APCE_MICDP
ID APCE_MICDP Reviewed; 1080 AA.
AC P16566;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Phycobiliprotein ApcE;
DE EC=4.-.-.-;
DE AltName: Full=Core-membrane linker protein;
DE AltName: Full=L-CM 92;
DE AltName: Full=Phycobilisome 120 kDa linker polypeptide, core;
GN Name=apcE;
OS Microchaete diplosiphon (Fremyella diplosiphon).
OC Bacteria; Cyanobacteria; Nostocales; Rivulariaceae; Microchaete.
OX NCBI_TaxID=1197;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2107546; DOI=10.1073/pnas.87.6.2152;
RA Houmard J., Capuano V., Colombano M.V., Coursin T., de Marsac N.;
RT "Molecular characterization of the terminal energy acceptor of
RT cyanobacterial phycobilisomes.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:2152-2156(1990).
RN [2]
RP PROTEIN SEQUENCE OF 2-11.
RX PubMed=1551428; DOI=10.1016/0014-5793(92)80318-b;
RA Glauser M., Sidler W.A., Graham K.W., Bryant D.A., Frank G., Wehrli E.,
RA Zuber H.;
RT "Three C-phycoerythrin-associated linker polypeptides in the phycobilisome
RT of green-light-grown Calothrix sp. PCC 7601 (cyanobacteria).";
RL FEBS Lett. 297:19-23(1992).
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.
CC -!- FUNCTION: Has intrinsic bilin lyase activity. {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.
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; M20806; AAA24873.1; -; Genomic_DNA.
DR PIR; A35088; A35088.
DR AlphaFoldDB; P16566; -.
DR SMR; P16566; -.
DR PRIDE; P16566; -.
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 Antenna complex; Bile pigment; Chromophore; Direct protein sequencing;
KW Electron transport; Lyase; Membrane; Photosynthesis; Phycobilisome; Repeat;
KW Thylakoid; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1551428"
FT CHAIN 2..1080
FT /note="Phycobiliprotein ApcE"
FT /id="PRO_0000199263"
FT DOMAIN 252..432
FT /note="PBS-linker 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00775"
FT DOMAIN 514..693
FT /note="PBS-linker 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00775"
FT DOMAIN 710..888
FT /note="PBS-linker 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00775"
FT DOMAIN 922..1080
FT /note="PBS-linker 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00775"
FT REGION 18..76
FT /note="Phycobilin-like 1"
FT REGION 77..144
FT /note="Phycobilin-like loop"
FT REGION 145..237
FT /note="Phycobilin-like 2"
FT REGION 906..930
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 195
FT /ligand="(2R,3E)-phycocyanobilin"
FT /ligand_id="ChEBI:CHEBI:85275"
FT /note="covalent, via 1 link"
FT /evidence="ECO:0000250"
FT CONFLICT 10
FT /note="S -> SS (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1080 AA; 120457 MW; 9979E5E5F86766C9 CRC64;
MSVKASGGSS VARPQLYQTL AVATITQAEQ QDRFLGTGEL NELATYFASG AKRLEIAQTL
TENSEIIVSR AANRIFVGGS PMSFLEKPRE AELAMATVAP GNVQEGMKLG TVTYVESRGG
FLENLRSIFN SSPSGPTPPG FRPINVARYG PSNMAKSLRD LSWFLRYATY AIVAGDPNII
AVNTRGLREI IENACSGEPT IVALQEIKAA SLSFFRQDAK ATEIVSQYMD VLLTEFKAAT
PSNKLRQRPS GDQQGLQLPQ IYFEAAERRP KFVMKPGLSA SEKNEVIRAA YRQIFERDIT
RAYSLSVSDL ESKVKNGDIS MKEFVRRLAK SPLYQKQFYQ PFINSRVIEL AFRHILGRGP
SSREEVQKYF SIISNGGLPA LVDALVDSPE YSDYFGEETV PYLRGLGQEA QECRNWGPQQ
DLFNYSAPFR KVPQFITTFA CLYDRPLPDQ HPYGSGNDPL EIQFGAIFPK ETRNPNTSPA
PFSKDTRRIL INQGPGINSQ VSNPGARGEF PGSLGPKVFR LDQLPGTIGK KAAKGASIKF
SESSTQAVIK AAYLQVFGRD VYEGQRLKVQ EIKLENGQLS VREFIRALAK SDVFRKTYWT
SLYVCKAIEY IHRRLLGRPT YGRQEINKYF DIAAKQGFYA VVDAIINSVE YSEAFGEDTV
PYERYLTPSG VALRQLRVGS IREDVGGKVQ KQETPLFVTL GTVTDTRTEP DIQFRINQGV
SKQREQTKVF KQVANISDKA AVQTLISAAY RQIFERDVAP YIAKNEFSAL ESKLSNGEIT
VKEFIEGLGY SNLYIKEFYT PYPNTKVIEL GTKHFLGRAP LDQVEIRKYN QILATQGIRA
FIGALVSSAE YAEVFGEDTV PYRRYPTLPA ANFPNTEKLY NQLTKQNDDL VVPSFKTVQP
RLTLAGTSSS GRNGFTDLGR SSTSAQGQLG ETANRCKPAR IYRLSGTNQA ETQLVINAIY
SQVLDLFSSD IPANYRLNAL EGKLQTGEIS VREFVRELAS SDIYCDRFYT PYPSAKVIEF
LYRHLLGRAP ATQEEISEYN KLMASRGLRA VVEAIVDSQE YARYFGEDVV PYPRSSSLGN
