CCMK2_SYNE7
ID CCMK2_SYNE7 Reviewed; 102 AA.
AC Q03511; Q31NB8;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Carboxysome shell protein CcmK2 {ECO:0000303|PubMed:22928045};
DE AltName: Full=Carbon dioxide-concentrating mechanism protein CcmK2;
GN Name=ccmK2 {ECO:0000303|PubMed:22928045};
GN Synonyms=ccmK {ECO:0000303|PubMed:8491708},
GN ccmK1 {ECO:0000303|PubMed:17675289, ECO:0000303|PubMed:20304968};
GN OrderedLocusNames=Synpcc7942_1421;
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], AND DISRUPTION PHENOTYPE.
RC STRAIN=PCC 7942 / FACHB-805;
RX PubMed=8491708; DOI=10.1128/jb.175.10.2871-2879.1993;
RA Price G.D., Howitt S.M., Harrison K., Badger M.R.;
RT "Analysis of a genomic DNA region from the cyanobacterium Synechococcus sp.
RT strain PCC7942 involved in carboxysome assembly and function.";
RL J. Bacteriol. 175:2871-2879(1993).
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 SUBCELLULAR LOCATION.
RC STRAIN=PCC 7942 / FACHB-805;
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 [4]
RP SUBCELLULAR LOCATION.
RC STRAIN=PCC 7942 / FACHB-805;
RX PubMed=20304968; DOI=10.1104/pp.110.154948;
RA Long B.M., Tucker L., Badger M.R., Price G.D.;
RT "Functional cyanobacterial beta-carboxysomes have an absolute requirement
RT for both long and short forms of the CcmM protein.";
RL Plant Physiol. 153:285-293(2010).
RN [5]
RP FUNCTION, INTERACTION WITH CCMO, SUBCELLULAR LOCATION, AND DISRUPTION
RP 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 [6]
RP INTERACTION WITH CCMN.
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 [7]
RP CARBOXYSOME ASSEMBLY PROCESS, FUNCTION, AND SUBCELLULAR LOCATION.
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 [8]
RP SUBCELLULAR LOCATION.
RC STRAIN=PCC 7942 / FACHB-805;
RX PubMed=28616951; DOI=10.1039/c7nr02524f;
RA Faulkner M., Rodriguez-Ramos J., Dykes G.F., Owen S.V., Casella S.,
RA Simpson D.M., Beynon R.J., Liu L.N.;
RT "Direct characterization of the native structure and mechanics of
RT cyanobacterial carboxysomes.";
RL Nanoscale 9:10662-10673(2017).
RN [9]
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 [10]
RP SUBCELLULAR LOCATION.
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 [11]
RP SUBUNIT.
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 [12] {ECO:0007744|PDB:4OX7}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS), SUBUNIT, SUBCELLULAR LOCATION,
RP DOMAIN, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF 34-TYR--ILE-37 AND
RP 35-GLU--ILE-37.
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).
CC -!- FUNCTION: One of the shell proteins of the carboxysome, a polyhedral
CC inclusion where RuBisCO (ribulose bisphosphate carboxylase, rbcL-rbcS)
CC is sequestered. Assembles into hexamers which make sheets that form the
CC facets of the polyhedral carboxysome. The hexamer central pore probably
CC regulates metabolite flux. {ECO:0000255|HAMAP-Rule:MF_00854}.
CC -!- FUNCTION: The major shell protein of the carboxysome, a polyhedral
CC inclusion where RuBisCO (ribulose bisphosphate carboxylase, rbcL-rbcS)
CC is sequestered. Hexamers make sheets that form the facets of the
CC polyhedral carboxysome (PubMed:22928045). The shell is 4.5 nm thick, as
CC observed for CcmK hexamers (PubMed:28616951). Required for recruitment
CC of CcmO to the pre-carboxysome (PubMed:22928045, PubMed:24267892). In
CC PCC 7942 there are several CcmK paralogs with presumably functional
CC differences; replacing the central pore residues (34-37) with those of
CC either CcmK4 from this organism (Tyr-Met-Arg-Ala) or from an alpha-type
CC carboxysome forming cyanobacterium (CsoS1 of P.marinus strain MIT 9313,
CC Arg-Glu-Phe-Val) allows the bacterium to make carboxysomes, but the
CC expression level is too low to know if the carboxysome is functional
CC for CO(2) fixation (PubMed:25117559). {ECO:0000269|PubMed:22928045,
CC ECO:0000269|PubMed:24267892, ECO:0000269|PubMed:25117559,
CC ECO:0000269|PubMed:28616951}.
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: Homohexamer (PubMed:25117559, PubMed:30389783). Interacts with
CC CcmO in the carboxysome (PubMed:22928045). Interacts with CcmN
CC (PubMed:22461622). {ECO:0000269|PubMed:22461622,
CC ECO:0000269|PubMed:22928045, ECO:0000269|PubMed:25117559,
CC ECO:0000269|PubMed:30389783}.
