CCMM_THEVB
ID CCMM_THEVB Reviewed; 652 AA.
AC Q8DKB5;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Carboxysome assembly protein CcmM {ECO:0000305};
DE Short=CcmM70 {ECO:0000305|PubMed:30591587};
DE Short=M70;
DE AltName: Full=Carbon dioxide concentrating mechanism protein CcmM;
DE AltName: Full=Carbonic anhydrase {ECO:0000303|PubMed:20133749};
DE EC=4.2.1.1 {ECO:0000269|PubMed:20133749};
GN Name=ccmM {ECO:0000303|PubMed:20133749}; OrderedLocusNames=tll0944;
OS Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1).
OC Bacteria; Cyanobacteria; Pseudanabaenales; Thermosynechococcaceae;
OC Thermosynechococcus.
OX NCBI_TaxID=197221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C.,
RA Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takeuchi C., Yamada M., Tabata S.;
RT "Complete genome structure of the thermophilic cyanobacterium
RT Thermosynechococcus elongatus BP-1.";
RL DNA Res. 9:123-130(2002).
RN [2] {ECO:0007744|PDB:3KWC, ECO:0007744|PDB:3KWD, ECO:0007744|PDB:3KWE}
RP X-RAY CRYSTALLOGRAPHY (1.10 ANGSTROMS) OF 1-193 IN COMPLEX WITH ZINC, X-RAY
RP CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 1-209 IN COMPLEX WITH ZINC, FUNCTION AS
RP A CARBONIC ANHYDRASE, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION,
RP SUBCELLULAR LOCATION, DISULFIDE BONDS, AND MUTAGENESIS OF 174-ASP--ASN-197
RP AND CYS-200.
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=20133749; DOI=10.1073/pnas.0910866107;
RA Pena K.L., Castel S.E., de Araujo C., Espie G.S., Kimber M.S.;
RT "Structural basis of the oxidative activation of the carboxysomal gamma-
RT carbonic anhydrase, CcmM.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:2455-2460(2010).
RN [3] {ECO:0007744|PDB:6MR1}
RP X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 227-320, FUNCTION, SUBUNIT, AND
RP DOMAIN.
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=30591587; DOI=10.1074/jbc.ra118.006330;
RA Ryan P., Forrester T.J.B., Wroblewski C., Kenney T.M.G., Kitova E.N.,
RA Klassen J.S., Kimber M.S.;
RT "The small RbcS-like domains of the beta-carboxysome structural protein
RT CcmM bind RubisCO at a site distinct from that binding the RbcS subunit.";
RL J. Biol. Chem. 294:2593-2603(2019).
CC -!- FUNCTION: Functions as a scaffold protein for the assembly of beta-
CC carboxysomes, initiates carboxysome assembly by coalescing RuBisCO
CC (ribulose bisphosphate carboxylase, rbcL-rbcS) (Probable). Produced as
CC a full-length and a shorter form; both forms are required for correct
CC carboxysome assembly and growth (By similarity).
CC {ECO:0000250|UniProtKB:Q03513, ECO:0000305|PubMed:30591587}.
CC -!- FUNCTION: A carbonic anhydrase, catalyzes the reversible hydration of
CC carbon dioxide. Essential to photosynthetic carbon dioxide fixation,
CC supplies CO(2) to ribulose bisphosphate carboxylase (RuBisCO) in the
CC carboxysome. Active when the disulfide bond (194-200) is oxidized,
CC suggesting the interior of the carboxysome is oxidizing.
CC {ECO:0000269|PubMed:20133749}.
