CCMK3_SYNE7
ID CCMK3_SYNE7 Reviewed; 102 AA.
AC Q31RK3;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Carboxysome shell protein CcmK3 {ECO:0000303|PubMed:22928045};
DE AltName: Full=Carbon dioxide-concentrating mechanism protein CcmK3;
GN Name=ccmK3 {ECO:0000303|PubMed:22928045};
GN OrderedLocusNames=Synpcc7942_0284;
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 FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=PCC 7942 / FACHB-805;
RX PubMed=22928045; DOI=10.1371/journal.pone.0043871;
RA Rae B.D., Long B.M., Badger M.R., Price G.D.;
RT "Structural determinants of the outer shell of beta-carboxysomes in
RT Synechococcus elongatus PCC 7942: roles for CcmK2, K3-K4, CcmO, and CcmL.";
RL PLoS ONE 7:e43871-e43871(2012).
RN [3]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=PCC 7942 / FACHB-805;
RX PubMed=25117559; DOI=10.1021/sb500226j;
RA Cai F., Sutter M., Bernstein S.L., Kinney J.N., Kerfeld C.A.;
RT "Engineering bacterial microcompartment shells: chimeric shell proteins and
RT chimeric carboxysome shells.";
RL ACS Synth. Biol. 4:444-453(2015).
RN [4]
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 [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=PCC 7942 / FACHB-805;
RX PubMed=30389783; DOI=10.1104/pp.18.01190;
RA Sommer M., Sutter M., Gupta S., Kirst H., Turmo A., Lechno-Yossef S.,
RA Burton R.L., Saechao C., Sloan N.B., Cheng X., Chan L.G., Petzold C.J.,
RA Fuentes-Cabrera M., Ralston C.Y., Kerfeld C.A.;
RT "Heterohexamers Formed by CcmK3 and CcmK4 Increase the Complexity of Beta
RT Carboxysome Shells.";
RL Plant Physiol. 179:156-167(2019).
RN [6]
RP SUBUNIT.
RC STRAIN=PCC 7942 / FACHB-805;
RX PubMed=31603944; DOI=10.1371/journal.pone.0223877;
RA Garcia-Alles L.F., Root K., Maveyraud L., Aubry N., Lesniewska E.,
RA Mourey L., Zenobi R., Truan G.;
RT "Occurrence and stability of hetero-hexamer associations formed by beta-
RT carboxysome CcmK shell components.";
RL PLoS ONE 14:e0223877-e0223877(2019).
RN [7]
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: A non-essential, minor shell protein of the carboxysome, a
CC polyhedral inclusion where RuBisCO (ribulose bisphosphate carboxylase,
CC rbcL-rbcS) is sequestered. Hexamers form sheets that form the facets of
CC the polyhedral carboxysome. In PCC 7942 there are several CcmK paralogs
CC with presumably functional differences (PubMed:22928045,
CC PubMed:25117559). This subunit probably only makes heterohexamers with
CC CcmK4. The CcmK3-CcmK4 heterohexmers have been suggested to cap other
CC hexamers, perhaps to alter metabolite flux (Probable).
CC {ECO:0000269|PubMed:22928045, ECO:0000269|PubMed:25117559,
CC ECO:0000305|PubMed:30389783}.
CC -!- SUBUNIT: Interacts stably with CcmK4, probably forms heterohexamers
CC with a 1:2 CcmK3:CcmK4 stoichiometry (PubMed:30389783) (Probable).
CC Bulky residues in the pore region probably preclude the formation of
CC homohexamers by this subunit (Probable). {ECO:0000269|PubMed:30389783,
CC ECO:0000305|PubMed:30389783, ECO:0000305|PubMed:31603944}.
CC -!- SUBCELLULAR LOCATION: Carboxysome {ECO:0000255|HAMAP-Rule:MF_00854,
CC ECO:0000269|PubMed:30389783, ECO:0000269|PubMed:31048338,
CC ECO:0000305|PubMed:25117559}. Note=This cyanobacterium makes beta-type
CC carboxysomes. {ECO:0000269|PubMed:25117559}.
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 15 units of this protein per carboxysome, the numbers are
CC stable under low light and high light, and increase under high CO(2)
CC (at protein level). The CcmK3:CcmK4 ratio of 1:3.8 is stable over all
CC growth conditions. {ECO:0000269|PubMed:31048338}.
CC -!- DISRUPTION PHENOTYPE: Single deletion has a wild-type phenotype, a
CC double ccmK3-ccmK4 deletion has slightly larger, aggregated instead of
CC spatially separated carboxysomes, and has a photosynthetic affinity for
CC inorganic carbon between wild-type and carboxysome-less strains
CC (PubMed:22928045). In another study single mutant is wild-type, double
CC ccmK3-ccmK4 mutant has impaired growth rate; ccmK3 does not complement
CC the double deletion, while ccmK4 does (PubMed:30389783).
CC {ECO:0000269|PubMed:22928045, ECO:0000269|PubMed:30389783}.
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 bacterial microcompartments protein family.
CC CcmK subfamily. {ECO:0000255|HAMAP-Rule:MF_00854}.
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DR EMBL; CP000100; ABB56316.1; -; Genomic_DNA.
DR RefSeq; WP_011243540.1; NC_007604.1.
DR AlphaFoldDB; Q31RK3; -.
DR SMR; Q31RK3; -.
DR STRING; 1140.Synpcc7942_0284; -.
DR PRIDE; Q31RK3; -.
DR EnsemblBacteria; ABB56316; ABB56316; Synpcc7942_0284.
DR KEGG; syf:Synpcc7942_0284; -.
DR eggNOG; COG4577; Bacteria.
DR HOGENOM; CLU_064903_5_0_3; -.
DR OMA; ITHYIVP; -.
DR OrthoDB; 1802372at2; -.
DR BioCyc; SYNEL:SYNPCC7942_0284-MON; -.
DR GO; GO:0031470; C:carboxysome; IMP: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; -; 1.
DR HAMAP; MF_00854; CcmK; 1.
DR InterPro; IPR000249; BMC_dom.
DR InterPro; IPR046380; CcmK.
DR InterPro; IPR037233; CcmK-like_sf.
DR InterPro; IPR044872; CcmK/CsoS1_BMC.
DR Pfam; PF00936; BMC; 1.
DR SMART; SM00877; BMC; 1.
DR SUPFAM; SSF143414; SSF143414; 1.
DR PROSITE; PS51930; BMC_2; 1.
PE 1: Evidence at protein level;
KW Bacterial microcompartment; Carbon dioxide fixation; Carboxysome;
KW Photosynthesis.
FT CHAIN 1..102
FT /note="Carboxysome shell protein CcmK3"
FT /id="PRO_0000451235"
FT DOMAIN 4..90
FT /note="BMC"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00854"
SQ SEQUENCE 102 AA; 10794 MW; 80009A7C392BE56E CRC64;
MPIAVGTIQT LGFPPIIAAA DAMVKAARVT ITQYGLAESA QFFVSVRGPV SEVETAVEAG
LKAVAETEGA ELINYIVIPN PQENVETVMP IDFTAESEPF RS
