CCMM_NOSS1
ID CCMM_NOSS1 Reviewed; 555 AA.
AC Q8YYI3;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Carboxysome assembly protein CcmM {ECO:0000305};
DE Short=CcmM58 {ECO:0000303|PubMed:17675289};
DE Short=M58 {ECO:0000303|PubMed:17675289};
DE AltName: Full=Carbon dioxide concentrating mechanism protein CcmM;
DE AltName: Full=Carbonic anhydrase {ECO:0000303|PubMed:24907906};
DE EC=4.2.1.1 {ECO:0000269|PubMed:24907906};
GN Name=ccmM {ECO:0000303|PubMed:17675289}; OrderedLocusNames=all0865;
OS Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=103690;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT "Complete genomic sequence of the filamentous nitrogen-fixing
RT cyanobacterium Anabaena sp. strain PCC 7120.";
RL DNA Res. 8:205-213(2001).
RN [2]
RP PROTEIN SEQUENCE OF 227-233, 2 PROTEIN FORMS, AND ISOFORM CCMM35.
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=17675289; DOI=10.1074/jbc.m703896200;
RA Long B.M., Badger M.R., Whitney S.M., Price G.D.;
RT "Analysis of carboxysomes from Synechococcus PCC7942 reveals multiple
RT Rubisco complexes with carboxysomal proteins CcmM and CcaA.";
RL J. Biol. Chem. 282:29323-29335(2007).
RN [3]
RP FUNCTION AS A CARBONIC ANHYDRASE, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBCELLULAR LOCATION, DOMAIN, AND 2 PROTEIN FORMS.
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=24907906; DOI=10.1007/s11120-014-0018-4;
RA de Araujo C., Arefeen D., Tadesse Y., Long B.M., Price G.D., Rowlett R.S.,
RA Kimber M.S., Espie G.S.;
RT "Identification and characterization of a carboxysomal gamma-carbonic
RT anhydrase from the cyanobacterium Nostoc sp. PCC 7120.";
RL Photosyn. Res. 121:135-150(2014).
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) (By similarity).
CC Produced as a full-length (M58) and a short form (M35), possibly by
CC alternative translation initiation; probably both forms are required
CC for correct carboxysome assembly and growth. In this strain both forms
CC are equally abundant (PubMed:24907906). {ECO:0000250|UniProtKB:Q03513,
CC ECO:0000269|PubMed:24907906}.
CC -!- FUNCTION: A moderately active carbonic anhydrase that catalyzes the
CC reversible hydration of carbon dioxide. Essential to photosynthetic
CC carbon dioxide fixation, supplies CO(2) to ribulose bisphosphate
CC carboxylase (RuBisCO) in the carboxysome. Also hydrolyzes COS.
CC {ECO:0000269|PubMed:24907906}.
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. CcmN interacts with the N-
CC terminus of full length CcmM, and then recruits the shell proteins
CC (CcmK) via CcmN's encapsulation peptide. Shell formation requires both
CC CcmK proteins and CcmO. CcmL caps the otherwise elongated carboxysome.
CC Once fully encapsulated carboxysomes are formed, they migrate within
CC the cell probably via interactions with the cytoskeleton.
CC {ECO:0000250|UniProtKB:Q03513}.
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:24907906};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q8DKB5};
CC Note=Binds 3 zinc per trimer. {ECO:0000250|UniProtKB:Q8DKB5};
CC -!- ACTIVITY REGULATION: Carbonic anhydrase (CA) activity is probably under
CC redox control to remain inactive in the cytoplasm. Carbonic anhydrase
CC (CA) activity of full-length protein and N-terminal fragment is
CC inhibited by ethoxyzolamide. N-terminal fragment CA activity is
CC activated under oxidizing conditions and inhibited under reducing
CC conditions. {ECO:0000269|PubMed:24907906}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=10.2 mM for CO(2) at pH 7.5, 25 degrees Celsius, for N-terminal
CC 209 residue fragment {ECO:0000269|PubMed:24907906};
CC KM=5.2 mM for CO(2) at pH 8.0, 25 degrees Celsius, N-terminal 209
CC residue fragment {ECO:0000269|PubMed:24907906};
CC Note=kcat at pH 7.5 is 19000 sec(-1), at pH 8.0 is 22000 sec(-1).
CC {ECO:0000269|PubMed:24907906};
CC pH dependence:
CC Optimum pH is 8.0 - 9.5. {ECO:0000269|PubMed:24907906};
CC Temperature dependence:
CC Optimum temperature is 25-35 degrees Celsius for N-terminal 209
CC residue fragment. {ECO:0000269|PubMed:24907906};
CC -!- SUBUNIT: Probable homotrimer; zinc is bound between adjacent monomers
CC (By similarity). Full length protein (M58) interacts with CcmN. The C-
CC terminal RbcS-like domains (SSUL) bind to holo-RuBisCO, as does the M35
CC short form (By similarity). {ECO:0000250|UniProtKB:Q03513,
CC ECO:0000250|UniProtKB:Q8DKB5}.
CC -!- SUBCELLULAR LOCATION: Carboxysome {ECO:0000269|PubMed:24907906}.
