RBS_HALNC
ID RBS_HALNC Reviewed; 110 AA.
AC P45686; D0KZ91;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 25-MAY-2022, entry version 107.
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, ECO:0000303|PubMed:9696760};
GN Synonyms=rbcS; OrderedLocusNames=Hneap_0921;
OS Halothiobacillus neapolitanus (strain ATCC 23641 / c2) (Thiobacillus
OS neapolitanus).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC Halothiobacillaceae; Halothiobacillus.
OX NCBI_TaxID=555778;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC STRAIN=ATCC 23641 / c2;
RX PubMed=9696760; DOI=10.1128/jb.180.16.4133-4139.1998;
RA Baker S.H., Jin S., Aldrich H.C., Howard G.T., Shively J.M.;
RT "Insertion mutation of the form I cbbL gene encoding ribulose bisphosphate
RT carboxylase/oxygenase (RuBisCO) in Thiobacillus neapolitanus results in
RT expression of form II RuBisCO, loss of carboxysomes, and an increased CO2
RT requirement for growth.";
RL J. Bacteriol. 180:4133-4139(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23641 / c2;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Davenport K., Brettin T., Detter J.C., Han C.,
RA Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Kerfeld C., Cannon G., Heinhort S.;
RT "Complete sequence of Halothiobacillus neapolitanus c2.";
RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX DOI=10.1007/BF00429407;
RA Cannon G.C., Shively J.M.;
RT "Characterization of a Homogenous Preparation of Carboxysomes from
RT Thiobacillus neapolitanus.";
RL Arch. Microbiol. 134:52-59(1983).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=16535117; DOI=10.1128/aem.61.9.3256-3260.1995;
RA English R.S., Jin S., Shively J.M.;
RT "Use of Electroporation To Generate a Thiobacillus neapolitanus Carboxysome
RT Mutant.";
RL Appl. Environ. Microbiol. 61:3256-3260(1995).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=14729686; DOI=10.1128/jb.186.3.623-630.2004;
RA So A.K., Espie G.S., Williams E.B., Shively J.M., Heinhorst S.,
RA Cannon G.C.;
RT "A novel evolutionary lineage of carbonic anhydrase (epsilon class) is a
RT component of the carboxysome shell.";
RL J. Bacteriol. 186:623-630(2004).
RN [6]
RP PROTEIN ABUNDANCE, AND SUBCELLULAR LOCATION.
RX DOI=10.1007/7171_023;
RA Heinhorst S., Cannon G.C., Shively J.M.;
RT "Carboxysomes and Carboxysome-like Inclusions.";
RL (In) Shively J.M. (eds.);
RL Microbiology Monographs, pp.2:141-164, Springer-Verlag, Berlin (2006).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=ATCC 23641 / c2;
RX PubMed=18258595; DOI=10.1074/jbc.m709285200;
RA Dou Z., Heinhorst S., Williams E.B., Murin C.D., Shively J.M., Cannon G.C.;
RT "CO2 fixation kinetics of Halothiobacillus neapolitanus mutant carboxysomes
RT lacking carbonic anhydrase suggest the shell acts as a diffusional barrier
RT for CO2.";
RL J. Biol. Chem. 283:10377-10384(2008).
RN [8]
RP DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 23641 / c2;
RX PubMed=18974784; DOI=10.1371/journal.pone.0003570;
RA Menon B.B., Dou Z., Heinhorst S., Shively J.M., Cannon G.C.;
RT "Halothiobacillus neapolitanus carboxysomes sequester heterologous and
RT chimeric RubisCO species.";
RL PLoS ONE 3:e3570-e3570(2008).
RN [9]
RP BIOTECHNOLOGY.
RC STRAIN=ATCC 23641 / c2;
RX PubMed=22184212; DOI=10.1073/pnas.1108557109;
RA Bonacci W., Teng P.K., Afonso B., Niederholtmeyer H., Grob P., Silver P.A.,
RA Savage D.F.;
RT "Modularity of a carbon-fixing protein organelle.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:478-483(2012).
RN [10]
RP SUBUNIT.
RC STRAIN=ATCC 23641 / c2;
RX PubMed=25826651; DOI=10.3390/life5021141;
RA Cai F., Dou Z., Bernstein S.L., Leverenz R., Williams E.B., Heinhorst S.,
RA Shively J., Cannon G.C., Kerfeld C.A.;
RT "Advances in Understanding Carboxysome Assembly in Prochlorococcus and
RT Synechococcus Implicate CsoS2 as a Critical Component.";
RL Life 5:1141-1171(2015).
