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Entry version 79 (07 Apr 2021)
Sequence version 1 (06 Dec 2005)
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Protein

Ribulose bisphosphate carboxylase small subunit

Gene

cbbS

Organism
Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans R2)
Status
Reviewed-Annotation score:

Annotation score:4 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site.UniRule annotation2 Publications
Beta-carboxysome assembly initiates when soluble RuBisCO aggregates is condensed into a liquid matrix in a pre-carboxysome by the RbcS-like domains of probably both CcmM58 and CcmM35. CcmN interacts with the N-terminus of CcmM58, and then recruits the CcmK2 major shell protein via CcmN's encapsulation peptide. Shell formation requires CcmK proteins and CcmO. CcmL caps the otherwise elongated carboxysome. Once fully encapsulated carboxysomes are formed, they migrate within the cell probably via interactions with the cytoskeleton.2 Publications

Miscellaneous

RuBisCO folding and assembly commences when the nascent large subunit folds with the help of chaperonin GroEL-GroES. Both RbcX and Raf1 help folded RbcL release from the chaperonin and dimerize; dimeric Raf1 binds to RbcL2 leading to an RbcL8-Raf18 complex. RbcS displaces Raf1, resulting in holoenzyme formation.1 Publication1 Publication
The basic functional RuBisCO is composed of a large chain homodimer in a 'head-to-tail' conformation. In form I RuBisCO this homodimer is arranged in a barrel-like tetramer with the small subunits forming a tetrameric 'cap' on each end of the 'barrel'.UniRule annotation

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Biological processCalvin cycle, Carbon dioxide fixation, Photorespiration, Photosynthesis

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
SYNEL:SYNPCC7942_1427-MONOMER

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Ribulose bisphosphate carboxylase small subunitUniRule annotation
Short name:
RuBisCO small subunitUniRule annotation
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:cbbSUniRule annotation
Synonyms:rbcS1 PublicationUniRule annotation
Ordered Locus Names:Synpcc7942_1427
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiSynechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans R2)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri1140 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaCyanobacteriaSynechococcalesSynechococcaceaeSynechococcus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002717 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Carboxysome

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section describes the use of a specific protein in the biotechnological industry.<p><a href='/help/biotechnological_use' target='_top'>More...</a></p>Biotechnological usei

Heterologous expression of 12 carboxysomal genes in E.coli (ccaA, ccmK2, ccmK3, ccmK4, ccmL, ccmM, ccmN, ccmO, ccmP, rbcL, rbcS, rbcX) leads to the formation of bodies that resemble carboxysomes, have densely packed paracrystalline arrays and RuBisCO activity. These structures open the door to generating carboxysomes in plant cells to increase their photosynthesis and productivity, as well as tailoring bacterial microcompartments to specific metabolic needs and molecule delivery.1 Publication

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004512481 – 111Ribulose bisphosphate carboxylase small subunitAdd BLAST111

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
Q31NB2

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Carboxysome size and components vary with growth conditions. When grown in ambient air at medium light (50 uE meter(-2) second(-1)) there are 853 RuBisCO complexes (RbcL8S8) per carboxysome, the numbers decrease under low light and high CO2, and increase under high light (at protein level).1 Publication

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Heterohexadecamer of 8 large and 8 small subunits (Probable). The CcmM short form purifies from carboxysomes in complex with both RuBisCO subunits; a second complex with full-length CcmM and RuBisCO also includes carbonic anhydrase (CA, ccaA). RuBisCO-CcmM complexes are probably associated with the carboxysome shell (PubMed:17675289). Isolated reduced and oxidized SSUL1 binds holo-RuBisCO (RbcL8-RbcS8) but not either subunit octamer alone; RuBisCO has a higher affinity for reduced SSUL1 (PubMed:30675061).

2 Publications2 Publications

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
1140.Synpcc7942_1427

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1111
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
Q31NB2

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the RuBisCO small chain family.UniRule annotation

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4108VFZ, Bacteria
COG4451, LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_098114_2_0_3

Identification of Orthologs from Complete Genome Data

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OMAi
KQCQVLS

Family and domain databases

Conserved Domains Database

More...
CDDi
cd03527, RuBisCO_small, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.30.190.10, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_00859, RuBisCO_S_bact, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR000894, RuBisCO_sc_dom
IPR036385, RuBisCO_ssu_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00101, RuBisCO_small, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00961, RuBisCO_small, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF55239, SSF55239, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

Q31NB2-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSMKTLPKER RFETFSYLPP LSDRQIAAQI EYMIEQGFHP LIEFNEHSNP
60 70 80 90 100
EEFYWTMWKL PLFDCKSPQQ VLDEVRECRS EYGDCYIRVA GFDNIKQCQT
110
VSFIVHRPGR Y
Length:111
Mass (Da):13,333
Last modified:December 6, 2005 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iF854F73FA70BD57B
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
CP000100 Genomic DNA Translation: ABB57457.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
ABB57457; ABB57457; Synpcc7942_1427

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
syf:Synpcc7942_1427

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000100 Genomic DNA Translation: ABB57457.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
6HBCelectron microscopy2.78D/E1-111[»]
SMRiQ31NB2
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi1140.Synpcc7942_1427

Proteomic databases

PRIDEiQ31NB2

Genome annotation databases

EnsemblBacteriaiABB57457; ABB57457; Synpcc7942_1427
KEGGisyf:Synpcc7942_1427

Phylogenomic databases

eggNOGiENOG4108VFZ, Bacteria
COG4451, LUCA
HOGENOMiCLU_098114_2_0_3
OMAiKQCQVLS

Enzyme and pathway databases

BioCyciSYNEL:SYNPCC7942_1427-MONOMER

Family and domain databases

CDDicd03527, RuBisCO_small, 1 hit
Gene3Di3.30.190.10, 1 hit
HAMAPiMF_00859, RuBisCO_S_bact, 1 hit
InterProiView protein in InterPro
IPR000894, RuBisCO_sc_dom
IPR036385, RuBisCO_ssu_sf
PfamiView protein in Pfam
PF00101, RuBisCO_small, 1 hit
SMARTiView protein in SMART
SM00961, RuBisCO_small, 1 hit
SUPFAMiSSF55239, SSF55239, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiRBS_SYNE7
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q31NB2
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 7, 2020
Last sequence update: December 6, 2005
Last modified: April 7, 2021
This is version 79 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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