RAF1_NOSS1
ID RAF1_NOSS1 Reviewed; 361 AA.
AC Q8YLP6;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=RuBisCO accumulation factor 1 {ECO:0000255|HAMAP-Rule:MF_00856, ECO:0000303|PubMed:32451445};
GN Name=raf1 {ECO:0000255|HAMAP-Rule:MF_00856, ECO:0000303|PubMed:32451445};
GN OrderedLocusNames=all5250;
OS Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=103690;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT "Complete genomic sequence of the filamentous nitrogen-fixing
RT cyanobacterium Anabaena sp. strain PCC 7120.";
RL DNA Res. 8:205-213(2001).
RN [2] {ECO:0007744|PDB:6KKM, ECO:0007744|PDB:6KKN, ECO:0007744|PDB:6LRR}
RP X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS), X-RAY CRYSTALLOGRAPHY (3.00
RP ANGSTROMS) IN COMPLEX WITH RUBISCO LARGE SUBUNIT (RBCL), STRUCTURE BY
RP ELECTRON MICROSCOPY (3.37 ANGSTROMS) OF 206-361 IN COMPLEX WITH RUBISCO,
RP FUNCTION, SUBUNIT, DOMAIN, AND MUTAGENESIS OF 354-LYS--GLU-361 AND GLU-361.
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=32451445; DOI=10.1038/s41477-020-0665-8;
RA Xia L.Y., Jiang Y.L., Kong W.W., Sun H., Li W.F., Chen Y., Zhou C.Z.;
RT "Molecular basis for the assembly of RuBisCO assisted by the chaperone
RT Raf1.";
RL Nat. Plants 6:708-717(2020).
CC -!- FUNCTION: A major RuBisCO chaperone. Acts after GroEL-GroES chaperonin
CC to fold and/or assemble the large subunit of RuBisCO (ccbL, rbcL).
CC Cooperates with RbcX in RbcL folding, plays the major role in assembly
CC of dimers into RbcL(8)-Raf1(8) intermediate complexes. RbcS replaces
CC Raf1, leading to holoenzyme formation. {ECO:0000255|HAMAP-
CC Rule:MF_00856, ECO:0000269|PubMed:32451445}.
CC -!- FUNCTION: In vitro acts as an antagonist to CcmM35, suggesting it might
CC regulate RuBisCO condensation and decondensation.
CC {ECO:0000269|PubMed:32451445}.
CC -!- SUBUNIT: Homodimer. Forms an RbcL(8)-Raf1(8) complex. Each Raf1 dimer
CC clamps the exterior of an RbcL dimer, protecting it. The extreme C-
CC terminus (residues 354-361) inserts into the catalytic pocket of RbcL
CC where the Glu-361 forms a salt bridge with 'Lys-202'. This insertion
CC probably contributes to the assembly of RbcL(8). Forms complexes of
CC many stoichiometries with RbcL with and without RbcS. RbcX and Raf1 can
CC bind simultaneously to RbcL. {ECO:0000269|PubMed:32451445}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00856}.
CC -!- DOMAIN: Has 3 domains, the N-terminal alpha-helical domain, an extended
CC flexible linker and the C-terminal beta-sheet domain. The 2 C-terminal
CC beta-sheet domains are swapped and pack against each other to form the
CC dimer interface. {ECO:0000255|HAMAP-Rule:MF_00856,
CC ECO:0000269|PubMed:32451445}.
CC -!- SIMILARITY: Belongs to the RAF family. {ECO:0000255|HAMAP-
CC Rule:MF_00856}.
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DR EMBL; BA000019; BAB76949.1; -; Genomic_DNA.
DR PIR; AB2462; AB2462.
DR RefSeq; WP_010999374.1; NZ_RSCN01000005.1.
DR PDB; 6KKM; X-ray; 3.00 A; E/F/G/H=1-361.
DR PDB; 6KKN; X-ray; 2.85 A; A=1-361.
DR PDB; 6LRR; EM; 3.37 A; I/J/K/L/M/N/O/P=206-361.
DR PDBsum; 6KKM; -.
DR PDBsum; 6KKN; -.
DR PDBsum; 6LRR; -.
DR AlphaFoldDB; Q8YLP6; -.
DR SMR; Q8YLP6; -.
DR STRING; 103690.17134389; -.
DR EnsemblBacteria; BAB76949; BAB76949; BAB76949.
DR KEGG; ana:all5250; -.
DR eggNOG; ENOG502Z7IG; Bacteria.
DR OMA; IVASQVY; -.
DR OrthoDB; 951992at2; -.
DR Proteomes; UP000002483; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-KW.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR GO; GO:0110102; P:ribulose bisphosphate carboxylase complex assembly; IDA:UniProtKB.
DR HAMAP; MF_00856; Raf1; 1.
DR InterPro; IPR037494; RAF1.
