RAF1_SYNY3
ID RAF1_SYNY3 Reviewed; 358 AA.
AC Q55875;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=RuBisCO accumulation factor 1 {ECO:0000255|HAMAP-Rule:MF_00856, ECO:0000303|PubMed:28108864};
GN Name=raf1 {ECO:0000255|HAMAP-Rule:MF_00856, ECO:0000303|PubMed:28108864};
GN OrderedLocusNames=sll0102;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
RN [2]
RP POSSIBLE FUNCTION, SUBUNIT, AND DISRUPTION PHENOTYPE.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=28108864; DOI=10.1007/s11120-017-0336-4;
RA Kolesinski P., Rydzy M., Szczepaniak A.;
RT "Is RAF1 protein from Synechocystis sp. PCC 6803 really needed in the
RT cyanobacterial Rubisco assembly process?";
RL Photosyn. Res. 132:135-148(2017).
RN [3]
RP ERRATUM.
RX PubMed=28181142; DOI=10.1007/s11120-017-0344-4;
RA Kolesinski P., Rydzy M., Szczepaniak A.;
RT "Is RAF1 protein from Synechocystis sp. PCC 6803 really needed in the
RT cyanobacterial Rubisco assembly process?";
RL Photosyn. Res. 132:149-149(2017).
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}.
CC -!- FUNCTION: Required for optimal reconstitution of RbcL(8) upon
CC expression in E.coli (PubMed:28108864). Has been suggested to be
CC involved in RuBisCO recycling and homeostasis rather than assembly
CC (Probable). {ECO:0000269|PubMed:28108864, ECO:0000305|PubMed:28108864}.
CC -!- SUBUNIT: Homodimer. Forms an RbcL(8)-Raf1(8) complex. Forms complexes
CC of many stoichiometries with RbcL with and without RbcS. RbcX and Raf1
CC can bind simultaneously to RbcL (By similarity). Interacts with both
CC RuBisCO subunits (ccbL, ccbS), GroEL, DnaK and alpha and beta
CC phycocyanin (cpcA, cpcB) in pull-down experiments with tagged protein.
CC C-terminally tagged Raf1 does not interact with either RuBisCO subunit,
CC suggesting its C-terminus is involved in binding (PubMed:28108864).
CC {ECO:0000255|HAMAP-Rule:MF_00856, ECO:0000269|PubMed:28108864}.
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 -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, no change in RuBisCO large subunit levels, no change in
CC RuBisCO carboxylase activity. During sulfur starvation deletion cells
CC are protected against protein degradation.
CC {ECO:0000269|PubMed:28108864}.
CC -!- SIMILARITY: Belongs to the RAF family. {ECO:0000255|HAMAP-
CC Rule:MF_00856}.
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DR EMBL; BA000022; BAA10636.1; -; Genomic_DNA.
DR PIR; S76692; S76692.
DR AlphaFoldDB; Q55875; -.
DR SMR; Q55875; -.
DR DIP; DIP-48799N; -.
DR IntAct; Q55875; 2.
DR STRING; 1148.1208468; -.
DR PaxDb; Q55875; -.
DR EnsemblBacteria; BAA10636; BAA10636; BAA10636.
DR KEGG; syn:sll0102; -.
DR eggNOG; ENOG502Z7IG; Bacteria.
DR InParanoid; Q55875; -.
DR OMA; IVASQVY; -.
DR PhylomeDB; Q55875; -.
DR Proteomes; UP000001425; 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; IEA:UniProt.
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 Carbon dioxide fixation; Chaperone; Cytoplasm; Photosynthesis;
KW Reference proteome.
FT CHAIN 1..358
FT /note="RuBisCO accumulation factor 1"
FT /id="PRO_0000451579"
FT REGION 11..194
FT /note="N-terminal alpha-helix"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00856"
FT REGION 218..344
FT /note="C-terminal beta-sheet"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00856"
SQ SEQUENCE 358 AA; 40097 MW; 6572E4E8BC4ECA89 CRC64;
MTHSPESNPT VSAAEAAELI RSLLHKEGTW VDWGKKCQQL QKAGYGAEEI FEQSGFQKVQ
QNLVIVASQV YESLVKQGID ETVLSYYRGP KSDVLYELRI LNHQQRAIAA VEAQQKNLAA
DEAKELAKAF QEFGYLSQLP EGFTDHPGDA LAYQCWKLAR QKKNLPERTR LIVKGLKFAH
SPNARQAIEK LLTDLTAQPS RKAPLVPVFR LEEDQEAARL IPVAGTFPLQ PQAVQAVQSL
EQVEPFGLVS YQGEGAVVPV PQWQAILTAE DPVAIFCPAG QVSESLARKD EQVLVVVDRS
KKIWNDGSYF LLNQGETVAI QWCETEPERE ILAQVVLVLR PKKIFDANNL REPWQMDD
