CCMK1_SYNY3
ID CCMK1_SYNY3 Reviewed; 111 AA.
AC P72760;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Carboxysome shell protein CcmK1 {ECO:0000303|PubMed:17993516};
DE AltName: Full=Carbon dioxide-concentrating mechanism protein CcmK1;
GN Name=ccmK1 {ECO:0000303|PubMed:17993516}; OrderedLocusNames=sll1029;
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 PROTEIN SEQUENCE OF 2-21.
RX PubMed=9298645; DOI=10.1002/elps.1150180806;
RA Sazuka T., Ohara O.;
RT "Towards a proteome project of cyanobacterium Synechocystis sp. strain
RT PCC6803: linking 130 protein spots with their respective genes.";
RL Electrophoresis 18:1252-1258(1997).
RN [3]
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 [4]
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 [5]
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 [6] {ECO:0007744|PDB:3BN4}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS), FUNCTION, SUBUNIT, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=18292340; DOI=10.1126/science.1151458;
RA Tanaka S., Kerfeld C.A., Sawaya M.R., Cai F., Heinhorst S., Cannon G.C.,
RA Yeates T.O.;
RT "Atomic-level models of the bacterial carboxysome shell.";
RL Science 319:1083-1086(2008).
RN [7] {ECO:0007744|PDB:3BN4, ECO:0007744|PDB:3DN9}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS), X-RAY CRYSTALLOGRAPHY (2.28
RP ANGSTROMS) OF 1-91, SUBUNIT, DOMAIN, AND MUTAGENESIS OF 92-ARG--ARG-111.
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).
RN [8] {ECO:0007744|PDB:4LIW}
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 1-91, AND SUBUNIT.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=24419393; DOI=10.1107/s139900471302422x;
RA Thompson M.C., Yeates T.O.;
RT "A challenging interpretation of a hexagonally layered protein structure.";
RL Acta Crystallogr. D 70:203-208(2014).
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: Probably the major shell protein of the carboxysome, a
CC polyhedral inclusion where RuBisCO (ribulose bisphosphate carboxylase,
CC rbcL-rbcS) is sequestered. The central pore probably regulates
CC metabolite flux (PubMed:18292340). Hexamers make sheets that form the
CC facets of the carboxysome (Probable) (PubMed:19844993).
CC {ECO:0000269|PubMed:18292340, ECO:0000269|PubMed:19844993,
CC ECO:0000305|PubMed:19177356, ECO:0000305|PubMed:24419393}.
CC -!- SUBUNIT: Homohexamer (PubMed:19844993, PubMed:18292340,
CC PubMed:19177356, PubMed:24419393, PubMed:31603944). Interacts with
CC full-length CcmM (PubMed:17993516). Forms mixed heterohexamers of all
CC possible stoichiometries with CcmK2, which might form dodecamers. Only
CC very weak interactions with CcmK3 and CcmK4 were seen
CC (PubMed:31603944). Interacts with CcmN and CcmO in the carboxysome (By
CC similarity). {ECO:0000250|UniProtKB:Q03511,
CC ECO:0000269|PubMed:17993516, ECO:0000269|PubMed:18292340,
CC ECO:0000269|PubMed:19177356, ECO:0000269|PubMed:19844993,
CC ECO:0000269|PubMed:24419393, ECO:0000269|PubMed:31603944}.
CC -!- SUBCELLULAR LOCATION: Carboxysome {ECO:0000255|HAMAP-Rule:MF_00854,
CC ECO:0000305|PubMed:18292340}. Note=This cyanobacterium makes beta-type
CC carboxysomes (Probable). Forms walls in the polyhedral carboxysome
CC (Probable). {ECO:0000305|PubMed:17993516, ECO:0000305|PubMed:18292340,
CC ECO:0000305|PubMed:19177356, ECO:0000305|PubMed:24419393}.
CC -!- DOMAIN: The tight homohexamer forms a pore with an opening of about 5.0
CC Angstroms in diameter which is positively charged. Sulfate ions are
CC bound in one crystal form in both the pore and between hexamers which
CC may represent metabolite flux. The C-terminal flexible tail, which is
CC the most variable part of CcmK proteins, seems to be involved in
CC packing of hexamers in layers. {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; BAA16775.1; -; Genomic_DNA.
DR PIR; S74623; S74623.
DR PDB; 3BN4; X-ray; 2.00 A; A/B/C/D/E/F=1-111.
DR PDB; 3DN9; X-ray; 2.28 A; A/B/C/D/E/F=1-91.
DR PDB; 4LIW; X-ray; 1.60 A; A/B=1-91.
DR PDBsum; 3BN4; -.
DR PDBsum; 3DN9; -.
DR PDBsum; 4LIW; -.
DR AlphaFoldDB; P72760; -.
DR SMR; P72760; -.
DR IntAct; P72760; 3.
DR STRING; 1148.1651848; -.
DR PaxDb; P72760; -.
DR EnsemblBacteria; BAA16775; BAA16775; BAA16775.
DR KEGG; syn:sll1029; -.
DR eggNOG; COG4577; Bacteria.
DR InParanoid; P72760; -.
DR OMA; QFREGVN; -.
DR PhylomeDB; P72760; -.
DR EvolutionaryTrace; P72760; -.
DR Proteomes; UP000001425; Chromosome.
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; Direct protein sequencing; Photosynthesis; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9298645"
FT CHAIN 2..111
FT /note="Carboxysome shell protein CcmK1"
FT /id="PRO_0000201506"
FT DOMAIN 4..90
FT /note="BMC"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00854"
FT MUTAGEN 92..111
FT /note="Missing: Alters hexamer layer packing."
FT /evidence="ECO:0000269|PubMed:19177356"
FT STRAND 4..12
FT /evidence="ECO:0007829|PDB:4LIW"
FT HELIX 13..26
FT /evidence="ECO:0007829|PDB:4LIW"
FT STRAND 27..36
FT /evidence="ECO:0007829|PDB:4LIW"
FT STRAND 41..48
FT /evidence="ECO:0007829|PDB:4LIW"
FT HELIX 50..64
FT /evidence="ECO:0007829|PDB:4LIW"
FT STRAND 72..80
FT /evidence="ECO:0007829|PDB:4LIW"
FT HELIX 83..87
FT /evidence="ECO:0007829|PDB:4LIW"
SQ SEQUENCE 111 AA; 12102 MW; 4C3B3E207A600609 CRC64;
MSIAVGMIET LGFPAVVEAA DSMVKAARVT LVGYEKIGSG RVTVIVRGDV SEVQASVTAG
IENIRRVNGG EVLSNHIIAR PHENLEYVLP IRYTEAVEQF REIVNPSIIR R