DR InterPro; IPR040858; Raf1_C.
DR InterPro; IPR046382; Raf1_cyn.
DR InterPro; IPR040781; Raf1_HTH.
DR InterPro; IPR041358; Raf1_N.
DR PANTHER; PTHR35299; PTHR35299; 1.
DR Pfam; PF18579; Raf1_HTH; 1.
DR Pfam; PF18578; Raf1_N; 1.
DR Pfam; PF18087; RuBisCo_chap_C; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbon dioxide fixation; Chaperone; Cytoplasm;
KW Photosynthesis; Reference proteome.
FT CHAIN 1..361
FT /note="RuBisCO accumulation factor 1"
FT /id="PRO_0000451576"
FT REGION 16..197
FT /note="N-terminal alpha-helix"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00856,
FT ECO:0000305|PubMed:32451445"
FT REGION 221..347
FT /note="C-terminal beta-sheet"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00856,
FT ECO:0000305|PubMed:32451445"
FT MUTAGEN 354..361
FT /note="Missing: Forms more RbcL(2)-Raf1(2) but little
FT RbcL(8)-Raf1(8)."
FT /evidence="ECO:0000269|PubMed:32451445"
FT MUTAGEN 361
FT /note="E->EHHH: Forms more RbcL(2)-Raf1(2) but little
FT RbcL(8)-Raf1(8)."
FT /evidence="ECO:0000269|PubMed:32451445"
FT HELIX 18..28
FT /evidence="ECO:0007829|PDB:6KKN"
FT HELIX 33..45
FT /evidence="ECO:0007829|PDB:6KKN"
FT HELIX 50..56
FT /evidence="ECO:0007829|PDB:6KKN"
FT HELIX 61..79
FT /evidence="ECO:0007829|PDB:6KKN"
FT HELIX 84..92
FT /evidence="ECO:0007829|PDB:6KKN"
FT HELIX 95..99
FT /evidence="ECO:0007829|PDB:6KKN"
FT TURN 100..103
FT /evidence="ECO:0007829|PDB:6KKN"
FT HELIX 106..118
FT /evidence="ECO:0007829|PDB:6KKN"
FT HELIX 123..136
FT /evidence="ECO:0007829|PDB:6KKN"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:6KKM"
FT HELIX 150..164
FT /evidence="ECO:0007829|PDB:6KKN"
FT STRAND 167..169
FT /evidence="ECO:0007829|PDB:6KKN"
FT HELIX 170..181
FT /evidence="ECO:0007829|PDB:6KKN"
FT HELIX 185..196
FT /evidence="ECO:0007829|PDB:6KKN"
FT STRAND 216..218
FT /evidence="ECO:0007829|PDB:6KKN"
FT STRAND 222..231
FT /evidence="ECO:0007829|PDB:6KKN"
FT HELIX 234..238
FT /evidence="ECO:0007829|PDB:6KKN"
FT TURN 247..250
FT /evidence="ECO:0007829|PDB:6KKN"
FT STRAND 251..254
FT /evidence="ECO:0007829|PDB:6KKM"
FT STRAND 259..263
FT /evidence="ECO:0007829|PDB:6KKN"
FT HELIX 267..271
FT /evidence="ECO:0007829|PDB:6KKN"
FT STRAND 273..281
FT /evidence="ECO:0007829|PDB:6KKN"
FT HELIX 282..284
FT /evidence="ECO:0007829|PDB:6KKN"
FT STRAND 295..301
FT /evidence="ECO:0007829|PDB:6KKN"
FT STRAND 311..316
FT /evidence="ECO:0007829|PDB:6KKN"
FT STRAND 318..325
FT /evidence="ECO:0007829|PDB:6KKN"
FT STRAND 334..342
FT /evidence="ECO:0007829|PDB:6KKN"
FT HELIX 349..352
FT /evidence="ECO:0007829|PDB:6LRR"
SQ SEQUENCE 361 AA; 41009 MW; FAE91E6A407109CA CRC64;
MTELPPNAPN PENATNELAQ ELLRKLRQKQ GNWVEWGQAI ASLQKSGYNP QDIFEATGFE
PVQQNQVIVG SQVYNSLEKS GASAATLAHY ATRGSDVLYE LRLLTHEERA AAGDLTFTHK
VDADEAREIA KAIKDFSRFR ILPEGFSNHP GDAVAYQAWK LARQYSDLQE RSRLIARGLR
FAHSETARKQ IEQLLVDFTV VSQRPAPIPP FFRFDTEDEL PRIVPVVGQL PLKAEELKAV
PLVEEIEPFR LVKFSGEQAW VALPGWQVLL AAEDPVTILA TSDRFPKQNQ TEPGPVLVVV
DRSQREWNDF SYFVVDHDGE LDFQWFETKP EFPILGKVII LVRPRRILDE NVTKDSWQID
E
