RAF1_THEVB
ID RAF1_THEVB Reviewed; 356 AA.
AC Q8DI26;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, 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:25041569};
GN Name=raf1 {ECO:0000255|HAMAP-Rule:MF_00856, ECO:0000303|PubMed:25041569};
GN OrderedLocusNames=tlr1766;
OS Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1).
OC Bacteria; Cyanobacteria; Pseudanabaenales; Thermosynechococcaceae;
OC Thermosynechococcus.
OX NCBI_TaxID=197221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C.,
RA Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takeuchi C., Yamada M., Tabata S.;
RT "Complete genome structure of the thermophilic cyanobacterium
RT Thermosynechococcus elongatus BP-1.";
RL DNA Res. 9:123-130(2002).
RN [2]
RP FUNCTION, INTERACTION WITH RBCL, AND SUBCELLULAR LOCATION.
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=25041569; DOI=10.1111/febs.12928;
RA Kolesinski P., Belusiak I., Czarnocki-Cieciura M., Szczepaniak A.;
RT "Rubisco Accumulation Factor 1 from Thermosynechococcus elongatus
RT participates in the final stages of ribulose-1,5-bisphosphate
RT carboxylase/oxygenase assembly in Escherichia coli cells and in vitro.";
RL FEBS J. 281:3920-3932(2014).
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 RuBisCO upon
CC expression of rbcL-rbcS subunits in E.coli. Only interacts with the
CC large subunit (cbbL, rbcL). Probably acts in the final stages of
CC RuBisCO assembly, possibly participating in the addition of the small
CC subunit (ccbS, rbcS). {ECO:0000269|PubMed:25041569}.
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. {ECO:0000255|HAMAP-Rule:MF_00856,
CC ECO:0000305|PubMed:25041569}.
CC -!- INTERACTION:
CC Q8DI26; Q8DIS5: cbbL; NbExp=2; IntAct=EBI-9639332, EBI-9639313;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00856,
CC ECO:0000269|PubMed:25041569}. Note=Interacts with the large subunit of
CC RuBisCO in the cytoplasm. {ECO:0000269|PubMed:12240834}.
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 -!- SIMILARITY: Belongs to the RAF family. {ECO:0000255|HAMAP-
CC Rule:MF_00856}.
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DR EMBL; BA000039; BAC09318.1; -; Genomic_DNA.
DR RefSeq; NP_682556.1; NC_004113.1.
DR RefSeq; WP_011057603.1; NC_004113.1.
DR AlphaFoldDB; Q8DI26; -.
DR SMR; Q8DI26; -.
DR IntAct; Q8DI26; 1.
DR MINT; Q8DI26; -.
DR STRING; 197221.22295492; -.
DR EnsemblBacteria; BAC09318; BAC09318; BAC09318.
DR KEGG; tel:tlr1766; -.
DR PATRIC; fig|197221.4.peg.1847; -.
DR eggNOG; ENOG502Z7IG; Bacteria.
DR OMA; IVASQVY; -.
DR OrthoDB; 951992at2; -.
DR Proteomes; UP000000440; 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 Carbon dioxide fixation; Chaperone; Cytoplasm; Photosynthesis;
KW Reference proteome.
FT CHAIN 1..356
FT /note="RuBisCO accumulation factor 1"
FT /id="PRO_0000451580"
FT REGION 7..185
FT /note="N-terminal alpha-helix"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00856"
FT REGION 209..342
FT /note="C-terminal beta-sheet"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00856"
SQ SEQUENCE 356 AA; 39462 MW; ABA5654DB71966A9 CRC64;
MSQDQDALTT EVLQRLRRKE GTWQDWGAGC RQLQKQGLSP QAIFEATGIE PIHQNQLITA
LQVSQSLGEA PESVRAYFQT RGSDLLYELR VLSAGDRLAA ATLIVEKQLD VTAVHEVCRA
LKAVSYRKDN SEGFGESVGD RIGRYYWQLA RQQRDLAQRS RLIAQGLRFV ESASGRQALE
KLLTDFTVVP AVNQPRLPLY RLDTAEEVPY LVPVAGTAPL TATVLQQVPR LSCTEVFRVV
AVPQGMSLVA LPAWQVLLNA VDPVAILWPA ADLPAELPPS PEGLPIAQVL LVVDRGLAEW
DRDRYLLIAP SPSEAVQLAW LPEPPTATVV GQLLLVLRPP QVLDESLNRE LWFFEE
