CCMK2_SYNY3
ID CCMK2_SYNY3 Reviewed; 103 AA.
AC P72761;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Carboxysome shell protein CcmK2 {ECO:0000303|PubMed:17993516};
DE AltName: Full=Carbon dioxide-concentrating mechanism protein CcmK2;
GN Name=ccmK2 {ECO:0000303|PubMed:17993516}; OrderedLocusNames=sll1028;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
RN [2]
RP INTERACTION WITH CCMM.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=17993516; DOI=10.1128/jb.01283-07;
RA Cot S.S., So A.K., Espie G.S.;
RT "A multiprotein bicarbonate dehydration complex essential to carboxysome
RT function in cyanobacteria.";
RL J. Bacteriol. 190:936-945(2008).
RN [3]
RP FUNCTION, TWO-DIMENSIONAL CRYSTALS, AND SUBUNIT.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=19844993; DOI=10.1002/pro.272;
RA Dryden K.A., Crowley C.S., Tanaka S., Yeates T.O., Yeager M.;
RT "Two-dimensional crystals of carboxysome shell proteins recapitulate the
RT hexagonal packing of three-dimensional crystals.";
RL Protein Sci. 18:2629-2635(2009).
RN [4]
RP SUBUNIT.
RC STRAIN=PCC 6803 / Kazusa;
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 [5] {ECO:0007744|PDB:2A1B}
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS), FUNCTION, SUBUNIT, AND DOMAIN.
RX PubMed=16081736; DOI=10.1126/science.1113397;
RA Kerfeld C.A., Sawaya M.R., Tanaka S., Nguyen C.V., Phillips M., Beeby M.,
RA Yeates T.O.;
RT "Protein structures forming the shell of primitive bacterial organelles.";
RL Science 309:936-938(2005).
RN [6] {ECO:0007744|PDB:3CIM, ECO:0007744|PDB:3DNC}
RP X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) OF 1-91, FUNCTION, SUBUNIT, DOMAIN,
RP AND MUTAGENESIS OF 92-ARG--TYR-103.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=19177356; DOI=10.1002/pro.14;
RA Tanaka S., Sawaya M.R., Phillips M., Yeates T.O.;
RT "Insights from multiple structures of the shell proteins from the beta-
RT carboxysome.";
RL Protein Sci. 18:108-120(2009).
CC -!- FUNCTION: One of the shell proteins of the carboxysome, a polyhedral
CC inclusion where RuBisCO (ribulose bisphosphate carboxylase, rbcL-rbcS)
CC is sequestered. The central pore probably regulates metabolite flux
CC (PubMed:16081736). Hexamers make sheets that form the facets of the
CC polyhedral carboxysome (Probable) (PubMed:19844993).
CC {ECO:0000269|PubMed:16081736, ECO:0000269|PubMed:19844993,
CC ECO:0000305|PubMed:16081736, ECO:0000305|PubMed:19177356}.
CC -!- SUBUNIT: Homohexamer, might also make dodecamers (PubMed:16081736,
CC PubMed:19177356, PubMed:31603944). Interacts with full-length CcmM
CC (PubMed:17993516). Forms mixed heterohexamers of all possible
CC stoichiometries with CcmK1, which might form dodecamers. Only very weak
CC interactions with CcmK3 and CcmK4 were seen (PubMed:31603944).
CC {ECO:0000269|PubMed:16081736, ECO:0000269|PubMed:17993516,
CC ECO:0000269|PubMed:19177356, ECO:0000269|PubMed:31603944}.
CC -!- SUBCELLULAR LOCATION: Carboxysome {ECO:0000255|HAMAP-Rule:MF_00854,
CC ECO:0000305|PubMed:16081736, ECO:0000305|PubMed:17993516,
CC ECO:0000305|PubMed:19177356, ECO:0000305|PubMed:19844993}. Note=This
CC cyanobacterium makes beta-type carboxysomes.
CC {ECO:0000305|PubMed:17993516}.
CC -!- DOMAIN: The tight homohexamer forms a pore with an opening of about 5.9
CC Angstroms in diameter which is positively charged. The C-terminal
CC flexible tail, which is the most variable part of CcmK proteins, seems
CC to be involved in packing of hexamers in layers.
CC {ECO:0000269|PubMed:16081736, ECO:0000269|PubMed:19177356}.
CC -!- SIMILARITY: Belongs to the bacterial microcompartments protein family.
CC CcmK subfamily. {ECO:0000255|HAMAP-Rule:MF_00854}.
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DR EMBL; BA000022; BAA16776.1; -; Genomic_DNA.
DR PIR; S74624; S74624.
DR PDB; 2A1B; X-ray; 2.90 A; A/B/C/D/E/F/G/H/I/J/K/L=1-103.
DR PDB; 3CIM; X-ray; 1.30 A; A/B/C=1-91.
DR PDB; 3DNC; X-ray; 2.05 A; A=1-91.
DR PDBsum; 2A1B; -.
DR PDBsum; 3CIM; -.
DR PDBsum; 3DNC; -.
DR AlphaFoldDB; P72761; -.
DR SMR; P72761; -.
DR IntAct; P72761; 3.
DR STRING; 1148.1651849; -.
DR PaxDb; P72761; -.
DR EnsemblBacteria; BAA16776; BAA16776; BAA16776.
DR KEGG; syn:sll1028; -.
DR eggNOG; COG4577; Bacteria.
DR InParanoid; P72761; -.
DR OMA; HSEVEMI; -.
DR PhylomeDB; P72761; -.
DR EvolutionaryTrace; P72761; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0031470; C:carboxysome; IEA:UniProtKB-SubCell.
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; 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; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..103
FT /note="Carboxysome shell protein CcmK2"
FT /id="PRO_0000201507"
FT DOMAIN 4..90
FT /note="BMC"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00854"
FT MUTAGEN 92..103
FT /note="Missing: Alters hexamer layer packing."
FT /evidence="ECO:0000269|PubMed:19177356"
FT STRAND 4..12
FT /evidence="ECO:0007829|PDB:3CIM"
FT HELIX 13..26
FT /evidence="ECO:0007829|PDB:3CIM"
FT STRAND 27..38
FT /evidence="ECO:0007829|PDB:3CIM"
FT STRAND 41..48
FT /evidence="ECO:0007829|PDB:3CIM"
FT HELIX 50..65
FT /evidence="ECO:0007829|PDB:3CIM"
FT STRAND 71..80
FT /evidence="ECO:0007829|PDB:3CIM"
FT HELIX 83..87
FT /evidence="ECO:0007829|PDB:3CIM"
FT HELIX 98..101
FT /evidence="ECO:0007829|PDB:2A1B"
SQ SEQUENCE 103 AA; 11135 MW; 6A59E01CD4CE54CE CRC64;
MSIAVGMIET RGFPAVVEAA DSMVKAARVT LVGYEKIGSG RVTVIVRGDV SEVQASVSAG
IEAANRVNGG EVLSTHIIAR PHENLEYVLP IRYTEEVEQF RTY
