RBS_SYNP6
ID RBS_SYNP6 Reviewed; 111 AA.
AC P04716;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 144.
DE RecName: Full=Ribulose bisphosphate carboxylase small subunit {ECO:0000255|HAMAP-Rule:MF_00859};
DE Short=RuBisCO small subunit {ECO:0000255|HAMAP-Rule:MF_00859};
GN Name=cbbS {ECO:0000255|HAMAP-Rule:MF_00859};
GN Synonyms=rbcS {ECO:0000255|HAMAP-Rule:MF_00859};
GN OrderedLocusNames=syc0129_c;
OS Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) (Anacystis
OS nidulans).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=269084;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6415615; DOI=10.1093/nar/11.20.6957;
RA Shinozaki K., Sugiura M.;
RT "The gene for the small subunit of ribulose-1,5-bisphosphate
RT carboxylase/oxygenase is located close to the gene for the large subunit in
RT the cyanobacterium Anacystis nidulans 6301.";
RL Nucleic Acids Res. 11:6957-6963(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Shinozaki K., Sugiura M.;
RT "Genes for the large and small subunits of ribulose-1,5-bisphosphate
RT carboxylase/oxygenase constitute a single operon in a cyanobacterium
RT Anacystis nidulans 6301.";
RL Mol. Gen. Genet. 200:27-32(1985).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27144 / PCC 6301 / SAUG 1402/1;
RX PubMed=17211581; DOI=10.1007/s11120-006-9122-4;
RA Sugita C., Ogata K., Shikata M., Jikuya H., Takano J., Furumichi M.,
RA Kanehisa M., Omata T., Sugiura M., Sugita M.;
RT "Complete nucleotide sequence of the freshwater unicellular cyanobacterium
RT Synechococcus elongatus PCC 6301 chromosome: gene content and
RT organization.";
RL Photosyn. Res. 93:55-67(2007).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=9882445; DOI=10.1006/abbi.1998.0979;
RA Horken K.M., Tabita F.R.;
RT "Closely related form I ribulose bisphosphate carboxylase/oxygenase
RT molecules that possess different CO2/O2 substrate specificities.";
RL Arch. Biochem. Biophys. 361:183-194(1999).
RN [5]
RP SUBUNIT.
RC STRAIN=ATCC 27144 / PCC 6301 / SAUG 1402/1;
RX PubMed=17574029; DOI=10.1016/j.cell.2007.04.025;
RA Saschenbrecker S., Bracher A., Rao K.V., Rao B.V., Hartl F.U.,
RA Hayer-Hartl M.;
RT "Structure and function of RbcX, an assembly chaperone for hexadecameric
RT Rubisco.";
RL Cell 129:1189-1200(2007).
RN [6]
RP FUNCTION, FOLDING AND ASSEMBLY, AND SUBUNIT.
RC STRAIN=ATCC 27144 / PCC 6301 / SAUG 1402/1;
RX PubMed=21765418; DOI=10.1038/nsmb.2090;
RA Bracher A., Starling-Windhof A., Hartl F.U., Hayer-Hartl M.;
RT "Crystal structure of a chaperone-bound assembly intermediate of form I
RT Rubisco.";
RL Nat. Struct. Mol. Biol. 18:875-880(2011).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 2-110 OF ACTIVATED HOLOENZYME IN
RP COMPLEX WITH TRANSITION-STATE ANALOG 2-CABP, AND SUBUNIT.
RX PubMed=8245022; DOI=10.1016/s0021-9258(19)74469-x;
RA Newman J., Gutteridge S.;
RT "The X-ray structure of Synechococcus ribulose-bisphosphate
RT carboxylase/oxygenase-activated quaternary complex at 2.2-A resolution.";
RL J. Biol. Chem. 268:25876-25886(1993).
RN [8] {ECO:0007744|PDB:1RSC}
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF INACTIVATED HOLOENZYME IN COMPLEX
RP WITH PRODUCT ANALOG, FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RX PubMed=7922027; DOI=10.1016/s0969-2126(00)00050-2;
RA Newman J., Gutteridge S.;
RT "Structure of an effector-induced inactivated state of ribulose 1,5-
RT bisphosphate carboxylase/oxygenase: the binary complex between enzyme and
RT xylulose 1,5-bisphosphate.";
RL Structure 2:495-502(1994).
CC -!- FUNCTION: RuBisCO catalyzes two reactions: the carboxylation of D-
CC ribulose 1,5-bisphosphate, the primary event in carbon dioxide
CC fixation, as well as the oxidative fragmentation of the pentose
CC substrate. Both reactions occur simultaneously and in competition at
CC the same active site (PubMed:7922027, PubMed:9882445). The small
CC subunit displaces RbcX2 from the RbcL8-(RbcX2)8 assembly intermediate,
CC and stabilizes an RbcL loop ('Thr-64-Leu-70') in a catalytically
CC competent conformation (PubMed:21765418). {ECO:0000269|PubMed:21765418,
CC ECO:0000269|PubMed:7922027, ECO:0000269|PubMed:9882445}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=39 uM for ribulose 1,5-bisphosphate {ECO:0000269|PubMed:9882445};
CC KM=173 uM for CO(2) {ECO:0000269|PubMed:9882445};
CC Vmax=2.5 umol/min/mg enzyme with CO(2) as substrate
CC {ECO:0000269|PubMed:9882445};
CC Note=The CO(2)/O(2) specificity factor (tau) is 39.
