CCMP_SYNE7
ID CCMP_SYNE7 Reviewed; 213 AA.
AC Q31QW7;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Carboxysome shell protein CcmP {ECO:0000305};
DE AltName: Full=Carbon dioxide concentrating mechanism protein CcmP;
GN Name=ccmP {ECO:0000303|PubMed:23572529}; OrderedLocusNames=Synpcc7942_0520;
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 [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 [2]
RP DISRUPTION PHENOTYPE.
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).
RN [3]
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 [4] {ECO:0007744|PDB:4HT5, ECO:0007744|PDB:4HT7}
RP X-RAY CRYSTALLOGRAPHY (2.51 ANGSTROMS), FUNCTION, SUBUNIT, SUBCELLULAR
RP LOCATION, AND DOMAIN.
RC STRAIN=PCC 7942 / FACHB-805;
RX PubMed=23572529; DOI=10.1074/jbc.m113.456897;
RA Cai F., Sutter M., Cameron J.C., Stanley D.N., Kinney J.N., Kerfeld C.A.;
RT "The structure of CcmP, a tandem bacterial microcompartment domain protein
RT from the beta-carboxysome, forms a subcompartment within a
RT microcompartment.";
RL J. Biol. Chem. 288:16055-16063(2013).
RN [5] {ECO:0007744|PDB:5LSR, ECO:0007744|PDB:5LT5}
RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS), FUNCTION, SUBUNIT, AND DOMAIN.
RC STRAIN=PCC 7942 / FACHB-805;
RX PubMed=28369612; DOI=10.1093/jxb/erx070;
RA Larsson A.M., Hasse D., Valegard K., Andersson I.;
RT "Crystal structures of beta-carboxysome shell protein CcmP: ligand binding
RT correlates with the closed or open central pore.";
RL J. Exp. Bot. 68:3857-3867(2017).
CC -!- FUNCTION: Probably part of the carboxysome shell, a polyhedral
CC inclusion where RuBisCO (ribulose bisphosphate carboxylase, rbcL-rbcS)
CC is sequestered. It is thought that this protein controls transport of
CC RuBisCO reactants in and out of the carboxysome; residual densities in
CC the 4 X-ray structures suggest that differing compounds bind in
CC interior pockets, depending on the open or closed state of the pore.
CC {ECO:0000269|PubMed:23572529}.
CC -!- SUBUNIT: A dimer of stacked trimers, the same faces interact.
CC {ECO:0000269|PubMed:23572529, ECO:0000269|PubMed:28369612}.
CC -!- SUBCELLULAR LOCATION: Carboxysome {ECO:0000269|PubMed:23572529}.
CC Note=This cyanobacterium makes beta-type carboxysomes.
CC {ECO:0000269|PubMed:23572529}.
CC -!- DOMAIN: Contains 2 BMC domains, trimerizes to give a hexamer. Each
CC trimer forms a pore with an opening of about 13 Angstroms in diameter;
CC depending on the conformation of conserved residues Glu-69 and Arg-70
CC the pore is open or closed. Dimerization of the trimers forms a small
CC barrel-like compartment, accessible via the pore. Barrels with one open
CC and one closed pore or with 2 closed pores have been seen. A pocket
CC that is the right size to loosely bind RuBisCO substrates and products
CC is found between the 2 BMC domains in each monomer.
CC {ECO:0000269|PubMed:23572529, ECO:0000269|PubMed:28369612}.
CC -!- DISRUPTION PHENOTYPE: Tagging the C-terminus of this protein with a
CC fluroscent tag completely disrupts carboxysome formation.
CC {ECO:0000269|PubMed:31048338}.
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. The absence of ccaA, ccmK3, ccmK4, ccmP and rbcX
CC leads to less active RuBisCO. {ECO:0000269|PubMed:29922315}.
CC -!- SIMILARITY: Belongs to the EutL/PduB family. {ECO:0000255|PROSITE-
CC ProRule:PRU01279}.
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DR EMBL; CP000100; ABB56552.1; -; Genomic_DNA.
DR RefSeq; WP_011243312.1; NC_007604.1.
DR PDB; 4HT5; X-ray; 2.51 A; A/B/C/D/E/F=1-213.
DR PDB; 4HT7; X-ray; 3.30 A; A/B/C/D/E/F/G/H/I/J/K/L=1-213.