CC Cytoplasm {ECO:0000305|PubMed:24907906}. Note=This cyanobacterium makes
CC beta-type carboxysomes. Both isoforms are found equally distributed in
CC the interior of the carboxysome. An unexpectedly large amount is found
CC outside the carboxysome by immungold labelling, this might represent
CC coalescing RuBisCO-CcmM. {ECO:0000269|PubMed:24907906}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=CcmM58;
CC IsoId=Q8YYI3-1; Sequence=Displayed;
CC Name=CcmM35 {ECO:0000269|PubMed:17675289};
CC IsoId=Q8YYI3-2; Sequence=VSP_060775, VSP_060776;
CC -!- DOMAIN: The N-terminus (residues 1-209) has carbonic anhydrase (CA)
CC activity (PubMed:24907906). The C-terminus has 3 repeats that are
CC similar to the small subunit of RuBisCO (rbcS), called SSUL. The SSUL
CC are connected by flexible linkers. The N-terminal domain probably forms
CC a scaffold on which CcmN and maybe other carboxysomal proteins
CC assemble, while the C-terminus binds and coalesces RuBisCO (By
CC similarity). {ECO:0000250|UniProtKB:Q03513,
CC ECO:0000269|PubMed:24907906}.
CC -!- PTM: The first amino acid of the short form (equivalent to Val-226) is
CC not seen in Edman degradation, while Ser-230 may be post-
CC translationally modified (PubMed:17675289). Migrates in gels as 2 about
CC equal forms of about 60 and 35 kDa (called M58 and M35)
CC (PubMed:24907906). They are probably the result of alternative
CC translation initiation (Probable). {ECO:0000269|PubMed:17675289,
CC ECO:0000269|PubMed:24907906, ECO:0000305|PubMed:24907906}.
CC -!- SIMILARITY: Belongs to the gamma-class carbonic anhydrase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BA000019; BAB72822.1; -; Genomic_DNA.
DR PIR; AG1914; AG1914.
DR RefSeq; WP_010995039.1; NZ_RSCN01000006.1.
DR AlphaFoldDB; Q8YYI3; -.
DR SMR; Q8YYI3; -.
DR STRING; 103690.17130210; -.
DR EnsemblBacteria; BAB72822; BAB72822; BAB72822.
DR KEGG; ana:all0865; -.
DR eggNOG; COG0663; Bacteria.
DR eggNOG; COG4451; Bacteria.
DR OMA; RFKTKSW; -.
DR OrthoDB; 448757at2; -.
DR Proteomes; UP000002483; Chromosome.
DR GO; GO:0031470; C:carboxysome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004089; F:carbonate dehydratase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043886; F:structural constituent of carboxysome; 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; -; 3.
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; 3.
DR PIRSF; PIRSF037250; CcmM; 1.
DR SMART; SM00961; RuBisCO_small; 3.
DR SUPFAM; SSF51161; SSF51161; 1.
DR SUPFAM; SSF55239; SSF55239; 3.
PE 1: Evidence at protein level;
KW Alternative initiation; Bacterial microcompartment;
KW Carbon dioxide fixation; Carboxysome; Cytoplasm; Direct protein sequencing;
KW Disulfide bond; Lyase; Metal-binding; Photosynthesis; Reference proteome;
KW Repeat; Zinc.
FT CHAIN 1..555
FT /note="Carboxysome assembly protein CcmM"
FT /id="PRO_0000451243"
FT REGION 1..209
FT /note="Has carbonic anhydrase (CA) activity"
FT /evidence="ECO:0000269|PubMed:24907906"
FT REGION 223..315
FT /note="RbcS-like repeat 1, SSUL1"
FT /evidence="ECO:0000305"
FT REGION 323..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 347..440
FT /note="RbcS-like repeat 2, SSUL2"
FT /evidence="ECO:0000305"
FT REGION 441..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 460..555
FT /note="RbcS-like repeat 3, SSUL3"
FT /evidence="ECO:0000305"
FT COMPBIAS 324..351
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:0000250|UniProtKB:Q8DKB5"
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:0000250|UniProtKB:Q8DKB5"
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:0000250|UniProtKB:Q8DKB5"
FT DISULFID 194..200
FT /evidence="ECO:0000250|UniProtKB:Q8DKB5,
FT ECO:0000305|PubMed:24907906"
FT VAR_SEQ 1..225
FT /note="Missing (in isoform CcmM35)"
FT /evidence="ECO:0000269|PubMed:17675289"
FT /id="VSP_060775"
FT VAR_SEQ 226
FT /note="V -> M (in isoform CcmM35)"
FT /evidence="ECO:0000305|PubMed:17675289"
FT /id="VSP_060776"
SQ SEQUENCE 555 AA; 59465 MW; 2339CC0D90BCE319 CRC64;
MAVRSTAAPP TPWSRSLAEA QIHESAFVHP FSNIIGDVHI GANVIIAPGT SIRADEGTPF
HIGENTNIQD GVVIHGLEQG RVVGDDNKEY SVWVGSSASL THMALIHGPA YVGDNSFIGF
RSTVFNAKVG AGCIVMMHAL IKDVEVPPGK YVPSGAIITN QKQADRLPDV QPQDRDFAHH
VIGINQALRA GYLCAADSKC IAPLRNDQVK SYTSTTVIGL ERSSEVASNS LGAETIEQVR
YLLEQGYKIG SEHVDQRRFR TGSWTSCQPI EARSVGDALA ALEACLADHS GEYVRLFGID
PKGKRRVLET IIQRPDGVVA GSTSFKAPAS NTNGNGSYHS NGNGNGYSNG ATSGKVSAET
VDQIRQLLAG GYKIGTEHVD ERRFRTGSWN SCKPIEATSA GEVVAALEEC IDSHQGEYIR
LIGIDPKAKR RVLESIIQRP NGQVAPSSSP RTVVSASSAS SGTATATATR LSTEVVDQVR
QILGGGYKLS IEHVDQRRFR TGSWSSTGAI SATSEREAIA VIEASLSEFA GEYVRLIGID
PKAKRRVLET IIQRP
