APCB_MASLA
ID APCB_MASLA Reviewed; 161 AA.
AC P00318;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 2.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Allophycocyanin beta chain;
GN Name=apcB;
OS Mastigocladus laminosus (Fischerella sp.).
OC Bacteria; Cyanobacteria; Nostocales; Hapalosiphonaceae; Mastigocladus.
OX NCBI_TaxID=83541;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=6792029; DOI=10.1515/bchm2.1981.362.1.611;
RA Sidler W., Gysi J., Isker E., Zuber H.;
RT "The complete amino acid sequence of both subunits of allophycocyanin, a
RT light harvesting protein-pigment complex from the cyanobacterium
RT Mastigocladus laminosus.";
RL Hoppe-Seyler's Z. Physiol. Chem. 362:611-628(1981).
RN [2]
RP PROTEIN SEQUENCE OF 59-82, AND METHYLATION AT ASN-71.
RX PubMed=3122783; DOI=10.1515/bchm3.1987.368.2.1401;
RA Ruembeli R., Suter F., Wirth M., Sidler W., Zuber H.;
RT "Isolation and localization of N4-methylasparagine in phycobiliproteins
RT from the cyanobacterium Mastigocladus laminosus.";
RL Biol. Chem. Hoppe-Seyler 368:1401-1406(1987).
RN [3]
RP PROTEIN SEQUENCE OF 55-82, AND METHYLATION AT ASN-71.
RA Ruembeli R., Suter F., Wirth M., Sidler W., Zuber H.;
RT "Gamma-N-methylasparagine in phycobiliproteins from the cyanobacteria
RT Mastigocladus laminosus and Calothrix.";
RL FEBS Lett. 221:1-2(1987).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), AND METHYLATION AT ASN-71.
RC STRAIN=PCC 7603;
RX PubMed=9990029; DOI=10.1073/pnas.96.4.1363;
RA Reuter W., Wiegand G., Huber R., Than M.E.;
RT "Structural analysis at 2.2 A of orthorhombic crystals presents the
RT asymmetry of the allophycocyanin-linker complex, AP.LC7.8, from
RT phycobilisomes of Mastigocladus laminosus.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:1363-1368(1999).
CC -!- FUNCTION: Light-harvesting photosynthetic bile pigment-protein from the
CC phycobiliprotein complex. Allophycocyanin has a maximum absorption at
CC approximately 650 nanometers.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta chain.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane; Peripheral membrane
CC protein; Cytoplasmic side. Note=Forms the core of the phycobilisome.
CC -!- PTM: Contains one covalently linked phycocyanobilin chromophore.
CC -!- SIMILARITY: Belongs to the phycobiliprotein family. {ECO:0000305}.
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DR PDB; 1B33; X-ray; 2.30 A; B/D/F/I/K/M=1-161.
DR PDBsum; 1B33; -.
DR AlphaFoldDB; P00318; -.
DR SMR; P00318; -.
DR iPTMnet; P00318; -.
DR EvolutionaryTrace; P00318; -.
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:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR CDD; cd12126; APC_beta; 1.
DR Gene3D; 1.10.490.20; -; 1.
DR InterPro; IPR006245; ApcB.
DR InterPro; IPR009050; Globin-like_sf.
DR InterPro; IPR012128; Phycobilisome_asu/bsu.
DR InterPro; IPR038719; Phycobilisome_asu/bsu_sf.
DR PANTHER; PTHR34011:SF3; PTHR34011:SF3; 1.
DR Pfam; PF00502; Phycobilisome; 1.
DR PIRSF; PIRSF000081; Phycocyanin; 1.
DR SUPFAM; SSF46458; SSF46458; 1.
DR TIGRFAMs; TIGR01337; apcB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antenna complex; Bile pigment; Chromophore;
KW Direct protein sequencing; Electron transport; Membrane; Methylation;
KW Photosynthesis; Phycobilisome; Thylakoid; Transport.
FT CHAIN 1..161
FT /note="Allophycocyanin beta chain"
FT /id="PRO_0000199099"
FT BINDING 81
FT /ligand="(2R,3E)-phycocyanobilin"
FT /ligand_id="ChEBI:CHEBI:85275"
FT /note="covalent, via 1 link"
FT MOD_RES 71
FT /note="N4-methylasparagine"
FT /evidence="ECO:0000269|PubMed:3122783,
FT ECO:0000269|PubMed:9990029, ECO:0000269|Ref.3"
FT CONFLICT 59..60
FT /note="SL -> KT (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 67
FT /note="R -> L (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 71
FT /note="N -> D (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 4..13
FT /evidence="ECO:0007829|PDB:1B33"
FT TURN 14..16
FT /evidence="ECO:0007829|PDB:1B33"
FT HELIX 21..46
FT /evidence="ECO:0007829|PDB:1B33"
FT HELIX 48..59
FT /evidence="ECO:0007829|PDB:1B33"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:1B33"
FT TURN 64..66
FT /evidence="ECO:0007829|PDB:1B33"
FT HELIX 75..98
FT /evidence="ECO:0007829|PDB:1B33"
FT HELIX 102..107
FT /evidence="ECO:0007829|PDB:1B33"
FT HELIX 112..119
FT /evidence="ECO:0007829|PDB:1B33"
FT HELIX 123..160
FT /evidence="ECO:0007829|PDB:1B33"
SQ SEQUENCE 161 AA; 17374 MW; 18E7DD78D7178350 CRC64;
MQDAITAVIN SSDVQGKYLD TAALEKLKSY FSTGELRVRA ATTIAANAAA IVKEAVAKSL
LYSDITRPGG NMYTTRRYAA CIRDLDYYLR YATYAMLAGD PSILDERVLN GLKETYNSLG
VPISATVQAI QAMKEVTASL VGPDAGKEMG VYFDYICSGL S