RN [11]
RP INTERACTION WITH CSOS2, AND BIOTECHNOLOGY.
RC STRAIN=ATCC 23641 / c2;
RX PubMed=30305640; DOI=10.1038/s41598-018-33074-x;
RA Liu Y., He X., Lim W., Mueller J., Lawrie J., Kramer L., Guo J., Niu W.;
RT "Deciphering molecular details in the assembly of alpha-type carboxysome.";
RL Sci. Rep. 8:15062-15062(2018).
RN [12]
RP DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 23641 / c2;
RX PubMed=31406332; DOI=10.1038/s41564-019-0520-8;
RA Desmarais J.J., Flamholz A.I., Blikstad C., Dugan E.J., Laughlin T.G.,
RA Oltrogge L.M., Chen A.W., Wetmore K., Diamond S., Wang J.Y., Savage D.F.;
RT "DABs are inorganic carbon pumps found throughout prokaryotic phyla.";
RL Nat. Microbiol. 4:2204-2215(2019).
RN [13] {ECO:0007744|PDB:1SVD}
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RA Kerfeld C.A., Sawaya M.R., Pashkov I., Cannon G., Williams E., Tran K.,
RA Yeates T.O.;
RT "The structure of Halothiobacillus neapolitanus Rubisco.";
RL Submitted (APR-2005) to the PDB data bank.
RN [14] {ECO:0007744|PDB:6UEW}
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF HOLOENZYME, INTERACTION WITH
RP CSOS2, AND MUTAGENESIS OF TYR-96.
RX PubMed=32123388; DOI=10.1038/s41594-020-0387-7;
RA Oltrogge L.M., Chaijarasphong T., Chen A.W., Bolin E.R., Marqusee S.,
RA Savage D.F.;
RT "Multivalent interactions between CsoS2 and Rubisco mediate alpha-
RT carboxysome formation.";
RL Nat. Struct. Mol. Biol. 27:281-287(2020).
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 (Ref.3, PubMed:18258595, PubMed:18974784). There
CC are estimated to be 270 RuBisCO heterohexadecamers per carboxysome
CC (Ref.6). {ECO:0000269|PubMed:18258595, ECO:0000269|PubMed:18974784,
CC ECO:0000269|Ref.3, ECO:0000269|Ref.6}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=163.7 uM for CO(2);
CC Vmax=2.9 umol/min/mg enzyme {ECO:0000269|PubMed:18258595};
CC Note=For enzyme freed from the carboxysome.
CC {ECO:0000269|PubMed:18258595};
CC -!- SUBUNIT: Heterohexadecamer of 8 large and 8 small subunits
CC (PubMed:32123388). Interacts with CsoS2 (PubMed:30305640). Forms a
CC CsoS2-CsoS1-RuBisCO complex (Probable). Holo-RuBisCO interacts with the
CC N-terminal repeats of CsoS2; binding is sensitive to ionic strength. A
CC fusion of a single N-terminal repeat to the C-terminus of the large
CC subunit of RuBisCO (cbbL) shows the repeat can lie between a CbbL
CC dimer, making minor contacts to CbbS; thus each RuBisCO holoenzyme
CC could bind 8 repeats (PubMed:32123388). {ECO:0000269|PubMed:30305640,
CC ECO:0000269|PubMed:32123388, ECO:0000305|PubMed:25826651}.
CC -!- SUBCELLULAR LOCATION: Carboxysome {ECO:0000269|PubMed:14729686,
CC ECO:0000269|PubMed:18258595, ECO:0000269|PubMed:18974784,
CC ECO:0000269|Ref.3, ECO:0000305|PubMed:16535117}. Note=When the major
CC carboxysomal shell protein CsoS1A is disrupted most RuBisCO is found in
CC the soluble (cytoplasmic) fraction (PubMed:16535117). Most protein is
CC found in the carboxysome interior and not associated with the shell
CC (PubMed:14729686). This cyanobacterium makes alpha-type carboxysomes
CC (Ref.6, PubMed:18258595). {ECO:0000269|PubMed:14729686,
CC ECO:0000269|PubMed:16535117, ECO:0000269|PubMed:18258595,
CC ECO:0000269|Ref.6}.