CC {ECO:0000269|PubMed:9882445};
CC -!- SUBUNIT: Heterohexadecamer of 8 large and 8 small subunits
CC (PubMed:17574029, PubMed:21765418, PubMed:8245022, PubMed:7922027).
CC Displaces RbcX2 from the RbcL8-(RbcX2)8 assembly intermediate
CC (Probable) (PubMed:21765418). {ECO:0000269|PubMed:17574029,
CC ECO:0000269|PubMed:21765418, ECO:0000269|PubMed:7922027,
CC ECO:0000269|PubMed:8245022}.
CC -!- SUBCELLULAR LOCATION: Carboxysome {ECO:0000255|HAMAP-Rule:MF_00859}.
CC Note=In the carboxysome RuBisCO is organized into a paracrystalline
CC array (By similarity). This cyanobacterium makes beta-type carboxysomes
CC (Probable). {ECO:0000250|UniProtKB:Q31NB2, ECO:0000305}.
CC -!- MISCELLANEOUS: The basic functional RuBisCO is composed of a large
CC chain homodimer in a 'head-to-tail' conformation. In form I RuBisCO
CC this homodimer is arranged in a barrel-like tetramer with the small
CC subunits forming a tetrameric 'cap' on each end of the 'barrel'.
CC {ECO:0000255|HAMAP-Rule:MF_00859, ECO:0000269|PubMed:17574029,
CC ECO:0000269|PubMed:7922027, ECO:0000269|PubMed:8245022}.
CC -!- SIMILARITY: Belongs to the RuBisCO small chain family.
CC {ECO:0000255|HAMAP-Rule:MF_00859}.
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DR EMBL; X03220; CAA26973.1; -; Genomic_DNA.
DR EMBL; AP008231; BAD78319.1; -; Genomic_DNA.
DR PIR; S07351; RKYCS.
DR PDB; 1RBL; X-ray; 2.20 A; I/J/K/L/M/N/O/P=2-110.
DR PDB; 1RSC; X-ray; 2.30 A; I/J/K/L/M/N/O/P=1-111.
DR PDB; 1UZH; X-ray; 2.20 A; C/F/I/J/M/P/T/W=12-58, C/F/I/J/M/P/T/W=102-110.
DR PDBsum; 1RBL; -.
DR PDBsum; 1RSC; -.
DR PDBsum; 1UZH; -.
DR AlphaFoldDB; P04716; -.
DR SMR; P04716; -.
DR DIP; DIP-6211N; -.
DR STRING; 269084.syc0129_c; -.
DR EnsemblBacteria; BAD78319; BAD78319; syc0129_c.
DR KEGG; syc:syc0129_c; -.
DR eggNOG; COG4451; Bacteria.
DR OMA; KQCQVLS; -.
DR SABIO-RK; P04716; -.
DR EvolutionaryTrace; P04716; -.
DR Proteomes; UP000001175; Chromosome.
DR GO; GO:0031470; C:carboxysome; IEA:UniProtKB-SubCell.
DR GO; GO:0009853; P:photorespiration; IEA:UniProtKB-KW.
DR GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-KW.
DR CDD; cd03527; RuBisCO_small; 1.
DR Gene3D; 3.30.190.10; -; 1.
DR HAMAP; MF_00859; RuBisCO_S_bact; 1.
DR InterPro; IPR024681; RuBisCO_ssu.
DR InterPro; IPR000894; RuBisCO_ssu_dom.
DR InterPro; IPR036385; RuBisCO_ssu_sf.
DR PANTHER; PTHR31262; PTHR31262; 1.
DR Pfam; PF00101; RuBisCO_small; 1.
DR SMART; SM00961; RuBisCO_small; 1.
DR SUPFAM; SSF55239; SSF55239; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Bacterial microcompartment; Calvin cycle;
KW Carbon dioxide fixation; Carboxysome; Photorespiration; Photosynthesis.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..111
FT /note="Ribulose bisphosphate carboxylase small subunit"
FT /id="PRO_0000198624"
FT REGION 12..21
FT /note="Hydrophobic"
FT TURN 14..17
FT /evidence="ECO:0007829|PDB:1RBL"
FT HELIX 23..36
FT /evidence="ECO:0007829|PDB:1RBL"
FT STRAND 39..46
FT /evidence="ECO:0007829|PDB:1RBL"
FT STRAND 56..60
FT /evidence="ECO:0007829|PDB:1UZH"
FT HELIX 68..81
FT /evidence="ECO:0007829|PDB:1RBL"
FT STRAND 85..93
FT /evidence="ECO:0007829|PDB:1RBL"
FT TURN 94..97
FT /evidence="ECO:0007829|PDB:1RBL"
FT STRAND 98..106
FT /evidence="ECO:0007829|PDB:1RBL"
SQ SEQUENCE 111 AA; 13333 MW; F854F73FA70BD57B CRC64;
MSMKTLPKER RFETFSYLPP LSDRQIAAQI EYMIEQGFHP LIEFNEHSNP EEFYWTMWKL
PLFDCKSPQQ VLDEVRECRS EYGDCYIRVA GFDNIKQCQT VSFIVHRPGR Y
