CCMK4_SYNY3
ID CCMK4_SYNY3 Reviewed; 112 AA.
AC P73407;
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 CcmK4 {ECO:0000255|HAMAP-Rule:MF_00854, ECO:0000303|PubMed:17993516};
DE AltName: Full=Carbon dioxide-concentrating mechanism protein CcmK4 {ECO:0000255|HAMAP-Rule:MF_00854};
GN Name=ccmK4 {ECO:0000255|HAMAP-Rule:MF_00854, ECO:0000303|PubMed:17993516};
GN OrderedLocusNames=slr1839;
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] {ECO:0007744|PDB:2A10, ECO:0007744|PDB:2A18}
RP X-RAY CRYSTALLOGRAPHY (1.80 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:6SCR}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 3-112, AND 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).
CC -!- FUNCTION: A probably minor shell protein component of the carboxysome,
CC a polyhedral inclusion where RuBisCO (ribulose bisphosphate
CC carboxylase, rbcL-rbcS) is sequestered. The central pore probably
CC regulates metabolite flux, as might the gaps between assembled
CC homohexamers (PubMed:16081736). Homohexamers make sheets that probably
CC form the facets of the polyhedral carboxysome (Probable)
CC (PubMed:19844993). This subunit probably makes both homohexamers and
CC heterohexamers with CcmK3 (Probable). {ECO:0000269|PubMed:16081736,
CC ECO:0000269|PubMed:19844993, ECO:0000305|PubMed:16081736,
CC ECO:0000305|PubMed:31603944}.
CC -!- SUBUNIT: Homohexamer (Probable) (PubMed:19844993, PubMed:31603944).
CC Interacts with full-length CcmM (PubMed:17993516). Forms mixed
CC heterohexamers with CcmK3, probably with 1:5 CcmK3:CcmK4 stoichiometry.
CC Only very weak interactions with CcmK1 and CcmK2 were seen
CC (PubMed:31603944). {ECO:0000269|PubMed:17993516,
CC ECO:0000269|PubMed:19844993, ECO:0000269|PubMed:31603944,
CC ECO:0000305|PubMed:16081736}.
CC -!- SUBCELLULAR LOCATION: Carboxysome {ECO:0000255|HAMAP-Rule:MF_00854,
CC ECO:0000305|PubMed:16081736, ECO:0000305|PubMed:17993516,
CC ECO:0000305|PubMed:19844993}. Note=This cyanobacterium makes beta-type
CC carboxysomes. {ECO:0000305|PubMed:17993516}.
CC -!- DOMAIN: The tight homohexamer forms a pore with an opening of about 4
CC Angstroms in diameter which is positively charged.
CC {ECO:0000269|PubMed:16081736}.
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; BAA17447.1; -; Genomic_DNA.
DR PIR; S77344; S77344.
DR PDB; 2A10; X-ray; 1.80 A; A/B/C/D/E/F=1-112.
DR PDB; 2A18; X-ray; 2.28 A; A/B/C=1-112.
DR PDB; 3GV2; X-ray; 7.00 A; A/B/C/D/E/F=1-110.
DR PDB; 6SCR; X-ray; 1.80 A; A/B=3-112.
DR PDBsum; 2A10; -.
DR PDBsum; 2A18; -.
DR PDBsum; 3GV2; -.
DR PDBsum; 6SCR; -.
DR AlphaFoldDB; P73407; -.
DR SMR; P73407; -.
DR IntAct; P73407; 3.
DR STRING; 1148.1652526; -.
DR PaxDb; P73407; -.
DR EnsemblBacteria; BAA17447; BAA17447; BAA17447.
DR KEGG; syn:slr1839; -.
DR eggNOG; COG4577; Bacteria.
DR InParanoid; P73407; -.
DR OMA; ESWVIIP; -.
DR PhylomeDB; P73407; -.
DR EvolutionaryTrace; P73407; -.
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; Direct protein sequencing; Photosynthesis; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9298645"
FT CHAIN 2..112
FT /note="Carboxysome shell protein CcmK4"
FT /id="PRO_0000201509"
FT DOMAIN 6..92
FT /note="BMC"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00854"
FT STRAND 6..14
FT /evidence="ECO:0007829|PDB:6SCR"
FT HELIX 15..28
FT /evidence="ECO:0007829|PDB:6SCR"
FT STRAND 29..40
FT /evidence="ECO:0007829|PDB:6SCR"
FT STRAND 43..50
FT /evidence="ECO:0007829|PDB:6SCR"
FT HELIX 52..67
FT /evidence="ECO:0007829|PDB:6SCR"
FT STRAND 74..82
FT /evidence="ECO:0007829|PDB:6SCR"
FT HELIX 85..90
FT /evidence="ECO:0007829|PDB:6SCR"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:6SCR"
FT HELIX 100..106
FT /evidence="ECO:0007829|PDB:6SCR"
SQ SEQUENCE 112 AA; 11903 MW; F483C04B1FEBC150 CRC64;
MSAQSAVGSI ETIGFPGILA AADAMVKAGR ITIVGYIRAG SARFTLNIRG DVQEVKTAMA
AGIDAINRTE GADVKTWVII PRPHENVVAV LPIDFSPEVE PFREAAEGLN RR