CC -!- FUNCTION: Beta-carboxysome assembly initiates when soluble RuBisCO is
CC condensed into a liquid matrix in a pre-carboxysome by the RbcS-like
CC domains of probably both forms of CcmM (Probable). CcmN interacts with
CC the N-terminus of full length CcmM, and then recruits the shell
CC proteins (CcmK) via CcmN's encapsulation peptide. Shell formation
CC requires both CcmK proteins and CcmO. CcmL caps the otherwise elongated
CC carboxysome. Once fully encapsulated carboxysomes are formed, they
CC migrate within the cell probably via interactions with the cytoskeleton
CC (By similarity). {ECO:0000250|UniProtKB:Q03513,
CC ECO:0000305|PubMed:30591587}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + hydrogencarbonate = CO2 + H2O; Xref=Rhea:RHEA:10748,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:17544; EC=4.2.1.1;
CC Evidence={ECO:0000269|PubMed:20133749};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:20133749, ECO:0007744|PDB:3KWC,
CC ECO:0007744|PDB:3KWD, ECO:0007744|PDB:3KWE};
CC Note=Binds 3 zinc per trimer. {ECO:0000269|PubMed:20133749};
CC -!- ACTIVITY REGULATION: Carbonic anhydrase (CA) activity is probably under
CC redox control to remain inactive in the cytoplasm. CA activity of full-
CC length protein inhibited by ethoxyzolamide, and for both full-length
CC and CcmM 1-209 construct by reducing agents.
CC {ECO:0000269|PubMed:20133749}.
CC -!- SUBUNIT: The N-terminal structure crystallizes as a homotrimer; zinc is
CC bound between adjacent monomers (PubMed:20133749). The C-terminal RbcS-
CC like domains bind to holo-RuBisCO (PubMed:30591587). Full length
CC protein interacts with CcmN (By similarity).
CC {ECO:0000250|UniProtKB:Q03513, ECO:0000269|PubMed:20133749,
CC ECO:0000269|PubMed:30591587}.
CC -!- SUBCELLULAR LOCATION: Carboxysome {ECO:0000269|PubMed:20133749}.
CC Note=This cyanobacterium makes beta-type carboxysomes.
CC {ECO:0000269|PubMed:20133749}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=CcmM70;
CC IsoId=Q8DKB5-1; Sequence=Displayed;
CC Name=CcmM47 {ECO:0000250|UniProtKB:Q03513};
CC IsoId=Q8DKB5-2; Sequence=VSP_060777;
CC -!- DOMAIN: The N-terminus (residues 1-164) forms a trimer with a partially
CC blocked channel forms at the trimer interface (PubMed:20133749). The C-
CC terminus has 4 domains that resemble the small subunit of RuBisCO
CC (rbcS) joined by flexible linkers; the first one (CcmMS1) has been
CC crystallized and folds much like RbcS. CcmMS1 binds to holo-RuBisCO
CC (RbcL(8)-RbcS(8)), a CcmMS1-CcmMS2 constructs binds about 10-fold
CC better, while the entire C-terminus with all 4 CcmMS domains binds with
CC an intermediate affinity. CcmMS1 binds to a different region of RbcL
CC than does RbcS, up to 5 CcmMS1 domains can bind to the intact holo
CC enzyme (PubMed:30591587). {ECO:0000269|PubMed:20133749,
CC ECO:0000269|PubMed:30591587}.
CC -!- SIMILARITY: Belongs to the gamma-class carbonic anhydrase family.
CC {ECO:0000305|PubMed:20133749}.
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DR EMBL; BA000039; BAC08496.1; -; Genomic_DNA.
DR RefSeq; NP_681734.1; NC_004113.1.
DR RefSeq; WP_011056788.1; NC_004113.1.
DR PDB; 3KWC; X-ray; 2.00 A; A/B/C/D/E/F=1-209.
DR PDB; 3KWD; X-ray; 1.10 A; A=1-193.
DR PDB; 3KWE; X-ray; 1.10 A; A=1-193.
DR PDB; 6MR1; X-ray; 1.35 A; A/B=227-320.
DR PDBsum; 3KWC; -.
DR PDBsum; 3KWD; -.
DR PDBsum; 3KWE; -.
DR PDBsum; 6MR1; -.
