKVKNGDI SMKEFVRRLA KSPLYQKQFY QPFINSRVIE LAFRHILGRG
     PSSREEVQKY FSIISNGGLP ALVDALVDSA EYSDYFGEET VPYLRGLGQE AQECRNWGPQ
     QDLFNYSAPF RKVPQFITTF AAYDRPLPDQ HPYGSGNDPL EIQFGAIFPK ETRNPSTSPA
     PFGKDTRRIL IHQGPGINNQ VSNPSARGLA PGSLGPKVFK LDQLPGTIGK KAAKGASVKF
     SESSTQAVIK ATYLQVFGRD VYEGQRLKVQ EIKLENGEIS VRDFVRALAK SDLFRKLYWT
     PFYVCKAIEY IHRRLLGRPT YGRQENNKYF DIASKKGLYA VVDAILDSLE YTETFGEDTV
     PYERYLTPAG VALRQLRVGT IREDVANVEK QETPRFVELG TVKENRTQPD IDFRINQGVT
     KQREQTKVFK RVAGIKDKAA IKTLISAAYR QIFERDIAPY IAQNEFSGWE SKLGNGEITV
     KEFIEGLGYS NLYLKEFYTP YPNTKVIELG TKHFLGRAPI DQAEIRKYNQ ILATQGIRAF
     INALVNSQEY NEVFGEDTVP YRRFPTLPAA NFPNTQKLYN QLTKQNNDVV IPSFKPVQAR
     IQSDKTPILA KAIADLAAQA KQMDKSKPLF IELGRSYNDG RGQSVEVGVG TTRRKPARIY
     RLTNGIGQAE KQLVINAIYR QVLDVFSGQV PDYYRRTELD SKLRNGEISV REFVREIASS
     EIYRKRFYTP YPNTKVIEFL FRHLLGRAPA TQGEIRQYNK LLADNGLRAA VEAIVDSPEY
     SRYFGEDVVP YPRFPSLPAG NYLGSVQAAA DLVKQSWSSL SPSTLTGRPG DR
 
 
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