CCMM_SYNP2
ID CCMM_SYNP2 Reviewed; 661 AA.
AC O30711;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 120.
DE RecName: Full=Carboxysome assembly protein CcmM {ECO:0000305};
DE Short=CcmM70 {ECO:0000305};
DE Short=M70 {ECO:0000305};
DE AltName: Full=Carbon dioxide concentrating mechanism protein CcmM {ECO:0000303|Ref.1};
GN Name=ccmM {ECO:0000303|Ref.1}; OrderedLocusNames=SYNPCC7002_A1800;
OS Synechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6) (Agmenellum
OS quadruplicatum).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=32049;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], DOMAIN, DISRUPTION PHENOTYPE, AND 2
RP FORMS OF THE PROTEIN.
RC STRAIN=ATCC 27264 / PCC 7002 / PR-6;
RX DOI=10.1046/j.1529-8817.2000.00028.x;
RA Ludwig M., Sultemeyer D., Price G.D.;
RT "Isolation of ccmKLMN genes from the marine cyanobacterium, Synechococcus
RT sp. PCC7002 (Cyanophyceae), and evidence that CcmM is essential for
RT carboxysome assembly.";
RL J. Phycol. 36:1109-1118(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27264 / PCC 7002 / PR-6;
RA Li T., Zhao J., Zhao C., Liu Z., Zhao F., Marquardt J., Nomura C.T.,
RA Persson S., Detter J.C., Richardson P.M., Lanz C., Schuster S.C., Wang J.,
RA Li S., Huang X., Cai T., Yu Z., Luo J., Zhao J., Bryant D.A.;
RT "Complete sequence of Synechococcus sp. PCC 7002.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP DISCUSSION OF SEQUENCE, AND ISOFORM CCMM46.
RC STRAIN=PCC 6803 / Kazusa;
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).
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). Produced as a full-
CC length and a shorter form; both forms are required for correct
CC carboxysome assembly and growth. {ECO:0000250|UniProtKB:Q03513}.
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 -!- SUBUNIT: Probable homotrimer (By similarity). Full length protein (M70)
CC interacts with CcmN. The C-terminal RbcS-like domains (SSUL) bind to
CC holo-RuBisCO, as does the M46 short form (By similarity).
CC {ECO:0000250|UniProtKB:Q03513, ECO:0000250|UniProtKB:Q8DKB5}.
CC -!- SUBCELLULAR LOCATION: Carboxysome {ECO:0000250|UniProtKB:Q03513}.
CC Note=This cyanobacterium makes beta-type carboxysomes. {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=CcmM70;
CC IsoId=O30711-1; Sequence=Displayed;
CC Name=CcmM46 {ECO:0000305|PubMed:17675289, ECO:0000305|Ref.1};
CC IsoId=O30711-2; Sequence=VSP_060773;
CC -!- DOMAIN: The N-terminus has a gamma-class carbonic anhydrase-like domain
CC (CA), while the C-terminus has 4 repeats that are similar to the small
CC subunit of RuBisCO (rbcS), called SSUL (Probable). The SSUL are
CC connected by flexible linkers. The N-terminal domain forms a scaffold
CC on which CA and other carboxysomal proteins assemble, while the C-
CC terminus binds RuBisCO (By similarity). {ECO:0000250|UniProtKB:Q03513,
CC ECO:0000305|Ref.1}.
CC -!- PTM: Identified as 2 proteins of 70 and 46 kDa in gels. They are
CC probably the result of alternative translation initiation.
CC {ECO:0000305|PubMed:17675289, ECO:0000305|Ref.1}.
CC -!- DISRUPTION PHENOTYPE: Single gene deletion does not form carboxysomes,
CC and does not grow in normal air but in 2% CO(2), called a high-CO(2)
CC requiring phenotype, HCR. {ECO:0000269|Ref.1}.
CC -!- SIMILARITY: Belongs to the gamma-class carbonic anhydrase family.
CC {ECO:0000305}.
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DR EMBL; AF015889; AAB66837.1; -; Genomic_DNA.
DR EMBL; CP000951; ACA99788.1; -; Genomic_DNA.
DR RefSeq; WP_012307411.1; NC_010475.1.
DR AlphaFoldDB; O30711; -.
DR SMR; O30711; -.
DR STRING; 32049.SYNPCC7002_A1800; -.
DR EnsemblBacteria; ACA99788; ACA99788; SYNPCC7002_A1800.
DR KEGG; syp:SYNPCC7002_A1800; -.
DR eggNOG; COG0663; Bacteria.
DR eggNOG; COG4451; Bacteria.
DR HOGENOM; CLU_019008_0_0_3; -.
DR OMA; RFKTKSW; -.
DR Proteomes; UP000001688; Chromosome.
DR GO; GO:0031470; C:carboxysome; IEA:UniProtKB-SubCell.
DR GO; GO:0043886; F:structural constituent of carboxysome; IEA:InterPro.
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 3: Inferred from homology;
KW Alternative initiation; Bacterial microcompartment;
KW Carbon dioxide fixation; Carboxysome; Photosynthesis; Reference proteome;
KW Repeat.
FT CHAIN 1..661
FT /note="Carboxysome assembly protein CcmM"
FT /id="PRO_0000451241"
FT REGION 192..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 221..341
FT /note="RbcS-like repeat 1, SSUL1"
FT /evidence="ECO:0000305|Ref.1"
FT REGION 312..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 350..431
FT /note="RbcS-like repeat 2, SSUL2"
FT /evidence="ECO:0000305|Ref.1"
FT REGION 456..541
FT /note="RbcS-like repeat 3, SSUL3"
FT /evidence="ECO:0000305|Ref.1"
FT REGION 545..575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 578..661
FT /note="RbcS-like repeat 4, SSUL4"
FT /evidence="ECO:0000305|Ref.1"
FT COMPBIAS 316..345
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..227
FT /note="Missing (in isoform CcmM46)"
FT /id="VSP_060773"
SQ SEQUENCE 661 AA; 70069 MW; 5AD9D8C3BE5D0D70 CRC64;
MVVRSTAAPP TPWSKDLAEP KIHESAYVHS FSNLIGDVTV CEHVLISPGT SIRADEGAPF
HIGAATNIQD GVVIHGLEQG RVVGADGHDY SVWIGDRSCI THMALVHGPA YIGNDCFVGF
RSTVFNARIG DGCVIMMHAL VQDVDIPPGK YVPSGAVITN QQQVERLSNV TEADRAFAKQ
VVEINEALRE VSPGATNNGS RIAANQQPTP SSSTNTSGTS EHQSVGNMSL NGDLYNQVRG
LAAQGCTFTA EYANKRRFKT KSWLSAGFVE GHSADQIIGN LNRVLADHAG EYVQLIAVAP
NSKSRAAEIV VQRPGDSAPV QTSTTASYSN NGNRSNGTSA GSQAAAVGGD LTSQIHALAS
QGCSFTAEHA NTRRFKTQSW LSAGFVEGHS AEQIITNVNG LLGQYPNEYV QVIAVDPHSK
FRVAELIVQR PGETGTLSTK ATASARRSGN KVVNTASGGD VAGQIAALAS QGCSFTAEHA
STRRFKTQSW LGAGFVEGHS ANQILANIQA IAAQFPNEYV QLIAVDPNSK TRAAEIIIQR
PGNNAPVQTA TATSSFSGGT KAAPSSNGFG GHSSGSLSGD VVSKVRSLLM QGYKIGTEHA
DKRRFRVKSW SSCGTIDSTQ EAEVLRHLEG CLQEHSGEYV RMIGVDEAAK RRVLEEIIQR
P
