RAF1_SYNP2
ID RAF1_SYNP2 Reviewed; 359 AA.
AC B1XK11;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=RuBisCO accumulation factor 1 {ECO:0000255|HAMAP-Rule:MF_00856, ECO:0000303|PubMed:26237510};
GN Name=raf1 {ECO:0000255|HAMAP-Rule:MF_00856, ECO:0000303|PubMed:26237510};
GN OrderedLocusNames=SYNPCC7002_A2388;
OS Synechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6) (Agmenellum
OS quadruplicatum).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=32049;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27264 / PCC 7002 / PR-6;
RA Li T., Zhao J., Zhao C., Liu Z., Zhao F., Marquardt J., Nomura C.T.,
RA Persson S., Detter J.C., Richardson P.M., Lanz C., Schuster S.C., Wang J.,
RA Li S., Huang X., Cai T., Yu Z., Luo J., Zhao J., Bryant D.A.;
RT "Complete sequence of Synechococcus sp. PCC 7002.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP SUBUNIT, INTERACTION WITH RBCL, AND DOMAIN.
RC STRAIN=ATCC 27264 / PCC 7002 / PR-6;
RX PubMed=26237510; DOI=10.1038/nsmb.3062;
RA Hauser T., Bhat J.Y., Milicic G., Wendler P., Hartl F.U., Bracher A.,
RA Hayer-Hartl M.;
RT "Structure and mechanism of the Rubisco-assembly chaperone Raf1.";
RL Nat. Struct. Mol. Biol. 22:720-728(2015).
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:26237510}.
CC -!- FUNCTION: Raf1 and RbcX are probably functionally redundant; it has
CC been suggested they may cooperate. {ECO:0000269|PubMed:26237510}.
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:26237510}.
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 -!- SIMILARITY: Belongs to the RAF family. {ECO:0000255|HAMAP-
CC Rule:MF_00856}.
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DR EMBL; CP000951; ACB00366.1; -; Genomic_DNA.
DR RefSeq; WP_012307984.1; NC_010475.1.
DR AlphaFoldDB; B1XK11; -.
DR SMR; B1XK11; -.
DR STRING; 32049.SYNPCC7002_A2388; -.
DR EnsemblBacteria; ACB00366; ACB00366; SYNPCC7002_A2388.
DR KEGG; syp:SYNPCC7002_A2388; -.
DR eggNOG; ENOG502Z7IG; Bacteria.
DR HOGENOM; CLU_766477_0_0_3; -.
DR OMA; IVASQVY; -.
DR Proteomes; UP000001688; 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..359
FT /note="RuBisCO accumulation factor 1"
FT /id="PRO_0000451578"
FT REGION 12..195
FT /note="N-terminal alpha-helix"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00856,
FT ECO:0000305|PubMed:26237510"
FT REGION 219..345
FT /note="C-terminal beta-sheet"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00856,
FT ECO:0000305|PubMed:26237510"
SQ SEQUENCE 359 AA; 39911 MW; 8299295556838B1A CRC64;
MIGQPQSPEY KLSPEETDAL FRSLLHKEGT WVEWGVGCQQ LQQSGHSAQE IFEQTGFQTA
QQNMIIVAAQ VYQSIASSGV PEDLLAYCRG PRSDVLYELR ILSHSQRAIA AQVCQAKSLE
FDGAKELARA MQEFARLPQI PDSFTEHPGD AVAYQAWRSA KQKKDLQDRT RLIAKGLKFA
HSATARQKIE QLLSDLTTSP TKAAPLLPLY RYDEDTNVPL LIPVAGSLPL ESDRLLSVPP
LKQASPFNLV TVATATSLVP LPSWQNVLTA GDPVVIFHQT DQLPQPIPGK PEPVLILLDR
QQTTWNDNSY FAVDADGKVE LGWFAEAPIA KILGQVLLVM RPKKILDENN LREPWQMDD