DR AlphaFoldDB; Q8DKB5; -.
DR SMR; Q8DKB5; -.
DR DIP; DIP-58532N; -.
DR IntAct; Q8DKB5; 1.
DR STRING; 197221.22294667; -.
DR EnsemblBacteria; BAC08496; BAC08496; BAC08496.
DR KEGG; tel:tll0944; -.
DR PATRIC; fig|197221.4.peg.991; -.
DR eggNOG; COG0663; Bacteria.
DR eggNOG; COG4451; Bacteria.
DR OMA; RFKTKSW; -.
DR OrthoDB; 448757at2; -.
DR EvolutionaryTrace; Q8DKB5; -.
DR Proteomes; UP000000440; Chromosome.
DR GO; GO:0031470; C:carboxysome; IDA:UniProtKB.
DR GO; GO:0004089; F:carbonate dehydratase activity; IDA:UniProtKB.
DR GO; GO:0043886; F:structural constituent of carboxysome; IPI:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-KW.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR Gene3D; 3.30.190.10; -; 4.
DR InterPro; IPR017156; CcmM.
DR InterPro; IPR001451; Hexapep.
DR InterPro; IPR000894; RuBisCO_ssu_dom.
DR InterPro; IPR036385; RuBisCO_ssu_sf.
DR InterPro; IPR011004; Trimer_LpxA-like_sf.
DR Pfam; PF00132; Hexapep; 1.
DR Pfam; PF00101; RuBisCO_small; 4.
DR PIRSF; PIRSF037250; CcmM; 1.
DR SMART; SM00961; RuBisCO_small; 4.
DR SUPFAM; SSF51161; SSF51161; 1.
DR SUPFAM; SSF55239; SSF55239; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative initiation; Bacterial microcompartment;
KW Carbon dioxide fixation; Carboxysome; Disulfide bond; Lyase; Metal-binding;
KW Photosynthesis; Reference proteome; Repeat; Zinc.
FT CHAIN 1..652
FT /note="Carboxysome assembly protein CcmM"
FT /id="PRO_0000451244"
FT REGION 1..209
FT /note="Has carbonic anhydrase (CA) activity"
FT /evidence="ECO:0000269|PubMed:20133749"
FT REGION 1..193
FT /note="Does not have CA activity"
FT /evidence="ECO:0000269|PubMed:20133749"
FT REGION 233..313
FT /note="RbcS-like repeat 1, CcmMS1"
FT /evidence="ECO:0000305|PubMed:30591587"
FT REGION 338..422
FT /note="RbcS-like repeat 2, CcmMS2"
FT /evidence="ECO:0000305|PubMed:30591587"
FT REGION 451..533
FT /note="RbcS-like repeat 3, CcmMS3"
FT /evidence="ECO:0000305|PubMed:30591587"
FT REGION 530..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 565..649
FT /note="RbcS-like repeat 4, CcmMS4"
FT /evidence="ECO:0000305|PubMed:30591587"
FT COMPBIAS 535..566
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 56
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P40881"
FT BINDING 75
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000269|PubMed:20133749,
FT ECO:0007744|PDB:3KWC, ECO:0007744|PDB:3KWD,
FT ECO:0007744|PDB:3KWE"
FT BINDING 102
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000269|PubMed:20133749,
FT ECO:0007744|PDB:3KWC, ECO:0007744|PDB:3KWD,
FT ECO:0007744|PDB:3KWE"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000269|PubMed:20133749,
FT ECO:0007744|PDB:3KWC, ECO:0007744|PDB:3KWD,
FT ECO:0007744|PDB:3KWE"
FT DISULFID 194..200
FT /evidence="ECO:0000269|PubMed:20133749,
FT ECO:0007744|PDB:3KWC"
FT VAR_SEQ 1..228
FT /note="Missing (in isoform CcmM47)"
FT /evidence="ECO:0000250|UniProtKB:Q03513"
FT /id="VSP_060777"
FT MUTAGEN 174..197
FT /note="DIHFAQHVVGINEALLSGYQCAEN->AYSHTNEAVVYVNVHLAEGYKETS:
FT About 50% activity (in the CcmM 1-209 construct), not
FT inhibited by reducing agents."
