CCMN_SYNE7
ID CCMN_SYNE7 Reviewed; 161 AA.
AC P46204; Q31NB5;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Carboxysome assembly protein CcmN {ECO:0000305};
DE AltName: Full=Carbon dioxide concentrating mechanism protein CcmN;
DE AltName: Full=ORF I {ECO:0000303|PubMed:2509426};
GN Name=ccmN {ECO:0000303|PubMed:22461622}; OrderedLocusNames=Synpcc7942_1424;
OS Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS R2).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=1140;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE, AND
RP VARIANT HCRO221 ASP-146.
RC STRAIN=PCC 7942 / FACHB-805;
RX PubMed=2509426; DOI=10.1128/jb.171.11.6069-6076.1989;
RA Friedberg D., Kaplan A., Ariel R., Kessel M., Seijffers J.;
RT "The 5'-flanking region of the gene encoding the large subunit of ribulose-
RT 1,5-bisphosphate carboxylase/oxygenase is crucial for growth of the
RT cyanobacterium Synechococcus sp. strain PCC 7942 at the level of CO2 in
RT air.";
RL J. Bacteriol. 171:6069-6076(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7942 / FACHB-805;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP INTERACTION WITH CCMM AND CCMK2, SUBCELLULAR LOCATION, DOMAIN, DISRUPTION
RP PHENOTYPE, AND MUTAGENESIS OF 123-VAL--ARG-161 AND 143-LYS--ARG-161.
RC STRAIN=PCC 7942 / FACHB-805;
RX PubMed=22461622; DOI=10.1074/jbc.m112.355305;
RA Kinney J.N., Salmeen A., Cai F., Kerfeld C.A.;
RT "Elucidating essential role of conserved carboxysomal protein CcmN reveals
RT common feature of bacterial microcompartment assembly.";
RL J. Biol. Chem. 287:17729-17736(2012).
RN [4]
RP CARBOXYSOME ASSEMBLY PROCESS, FUNCTION, SUBCELLULAR LOCATION, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=PCC 7942 / FACHB-805;
RX PubMed=24267892; DOI=10.1016/j.cell.2013.10.044;
RA Cameron J.C., Wilson S.C., Bernstein S.L., Kerfeld C.A.;
RT "Biogenesis of a bacterial organelle: the carboxysome assembly pathway.";
RL Cell 155:1131-1140(2013).
RN [5]
RP BIOTECHNOLOGY.
RC STRAIN=PCC 7942 / FACHB-805;
RX PubMed=29922315; DOI=10.3389/fpls.2018.00739;
RA Fang Y., Huang F., Faulkner M., Jiang Q., Dykes G.F., Yang M., Liu L.N.;
RT "Engineering and Modulating Functional Cyanobacterial CO2-Fixing
RT Organelles.";
RL Front. Plant Sci. 9:739-739(2018).
RN [6]
RP SUBCELLULAR LOCATION, AND INDUCTION.
RC STRAIN=PCC 7942 / FACHB-805;
RX PubMed=31048338; DOI=10.1105/tpc.18.00787;
RA Sun Y., Wollman A.J.M., Huang F., Leake M.C., Liu L.N.;
RT "Single-Organelle Quantification Reveals Stoichiometric and Structural
RT Variability of Carboxysomes Dependent on the Environment.";
RL Plant Cell 31:1648-1664(2019).
CC -!- FUNCTION: Required for carboxysome formation; the N-terminus interacts
CC with CcmM which itself binds RuBisCO (ribulose bisphosphate
CC carboxylase, rbcL-rbcS), while the C-terminal 18 residues interact with
CC carboxysome shell protein CcmK2 (PubMed:22461622). Required for growth
CC in normal air (PubMed:2509426). {ECO:0000269|PubMed:22461622,
CC ECO:0000269|PubMed:2509426}.
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 CcmM58 and CcmM35. CcmN interacts with the N-
CC terminus of CcmM58, and then recruits the CcmK2 major shell protein via
CC CcmN's encapsulation peptide. Shell formation requires CcmK proteins
CC and CcmO. CcmL caps the otherwise elongated carboxysome. Once fully
CC encapsulated carboxysomes are formed, they migrate within the cell
CC probably via interactions with the cytoskeleton.
CC {ECO:0000269|PubMed:24267892}.
CC -!- SUBUNIT: Interacts with CcmM via the N-terminus of CcmN. Interacts with
CC CcmK2 via the 18 C-terminal residues. {ECO:0000269|PubMed:22461622}.
CC -!- SUBCELLULAR LOCATION: Carboxysome {ECO:0000269|PubMed:22461622,
CC ECO:0000269|PubMed:31048338, ECO:0000305|PubMed:24267892}. Note=This
CC cyanobacterium makes beta-type carboxysomes.
CC {ECO:0000269|PubMed:22461622}.
CC -!- INDUCTION: Carboxysome size and components vary with growth conditions.
CC When grown in ambient air at medium light (50 uE meter(-2) second(-1))
CC there are 74 units of this protein per carboxysome, the numbers
CC decrease under low light and high CO(2), and increase under high light
CC (at protein level). {ECO:0000269|PubMed:31048338}.
