CCMK2_THEVB
ID CCMK2_THEVB Reviewed; 102 AA.
AC Q8DKB2;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Carboxysome shell protein CcmK2 {ECO:0000255|HAMAP-Rule:MF_00854, ECO:0000303|PubMed:24504539};
DE AltName: Full=Carbon dioxide-concentrating mechanism protein CcmK2 {ECO:0000255|HAMAP-Rule:MF_00854};
GN Name=ccmK2 {ECO:0000255|HAMAP-Rule:MF_00854, ECO:0000303|PubMed:24504539};
GN OrderedLocusNames=tll0947;
OS Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1).
OC Bacteria; Cyanobacteria; Pseudanabaenales; Thermosynechococcaceae;
OC Thermosynechococcus.
OX NCBI_TaxID=197221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C.,
RA Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takeuchi C., Yamada M., Tabata S.;
RT "Complete genome structure of the thermophilic cyanobacterium
RT Thermosynechococcus elongatus BP-1.";
RL DNA Res. 9:123-130(2002).
RN [2]
RP SUBUNIT.
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=24504539; DOI=10.1007/s11120-014-9973-z;
RA Keeling T.J., Samborska B., Demers R.W., Kimber M.S.;
RT "Interactions and structural variability of beta-carboxysomal shell protein
RT CcmL.";
RL Photosyn. Res. 121:125-133(2014).
RN [3] {ECO:0007744|PDB:3SSQ, ECO:0007744|PDB:3SSR}
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS), SUBUNIT, DOMAIN, AND MUTAGENESIS OF
RP 91-ILE--ASN-102 AND GLU-95.
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=22748766; DOI=10.1016/j.str.2012.05.013;
RA Samborska B., Kimber M.S.;
RT "A dodecameric CcmK2 structure suggests beta-carboxysomal shell facets have
RT a double-layered organization.";
RL Structure 20:1353-1362(2012).
CC -!- FUNCTION: Probably the major shell protein of the carboxysome, a
CC polyhedral inclusion where RuBisCO (ribulose bisphosphate carboxylase,
CC rbcL-rbcS) is sequestered. Assembles into hexamers which make sheets
CC that form the facets of the polyhedral carboxysome. The hexamer central
CC pore probably regulates metabolite flux. {ECO:0000255|HAMAP-
CC Rule:MF_00854, ECO:0000305|PubMed:22748766}.
CC -!- SUBUNIT: Homohexamer. Stacked hexamers, with the concave faces
CC together, have also been crystallized. Interacts preferentially with
CC itself, then with CcmK1 and CcmK4a in vitro (PubMed:22748766). May
CC interact with CcmL, this occurs at very high CcmK2 concentrations
CC (Probable). Interacts with CcmN and CcmO in the carboxysome (By
CC similarity). {ECO:0000250|UniProtKB:Q03511,
CC ECO:0000269|PubMed:22748766, ECO:0000305|PubMed:24504539}.
CC -!- INTERACTION:
CC Q8DKB2; Q8DKB3: ccmK1; NbExp=2; IntAct=EBI-15992959, EBI-15992989;
CC Q8DKB2; Q8DKB2: ccmK2; NbExp=5; IntAct=EBI-15992959, EBI-15992959;
CC -!- SUBCELLULAR LOCATION: Carboxysome {ECO:0000255|HAMAP-Rule:MF_00854,
CC ECO:0000305|PubMed:22748766, ECO:0000305|PubMed:24504539}. Note=This
CC cyanobacterium makes beta-type carboxysomes.
CC {ECO:0000269|PubMed:22748766}.
CC -!- DOMAIN: The tight homhexamer forms an irregular pore with an opening
CC about 4.8 X 6.5 Angstroms. {ECO:0000269|PubMed:22748766}.
CC -!- SIMILARITY: Belongs to the bacterial microcompartments protein family.
CC CcmK subfamily. {ECO:0000255|HAMAP-Rule:MF_00854}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BA000039; BAC08499.1; -; Genomic_DNA.
DR RefSeq; NP_681737.1; NC_004113.1.
DR RefSeq; WP_011056791.1; NC_004113.1.
DR PDB; 3SSQ; X-ray; 2.20 A; A/B/C/D/E/F=1-102.
DR PDB; 3SSR; X-ray; 1.60 A; A/B=1-102.
DR PDBsum; 3SSQ; -.
DR PDBsum; 3SSR; -.
DR AlphaFoldDB; Q8DKB2; -.
DR SMR; Q8DKB2; -.
DR DIP; DIP-59852N; -.
DR IntAct; Q8DKB2; 2.
DR STRING; 197221.22294670; -.
DR EnsemblBacteria; BAC08499; BAC08499; BAC08499.
DR KEGG; tel:tll0947; -.
DR PATRIC; fig|197221.4.peg.994; -.
DR eggNOG; COG4577; Bacteria.
DR OMA; HSEVEMI; -.
DR OrthoDB; 1802372at2; -.
DR Proteomes; UP000000440; Chromosome.
DR GO; GO:0031470; C:carboxysome; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
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 CHAIN 1..102
FT /note="Carboxysome shell protein CcmK2"
FT /id="PRO_0000451240"
FT DOMAIN 4..90
FT /note="BMC"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00854"
FT MUTAGEN 91..102
FT /note="Missing: Form hexamers poorly."
FT /evidence="ECO:0000269|PubMed:22748766"
FT MUTAGEN 95
FT /note="E->A: Form hexamers poorly."
FT /evidence="ECO:0000269|PubMed:22748766"
FT STRAND 3..12
FT /evidence="ECO:0007829|PDB:3SSR"
FT HELIX 13..26
FT /evidence="ECO:0007829|PDB:3SSR"
FT STRAND 27..38
FT /evidence="ECO:0007829|PDB:3SSR"
FT STRAND 41..49
FT /evidence="ECO:0007829|PDB:3SSR"
FT HELIX 50..66
FT /evidence="ECO:0007829|PDB:3SSR"
FT STRAND 72..80
FT /evidence="ECO:0007829|PDB:3SSR"
FT HELIX 83..86
FT /evidence="ECO:0007829|PDB:3SSR"
FT HELIX 95..99
FT /evidence="ECO:0007829|PDB:3SSR"
SQ SEQUENCE 102 AA; 10907 MW; 6BB01AA257FB2633 CRC64;
MPIAVGMIET RGFPAVVEAA DAMVKAARVT LVGYEKIGSG RVTVIVRGDV SEVQASVAAG
VDSAKRVNGG EVLSTHIIAR PHENLEYVLP IRYTEAVEQF RN
