| IED ID | IndEnz0002014251 |
| Enzyme Type ID | protease014251 |
| Protein Name |
Carboxysome assembly protein CcmM CcmM73 M73 Carbon dioxide concentrating mechanism protein CcmM |
| Gene Name | ccmM sll1031 |
| Organism | Synechocystis sp. (strain PCC 6803 / Kazusa) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Cyanobacteria/Melainabacteria group Cyanobacteria Synechococcales Merismopediaceae Synechocystis unclassified Synechocystis Synechocystis sp. PCC 6803 Synechocystis sp. (strain PCC 6803 / Kazusa) |
| Enzyme Sequence | MLAKSLGWLLAVSRRNYCMGSRTALASRPWSKHLADPQIDPTAYVHSFANVVGDVRIQPGVSVAPGSSIRADEGTPFWIGGNVLIQHGVVIHGLETGRVLGDDDQEYSVWIGPGTCVAHLALVHGPVYLGANCFIGFRSTVLNARVGDGAVVMMHSLVQDVEIPPNKLVPSGAMITQQHQADSLPDVQAGDRHFVQQIAAMHGQSASPTQGTDPTVCVLPESLPAVTPVTETPYINSIDNMSINSDITNQIRSLLAQGYGIGAEHANERRFKTKSWQSCGTADGFRPDQVIATVEGWLQEFAGEYVRLIGIDQGAKRRVVEVIIQRPGDVPGSPSRGTTTTKALSSGGSGRSAVAHQTGNLAGDSANQLRALLHQGYKIGLEYASARRFKTGSWLTGGTIGSHREGEALQELNRFLADHTNEYVRIIGIDPAGKRRVAEIVVHRPNGNGNGKPSSSSSSVGYKSAPVSSAGGSSAGGLTPEVIATVRGLLANGHSIGTEHTDKRRFKAKSWDTCPTIDGGREAEVLAKLEACLADHAGEYVRIIGIDRVGKRRVLEQIIQRPGDNVVAGRSPSSSSASTSSSASSNGFGSGNGGGYSNSAVRLDNSVVTQVRSLLAQGYKIGTEHTDKRRFKAKSWQSCAPITSTHESEVLRALEGCLADHNGEYVRLLGIDPTAKRRVLETIIQRP |
| Enzyme Length | 687 |
| Uniprot Accession Number | P72758 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Functions as a scaffold protein for the assembly of beta-carboxysomes, initiates carboxysome assembly via its N-terminal domain binding to CcaA, CcmK and CcmL. Binds HCO(3)-, suggesting it may play a role in the activity or regulation of bicarbonate dehydration (PubMed:17993516). Also initiates carboxysome assembly by coalescing RuBisCO (ribulose bisphosphate carboxylase, rbcL-rbcS) via its SSU-like domains. Produced as a full-length and a shorter form; both forms are required for correct carboxysome assembly and growth (By similarity). Despite its strong similarity to gamma-class carbonic anhydrase (CA) it does not have detectable CA activity (Ref.2, PubMed:17993516). {ECO:0000250|UniProtKB:Q03513, ECO:0000269|PubMed:17993516, ECO:0000269|Ref.2}.; FUNCTION: Beta-carboxysome assembly initiates when soluble RuBisCO is condensed into a liquid matrix in a pre-carboxysome by the RbcS-like domains of probably both forms of CcmM. CcmN interacts with the N-terminus of full length CcmM, and then recruits the shell proteins (CcmK) via CcmN's encapsulation peptide. CcmM73 also interacts with CcmK proteins and CcmL directly. 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. {ECO:0000250|UniProtKB:Q03513, ECO:0000269|PubMed:17993516, ECO:0000269|PubMed:27729545}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Alternative sequence (1); Chain (1); Compositional bias (3); Mutagenesis (1); Region (7) |
| Keywords | Alternative initiation;Bacterial microcompartment;Carbon dioxide fixation;Carboxysome;Photosynthesis;Reference proteome;Repeat |
| Interact With | Q54735; P72757; P52231 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Carboxysome {ECO:0000269|PubMed:17993516}. Note=This cyanobacterium makes beta-type carboxysomes. Full length protein associates with the shell portion of carboxysomes, CcmM52 associates with both the soluble and shell portion of carboxysomes. {ECO:0000269|PubMed:17993516}. |
| Modified Residue | |
| Post Translational Modification | PTM: Multiple forms of the protein of 73 (full length), 62, 52 (the most predominant form) and 36 kDa are seen even in the presence of protease inhibitors. CcmM52 interacts with CcaA. {ECO:0000269|PubMed:17993516}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 14673118; 17922517; 18000013; |
| Motif | |
| Gene Encoded By | |
| Mass | 73,121 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 4.2.1.1; |