CC -!- INDUCTION: Produced when grown in air or in air supplemented with 5%
CC CO(2). Part of the ccbL-ccbS operon. {ECO:0000269|PubMed:9696760}.
CC -!- DISRUPTION PHENOTYPE: A double ccbL-ccbS deletion does not grow in air,
CC grows well with 5% CO(2), a high-CO(2) requiring phenotype (hcr) and
CC forms empty but otherwise normal appearing carboxysomes. Required for
CC growth in ambient air (PubMed:31406332). {ECO:0000269|PubMed:18974784,
CC ECO:0000269|PubMed:31406332}.
CC -!- BIOTECHNOLOGY: Expression of 10 genes for alpha-carboxysome (Cb)
CC proteins (cbbL-cbbS-csoS2-csoS3-csoS4A-csoS4B-csoS1C-csoS1A-csoS1B-
CC csoS1D) in E.coli generates compartments that resemble Cb, contain
CC RuBisCO and have its catalytic activity, showing it is possible to make
CC artificial, functional Cb using these 10 genes. Cargo proteins can be
CC targeted to these organelles (PubMed:22184212, PubMed:30305640). Alpha-
CC carboxysomes are assembled in the complete absence of this enzyme in
CC this bacteria, suggesting carboxysome-based microcompartments can be
CC designed for applications such as custom chemical reactors or delivery
CC vehicles (PubMed:18974784, PubMed:30305640).
CC {ECO:0000269|PubMed:18974784, ECO:0000269|PubMed:22184212,
CC ECO:0000269|PubMed:30305640}.
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:32123388}.
CC -!- SIMILARITY: Belongs to the RuBisCO small chain family.
CC {ECO:0000255|HAMAP-Rule:MF_00859}.
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DR EMBL; AF038430; AAC32550.1; -; Genomic_DNA.
DR EMBL; CP001801; ACX95764.1; -; Genomic_DNA.
DR RefSeq; WP_012823800.1; NC_013422.1.
DR PDB; 1SVD; X-ray; 1.80 A; M=1-110.
DR PDB; 6UEW; X-ray; 2.40 A; B/D/F/H=1-110.
DR PDBsum; 1SVD; -.
DR PDBsum; 6UEW; -.
DR AlphaFoldDB; P45686; -.
DR SMR; P45686; -.
DR STRING; 555778.Hneap_0921; -.
DR EnsemblBacteria; ACX95764; ACX95764; Hneap_0921.
DR KEGG; hna:Hneap_0921; -.
DR eggNOG; COG4451; Bacteria.
DR HOGENOM; CLU_098114_2_0_6; -.
DR OMA; WNPAIEH; -.
DR OrthoDB; 1708389at2; -.
DR BRENDA; 4.1.1.39; 6349.
DR EvolutionaryTrace; P45686; -.
DR Proteomes; UP000009102; Chromosome.
DR GO; GO:0031470; C:carboxysome; IEA:UniProtKB-SubCell.
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; Reference proteome.
FT CHAIN 1..110
FT /note="Ribulose bisphosphate carboxylase small subunit"
FT /id="PRO_0000198631"
FT MUTAGEN 96
FT /note="Y->A: No longer binds N-repeats in CsoS2A; when
FT associated with 'A-72' and 'A-346' in CbbL."
FT /evidence="ECO:0000269|PubMed:32123388"
FT TURN 15..18
FT /evidence="ECO:0007829|PDB:1SVD"
FT HELIX 24..36
FT /evidence="ECO:0007829|PDB:1SVD"
FT STRAND 40..46
FT /evidence="ECO:0007829|PDB:1SVD"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:1SVD"
FT STRAND 57..60
FT /evidence="ECO:0007829|PDB:1SVD"
FT HELIX 69..82
FT /evidence="ECO:0007829|PDB:1SVD"
FT STRAND 86..94
FT /evidence="ECO:0007829|PDB:1SVD"
FT TURN 95..98
FT /evidence="ECO:0007829|PDB:1SVD"
FT STRAND 99..107
FT /evidence="ECO:0007829|PDB:1SVD"
SQ SEQUENCE 110 AA; 12855 MW; 9C4F1AB8D29B104D CRC64;
MAEMQDYKQS LKYETFSYLP PMNAERIRAQ IKYAIAQGWS PGIEHVEVKN SMNQYWYMWK
LPFFGEQNVD NVLAEIEACR SAYPTHQVKL VAYDNYAQSL GLAFVVYRGN
