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