CC -!- SUBCELLULAR LOCATION: Carboxysome {ECO:0000255|HAMAP-Rule:MF_00854,
CC ECO:0000269|PubMed:17675289, ECO:0000269|PubMed:20304968,
CC ECO:0000269|PubMed:22928045, ECO:0000269|PubMed:24267892,
CC ECO:0000269|PubMed:25117559, ECO:0000269|PubMed:28616951,
CC ECO:0000269|PubMed:31048338}. Note=This cyanobacterium makes beta-type
CC carboxysomes. {ECO:0000269|PubMed:22928045,
CC ECO:0000269|PubMed:25117559}.
CC -!- DOMAIN: The tight homohexamer forms a pore with an opening of about 5
CC Angstroms in diameter and is positively charged.
CC {ECO:0000269|PubMed:25117559}.
CC -!- DISRUPTION PHENOTYPE: Cells do not grow in normal air but do grow on 2%
CC CO(2), called a high-CO(2) requiring phenotype, HCR (PubMed:8491708,
CC PubMed:22928045). Cells make aberrantly large polar bodies instead of
CC wild-type carboxysomes, no accumulation of CcmO (PubMed:22928045,
CC PubMed:24267892). An alternatively generated deletion mutant does not
CC form abnormal polar bodies (PubMed:25117559).
CC {ECO:0000269|PubMed:22928045, ECO:0000269|PubMed:24267892,
CC ECO:0000269|PubMed:25117559, ECO:0000269|PubMed:8491708}.
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 bacterial microcompartments protein family.
CC CcmK subfamily. {ECO:0000255|HAMAP-Rule:MF_00854}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=A peculiar architecture
CC - Issue 237 of June 2021;
CC URL="https://web.expasy.org/spotlight/back_issues/237/";
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DR EMBL; M96929; AAA27304.1; -; Genomic_DNA.
DR EMBL; CP000100; ABB57451.1; -; Genomic_DNA.
DR PIR; B36904; B36904.
DR RefSeq; WP_011242449.1; NC_007604.1.
DR PDB; 4OX7; X-ray; 2.10 A; A/B/C/D/E/F=1-102.
DR PDBsum; 4OX7; -.
DR AlphaFoldDB; Q03511; -.
DR SMR; Q03511; -.
DR STRING; 1140.Synpcc7942_1421; -.
DR PRIDE; Q03511; -.
DR EnsemblBacteria; ABB57451; ABB57451; Synpcc7942_1421.
DR KEGG; syf:Synpcc7942_1421; -.
DR eggNOG; COG4577; Bacteria.
DR HOGENOM; CLU_064903_5_3_3; -.
DR OMA; HSEVEMI; -.
DR OrthoDB; 1802372at2; -.
DR BioCyc; SYNEL:SYNPCC7942_1421-MON; -.
DR GO; GO:0031470; C:carboxysome; IDA:UniProtKB.
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; 3.30.70.1710; -; 1.
DR HAMAP; MF_00854; CcmK; 1.
DR InterPro; IPR020808; Bact_microcomp_CS.
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; PS01139; BMC_1; 1.
DR PROSITE; PS51930; BMC_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Bacterial microcompartment; Carbon dioxide fixation;
KW Carboxysome; Photosynthesis.
FT CHAIN 1..102
FT /note="Carboxysome shell protein CcmK2"
FT /id="PRO_0000201503"
FT DOMAIN 4..90
FT /note="BMC"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00854"
FT MUTAGEN 34..37
FT /note="YEKI->REFV: Probably alters pore properties, is able
FT to form carboxysomes, residues correspond to CsoS1 of
FT P.marinus MIT 9313."
FT /evidence="ECO:0000269|PubMed:25117559"
FT MUTAGEN 35..37
FT /note="EKI->MRA: Probably alters pore properties, is able
FT to form carboxysomes, residues correspond to CcmK4 of this
FT organism."
FT /evidence="ECO:0000269|PubMed:25117559"
FT STRAND 4..12
FT /evidence="ECO:0007829|PDB:4OX7"
FT HELIX 13..26
FT /evidence="ECO:0007829|PDB:4OX7"
FT STRAND 27..38
FT /evidence="ECO:0007829|PDB:4OX7"
FT STRAND 41..48
FT /evidence="ECO:0007829|PDB:4OX7"
FT HELIX 50..64
FT /evidence="ECO:0007829|PDB:4OX7"
FT STRAND 72..80
FT /evidence="ECO:0007829|PDB:4OX7"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:4OX7"
FT HELIX 95..100
FT /evidence="ECO:0007829|PDB:4OX7"
SQ SEQUENCE 102 AA; 10904 MW; 7B7C0F5A3D1E1CB7 CRC64;
MPIAVGMIET LGFPAVVEAA DAMVKAARVT LVGYEKIGSG RVTVIVRGDV SEVQASVSAG
LDSAKRVAGG EVLSHHIIAR PHENLEYVLP IRYTEAVEQF RM