FT /evidence="ECO:0000269|PubMed:20133749"
FT MUTAGEN 200
FT /note="C->S: Loss of CA activity (in the CcmM 1-209
FT construct)."
FT /evidence="ECO:0000269|PubMed:20133749"
FT STRAND 32..40
FT /evidence="ECO:0007829|PDB:3KWD"
FT STRAND 51..57
FT /evidence="ECO:0007829|PDB:3KWD"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:3KWD"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:3KWD"
FT STRAND 89..94
FT /evidence="ECO:0007829|PDB:3KWD"
FT STRAND 105..112
FT /evidence="ECO:0007829|PDB:3KWD"
FT STRAND 123..129
FT /evidence="ECO:0007829|PDB:3KWD"
FT STRAND 140..143
FT /evidence="ECO:0007829|PDB:3KWD"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:3KWD"
FT HELIX 161..164
FT /evidence="ECO:0007829|PDB:3KWD"
FT HELIX 172..181
FT /evidence="ECO:0007829|PDB:3KWD"
FT HELIX 198..207
FT /evidence="ECO:0007829|PDB:3KWC"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:6MR1"
FT HELIX 234..243
FT /evidence="ECO:0007829|PDB:6MR1"
FT STRAND 246..252
FT /evidence="ECO:0007829|PDB:6MR1"
FT HELIX 254..258
FT /evidence="ECO:0007829|PDB:6MR1"
FT STRAND 263..268
FT /evidence="ECO:0007829|PDB:6MR1"
FT HELIX 273..286
FT /evidence="ECO:0007829|PDB:6MR1"
FT TURN 287..289
FT /evidence="ECO:0007829|PDB:6MR1"
FT STRAND 290..297
FT /evidence="ECO:0007829|PDB:6MR1"
FT TURN 299..301
FT /evidence="ECO:0007829|PDB:6MR1"
FT STRAND 304..313
FT /evidence="ECO:0007829|PDB:6MR1"
SQ SEQUENCE 652 AA; 71584 MW; 84157EFA0CB3110D CRC64;
MAVQSYAAPP TPWSRDLAEP EIAPTAYVHS FSNLIGDVRI KDYVHIAPGT SIRADEGTPF
HIGSRTNIQD GVVIHGLQQG RVIGDDGQEY SVWIGDNVSI THMALIHGPA YIGDGCFIGF
RSTVFNARVG AGCVVMMHVL IQDVEIPPGK YVPSGMVITT QQQADRLPNV EESDIHFAQH
VVGINEALLS GYQCAENIAC IAPIRNELQR QEDPPTLHVE MLTGEKNTMT TDYGTHVRQL
LQQGYQISLE YADARRYRTS SWQSGPTLTG QQESQVMAAI AQLLKEHEGE YVRLIGVDPK
AKRRVFEEII QRPGQAAVAS SSSSRPSATV NASPVGSLDA AVVAQVRQLL QQGYQIGTEH
ADARRYRTSS WTSCAPIQSK QEPEVLAALE ACLQEHAGEY VRLIGIDQKQ KRRVLEQIIQ
RPQGPVAIAP KTPTPVATSH ASVSSGGNDT LLSADLVNQI QDLLRQGCQV ITEYADQRRF
RTSSWQSGIK ITSAQQINDL RSFLAEHQRD YIRLVGVNPQ AKQRVLETII HRPNGKAASN
GNSTRGQGFT PRPTASSQGS PSTHSLSQEV IEQVRQLLQQ GYTLGLEHVD ARRYRTNSWQ
SGPRIEAKNL NEALAAIQAC LQEYSGEYVR LIGINPAGKQ RVAEILLQQA AK
