APCE_SYNP6
ID APCE_SYNP6 Reviewed; 705 AA.
AC P28035; Q5N2U5;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Phycobiliprotein ApcE;
DE EC=4.-.-.-;
DE AltName: Full=Anchor polypeptide LCM;
DE AltName: Full=Phycobilisome linker polypeptide;
GN Name=apcE; OrderedLocusNames=syc1185_d;
OS Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) (Anacystis
OS nidulans).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=269084;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1901865; DOI=10.1016/s0021-9258(20)89636-7;
RA Capuano V., Braux A.-S., Tandeau de Marsac N., Houmard J.;
RT "The 'anchor polypeptide' of cyanobacterial phycobilisomes. Molecular
RT characterization of the Synechococcus sp. PCC 6301 apcE gene.";
RL J. Biol. Chem. 266:7239-7247(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27144 / PCC 6301 / SAUG 1402/1;
RX PubMed=17211581; DOI=10.1007/s11120-006-9122-4;
RA Sugita C., Ogata K., Shikata M., Jikuya H., Takano J., Furumichi M.,
RA Kanehisa M., Omata T., Sugiura M., Sugita M.;
RT "Complete nucleotide sequence of the freshwater unicellular cyanobacterium
RT Synechococcus elongatus PCC 6301 chromosome: gene content and
RT organization.";
RL Photosyn. Res. 93:55-67(2007).
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: Phycobilisomes of this organism are composed of a two cylinder
CC core, from which six rods radiate. The core is mainly composed of
CC allophycocyanin alpha and beta chains, and of three minor components:
CC the allophycocyanin alpha-B chain, a 18.3 kDa polypeptide, and the
CC anchor polypeptide L-CM (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane; Peripheral membrane
CC protein; Cytoplasmic side. Note=Anchors the phycobilisome
CC perpendicularly to the cytoplasmic surface of the thylakoid membrane.
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; X53425; CAA37514.1; -; Genomic_DNA.
DR EMBL; AP008231; BAD79375.1; -; Genomic_DNA.
DR PIR; A39784; A39784.
DR RefSeq; WP_011243497.1; NC_006576.1.
DR AlphaFoldDB; P28035; -.
DR SMR; P28035; -.
DR STRING; 269084.syc1185_d; -.
DR EnsemblBacteria; BAD79375; BAD79375; syc1185_d.
DR KEGG; syc:syc1185_d; -.
DR eggNOG; COG0448; Bacteria.
DR OMA; MGWFLRY; -.
DR Proteomes; UP000001175; 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; -; 2.
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; 2.
DR Pfam; PF00502; Phycobilisome; 2.
DR SUPFAM; SSF46458; SSF46458; 1.
DR PROSITE; PS51445; PBS_LINKER; 2.
PE 3: Inferred from homology;
KW Antenna complex; Bile pigment; Chromophore; Electron transport; Lyase;
KW Membrane; Photosynthesis; Phycobilisome; Repeat; Thylakoid; Transport.
FT CHAIN 1..705
FT /note="Phycobiliprotein ApcE"
FT /id="PRO_0000199264"
FT DOMAIN 253..433
FT /note="PBS-linker 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00775"
FT DOMAIN 514..691
FT /note="PBS-linker 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00775"
FT REGION 18..76
FT /note="Phycobilin-like 1"
FT REGION 77..145
FT /note="Phycobilin-like loop"
FT REGION 146..238
FT /note="Phycobilin-like 2"
FT REGION 685..705
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 122..124
FT /note="FFS -> LLFH (in Ref. 1; CAA37514)"
FT /evidence="ECO:0000305"
FT CONFLICT 243
FT /note="S -> C (in Ref. 1; CAA37514)"
FT /evidence="ECO:0000305"
FT CONFLICT 411
FT /note="A -> R (in Ref. 1; CAA37514)"
FT /evidence="ECO:0000305"
FT CONFLICT 521..522
FT /note="VA -> AC (in Ref. 1; CAA37514)"
FT /evidence="ECO:0000305"
FT CONFLICT 681..705
FT /note="ASEKVKASLRPAAGAQERRPEVGRR -> SL (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 705 AA; 78807 MW; 75549DB322CCB852 CRC64;
MTVTASGGSS LARPQLYQTV PGSTIVQAEQ QDRFPQQGEL RELSSYFQSG LKRLAIAEII
TRNSDTIVSR AANRIFVGGS PLAYIERPKV DPRNLRSAEE QRAREAKLGT VTFVESSGGG
GFFSGLTAAL GGAGAVRIPS GFRPINVARY GPRNMQKSLR DMSWFLRYIT YAIVAGDPNI
LVVNVRGLRE IIEKACSTPA TLVALQDMRA TSAGYFRNDP EAQQLVKDYF DVLIREFEAP
TPSLKQRQRF AEDQQGLALP QSYANAAERR PKFVIKSTLS TVEKNEAIKA AYRQVFERDI
TRAYSQKVSD LESKVKNGEI STKEFIRRLG KSPLYRQQFH DRFVNSRVIE LAFRHFLGRG
ISSAEEFTRY FDLLSAKGFA ALIDALVDSQ EYADYFGEET VPYLRGLGQE AQECRNWGVQ
QELFKYSAPF VKVPQFVTLF GEYKQPLLDQ HPYGAGNDPL EIQFGAIFPS RTVNNRTNPA
PFGKDTRRLL VSKGGVNNQV GSAAFQQSGT TPTKIFKLTQ VAAGSSSIRS KSVGNPSIRQ
TESTTQAVIR AAYRQVFGRD LYEGQRLTVP EIKLENGEIT VREFVRQIAK SETFRKLYWN
NLYVVKAVEY IHRRLLGRPT TGRAEINAYF DISAKKGFYA LVDAILDSPE YIAAFGEDTV
PYERYITPKG LALRSVRGLE ASEKVKASLR PAAGAQERRP EVGRR