CC -!- DOMAIN: The N-terminus interacts with CcmM, while the 18 C-terminal
CC residues (encapsulation peptide) are required for interaction with the
CC hexameric shell proteins (CcmK2) and are predicted to form a helix. The
CC 2 regions are separated by a linker. {ECO:0000269|PubMed:22461622}.
CC -!- DISRUPTION PHENOTYPE: Cells with a disrupted or mutated protein do not
CC have carboxysomes, instead have less dense inclusions, do not grow in
CC normal air (PubMed:2509426). Targeted disruption do not grow normally
CC in air but have wild-type growth in 3% CO(2), called a high-CO(2)
CC requiring phenotype, HCR. Cells have a single polar aggregate instead
CC of carboxysomes; RuBisCO localizes to polar spots consistent with the
CC polar aggregates (PubMed:22461622, PubMed:24267892).
CC {ECO:0000269|PubMed:22461622, ECO:0000269|PubMed:24267892,
CC ECO:0000269|PubMed:2509426}.
CC -!- BIOTECHNOLOGY: Heterologous expression of 12 carboxysomal genes in
CC E.coli (ccaA, ccmK2, ccmK3, ccmK4, ccmL, ccmM, ccmN, ccmO, ccmP, rbcL,
CC rbcS, rbcX) leads to the formation of bodies that resemble
CC carboxysomes, have densely packed paracrystalline arrays and RuBisCO
CC activity. These structures open the door to generating carboxysomes in
CC plant cells to increase their photosynthesis and productivity, as well
CC as tailoring bacterial microcompartments to specific metabolic needs
CC and molecule delivery. {ECO:0000269|PubMed:29922315}.
CC -!- SIMILARITY: Belongs to the CcmN family. {ECO:0000305}.
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DR EMBL; M30808; AAA27326.1; -; Genomic_DNA.
DR EMBL; CP000100; ABB57454.1; -; Genomic_DNA.
DR RefSeq; WP_011242446.1; NC_007604.1.
DR PDB; 7D6C; X-ray; 2.89 A; 3/4/5/F=1-118.
DR PDBsum; 7D6C; -.
DR AlphaFoldDB; P46204; -.
DR SMR; P46204; -.
DR STRING; 1140.Synpcc7942_1424; -.
DR PRIDE; P46204; -.
DR EnsemblBacteria; ABB57454; ABB57454; Synpcc7942_1424.
DR KEGG; syf:Synpcc7942_1424; -.
DR eggNOG; COG0663; Bacteria.
DR HOGENOM; CLU_069354_0_0_3; -.
DR OMA; TIGANAC; -.
DR OrthoDB; 1411505at2; -.
DR BioCyc; SYNEL:SYNPCC7942_1424-MON; -.
DR GO; GO:0031470; C:carboxysome; IDA:UniProtKB.
DR GO; GO:0043886; F:structural constituent of carboxysome; IMP:UniProtKB.
DR GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-KW.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR InterPro; IPR011004; Trimer_LpxA-like_sf.
DR SUPFAM; SSF51161; SSF51161; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Bacterial microcompartment; Carbon dioxide fixation;
KW Carboxysome; Photosynthesis.
FT CHAIN 1..161
FT /note="Carboxysome assembly protein CcmN"
FT /id="PRO_0000066463"
FT REGION 111..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 144..161
FT /note="Encapsulation peptide"
FT /evidence="ECO:0000269|PubMed:22461622"
FT COMPBIAS 112..139
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 146
FT /note="G -> D (in hcrO221, requires high CO2 levels for
FT growth)"
FT /evidence="ECO:0000269|PubMed:2509426"
FT MUTAGEN 123..161
FT /note="Missing: Interacts with CcmM."
FT /evidence="ECO:0000269|PubMed:22461622"
FT MUTAGEN 143..161
FT /note="Missing: Does not grow in normal air, forms polar
FT masses of protein larger than carboxysomes. Interacts with
FT CcmM, does not interact with CcmK2."
FT /evidence="ECO:0000269|PubMed:22461622"
FT STRAND 15..22
FT /evidence="ECO:0007829|PDB:7D6C"
FT STRAND 24..28
FT /evidence="ECO:0007829|PDB:7D6C"
FT STRAND 33..36
FT /evidence="ECO:0007829|PDB:7D6C"
FT STRAND 41..44
FT /evidence="ECO:0007829|PDB:7D6C"
FT STRAND 46..50
FT /evidence="ECO:0007829|PDB:7D6C"
FT STRAND 55..65
FT /evidence="ECO:0007829|PDB:7D6C"
FT STRAND 76..83
FT /evidence="ECO:0007829|PDB:7D6C"
FT STRAND 94..97
FT /evidence="ECO:0007829|PDB:7D6C"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:7D6C"
SQ SEQUENCE 161 AA; 16327 MW; 86B4940D21000008 CRC64;
MHLPPLEPPI SDRYFASGEV TIAADVVIAP GVLLIAEADS RIEIASGVCI GLGSVIHARG
GAIIIQAGAL LAAGVLIVGQ SIVGRQACLG ASTTLVNTSI EAGGVTAPGS LLSAETPPTT
ATVSSSEPAG RSPQSSAIAH PTKVYGKEQF LRMRQSMFPD R