DR PDB; 5LSR; X-ray; 1.65 A; A/B/C=1-213.
DR PDB; 5LT5; X-ray; 1.45 A; A/B=1-213.
DR PDBsum; 4HT5; -.
DR PDBsum; 4HT7; -.
DR PDBsum; 5LSR; -.
DR PDBsum; 5LT5; -.
DR AlphaFoldDB; Q31QW7; -.
DR SMR; Q31QW7; -.
DR STRING; 1140.Synpcc7942_0520; -.
DR PRIDE; Q31QW7; -.
DR EnsemblBacteria; ABB56552; ABB56552; Synpcc7942_0520.
DR KEGG; syf:Synpcc7942_0520; -.
DR eggNOG; COG4577; Bacteria.
DR HOGENOM; CLU_091281_0_0_3; -.
DR OMA; WIEVAPG; -.
DR OrthoDB; 1374667at2; -.
DR BioCyc; SYNEL:SYNPCC7942_0520-MON; -.
DR GO; GO:0031470; C:carboxysome; IDA:UniProtKB.
DR GO; GO:0043886; F:structural constituent of carboxysome; IPI:UniProtKB.
DR GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-KW.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR Gene3D; 3.30.70.1710; -; 2.
DR InterPro; IPR044870; BMC_CP.
DR InterPro; IPR000249; BMC_dom.
DR InterPro; IPR037233; CcmK-like_sf.
DR SMART; SM00877; BMC; 2.
DR PROSITE; PS51931; BMC_CP; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Bacterial microcompartment; Carbon dioxide fixation;
KW Carboxysome; Photosynthesis; Repeat.
FT CHAIN 1..213
FT /note="Carboxysome shell protein CcmP"
FT /id="PRO_0000451246"
FT DOMAIN 4..106
FT /note="BMC circularly permuted 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01279"
FT DOMAIN 107..211
FT /note="BMC circularly permuted 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01279"
FT MOTIF 69..70
FT /note="Probably important for pore gating"
FT /evidence="ECO:0000305|PubMed:23572529,
FT ECO:0000305|PubMed:28369612"
FT SITE 18
FT /note="May bind RuBisCO reactants"
FT /evidence="ECO:0000305|PubMed:23572529,
FT ECO:0000305|PubMed:28369612"
FT STRAND 4..13
FT /evidence="ECO:0007829|PDB:5LT5"
FT HELIX 16..25
FT /evidence="ECO:0007829|PDB:5LT5"
FT STRAND 27..29
FT /evidence="ECO:0007829|PDB:5LT5"
FT STRAND 36..44
FT /evidence="ECO:0007829|PDB:5LT5"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:5LT5"
FT HELIX 48..58
FT /evidence="ECO:0007829|PDB:5LT5"
FT STRAND 62..68
FT /evidence="ECO:0007829|PDB:5LT5"
FT STRAND 73..80
FT /evidence="ECO:0007829|PDB:5LT5"
FT HELIX 82..96
FT /evidence="ECO:0007829|PDB:5LT5"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:5LT5"
FT STRAND 107..114
FT /evidence="ECO:0007829|PDB:5LT5"
FT HELIX 119..126
FT /evidence="ECO:0007829|PDB:5LT5"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:5LT5"
FT STRAND 139..147
FT /evidence="ECO:0007829|PDB:5LT5"
FT HELIX 150..161
FT /evidence="ECO:0007829|PDB:5LT5"
FT STRAND 165..170
FT /evidence="ECO:0007829|PDB:5LT5"
FT STRAND 173..182
FT /evidence="ECO:0007829|PDB:5LT5"
FT HELIX 184..200
FT /evidence="ECO:0007829|PDB:5LT5"
SQ SEQUENCE 213 AA; 23201 MW; EF4BAB17103F4939 CRC64;
MGVELRSYVY LDNLQRQHAS YIGTVATGFL TLPGDASVWI EISPGIEINR MMDIALKAAV
VRPGVQFIER LYGLMEVHAS NQGEVREAGR AVLSALGLTE RDRLKPKIVS SQIIRNIDAH
QAQLINRQRR GQMLLAGETL YVLEVQPAAY AALAANEAEK AALINILQVS AIGSFGRLFL
GGEERDIIAG SRAAVAALEN LSGREHPGDR SRE
