APCE_SYNP2
ID APCE_SYNP2 Reviewed; 886 AA.
AC O68973;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Phycobiliprotein ApcE;
DE EC=4.-.-.-;
DE AltName: Full=Phycobilisome core-membrane linker phycobiliprotein ApcE;
GN Name=apcE; OrderedLocusNames=SYNPCC7002_A2009;
OS Synechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6) (Agmenellum
OS quadruplicatum).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=32049;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 27264 / PCC 7002 / PR-6;
RA Zhou J., Stirewalt V.L., Bryant D.A.;
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27264 / PCC 7002 / PR-6;
RA Li T., Zhao J., Zhao C., Liu Z., Zhao F., Marquardt J., Nomura C.T.,
RA Persson S., Detter J.C., Richardson P.M., Lanz C., Schuster S.C., Wang J.,
RA Li S., Huang X., Cai T., Yu Z., Luo J., Zhao J., Bryant D.A.;
RT "Complete sequence of Synechococcus sp. PCC 7002.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION IN BILIN LYASE ACTIVITY, AND CHROMOPHORE ATTACHMENT.
RC STRAIN=ATCC 27264 / PCC 7002 / PR-6;
RX PubMed=20228104; DOI=10.1128/aem.03100-09;
RA Biswas A., Vasquez Y.M., Dragomani T.M., Kronfel M.L., Williams S.R.,
RA Alvey R.M., Bryant D.A., Schluchter W.M.;
RT "Biosynthesis of cyanobacterial phycobiliproteins in Escherichia coli:
RT chromophorylation efficiency and specificity of all bilin lyases from
RT Synechococcus sp. strain PCC 7002.";
RL Appl. Environ. Microbiol. 76:2729-2739(2010).
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 (By similarity). Has intrinsic bilin lyase activity.
CC {ECO:0000250, ECO:0000269|PubMed:20228104}.
CC -!- SUBUNIT: Heterodimer with 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.
CC -!- SIMILARITY: Belongs to the phycobilisome linker protein family.
CC {ECO:0000255|PROSITE-ProRule:PRU00775}.
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DR EMBL; AF059340; AAC14723.2; -; Genomic_DNA.
DR EMBL; CP000951; ACA99995.1; -; Genomic_DNA.
DR RefSeq; WP_012307618.1; NC_010475.1.
DR PDB; 7EXT; EM; 3.50 A; 03/13=1-886.
DR PDBsum; 7EXT; -.
DR AlphaFoldDB; O68973; -.
DR SMR; O68973; -.
DR STRING; 32049.SYNPCC7002_A2009; -.
DR EnsemblBacteria; ACA99995; ACA99995; SYNPCC7002_A2009.
DR KEGG; syp:SYNPCC7002_A2009; -.
DR eggNOG; COG0237; Bacteria.
DR eggNOG; COG0448; Bacteria.
DR HOGENOM; CLU_007759_0_0_3; -.
DR OMA; FYTPYPN; -.
DR Proteomes; UP000001688; 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..886
FT /note="Phycobiliprotein ApcE"
FT /id="PRO_0000403184"
FT DOMAIN 243..422
FT /note="PBS-linker 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00775"
FT DOMAIN 499..675
FT /note="PBS-linker 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00775"
FT DOMAIN 696..873
FT /note="PBS-linker 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00775"
FT BINDING 186
FT /ligand="(2R,3E)-phycocyanobilin"
FT /ligand_id="ChEBI:CHEBI:85275"
FT /note="covalent, via 1 link"
FT /evidence="ECO:0000305"
SQ SEQUENCE 886 AA; 99273 MW; 72421AC082718724 CRC64;
MTIKASGGSS LARPQLYQTV PLSNISQAEQ QDRYLESGEL TALKTFYDSG LKRLAIAQAI
KLSSQLIVSR AANRIFAGGS PLAYLDQPET DTDDSDLGVS MAVGDASGAT GIFGGVKNLF
LGSGGGKIPA GFRPISVSRY GPRNMTKSLR DMAWFLRYTT YAIVAGDPSI LVVNTRGLKE
VIENACSIPA TIVAIQEMKA ASLDLFRGDR EAQETVVQYF DVLITEMQTQ VPNDKLRQRP
SIDAQGLQLP QSYFNAAEKR QKFVMKPGLS ALEKNSVVKA AYRQIFERDI TRAYSQSISY
LESQVKSGDI SMKEFVRRLA KSPLYRKQFF EPFINSRALE LAFRHILGRG PSSREEVQEY
FAIVSSGGLA ALVDALVDSQ EYADYFGEET VPYLRGLGQE AQECRNWGMQ QDLFKYSAPF
RKVPQFITTF ASYNQPLPDQ HVYGSGNDAL EIQFGAIFPK ATRSPSASPA PFNKDTRRIL
IHRGPGINNQ LGNPRARATQ PGSLGAKVFR LNNELPSGKT TNVSFSESAT QKVIEAAYRQ
VFGRMVYAGQ RQKVAEIKLE NGEITLREFI RALAKSDVFR NTYWSSLYVT KAVEYIHRRL
LGRPTYGRQE INSYFDTCAK KGFYALVDAI IDSKEYEEAF GEDTVPYERY LTPGGYSLRQ
TRPGALREDV GVKVKVEKTA RFIELGTSST KNLPVTDVDA RLKQGVNIQR QQTKAFKLTD
TFNKVELKTA IAAAYRQIFE RDIEPYIVDA QFTALESKLG NREINMKEFI EGLGCSELYQ
KEFYTPYPNT KVIEMGTKHF LGRAPLDQQE IRKYNQILAS QGLKAFIGAM VNSMEYLDNF
GEDTVPFRRF PTLPAANFPN TERLYNQLTK QNRDLVVPSF EPAVKR
