CCMK4_HALP7
ID CCMK4_HALP7 Reviewed; 117 AA.
AC K9Y6N7;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2013, sequence version 1.
DT 03-AUG-2022, entry version 39.
DE RecName: Full=Carboxysome shell protein CcmK4 {ECO:0000303|PubMed:30389783};
DE AltName: Full=Carbon dioxide-concentrating mechanism protein CcmK4 {ECO:0000255|HAMAP-Rule:MF_00854};
GN Name=ccmK4 {ECO:0000303|PubMed:30389783}; OrderedLocusNames=PCC7418_0347;
OS Halothece sp. (strain PCC 7418) (Synechococcus sp. (strain PCC 7418)).
OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC Aphanothecaceae; Halothece cluster; Halothece; unclassified Halothece.
OX NCBI_TaxID=65093;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7418;
RX PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT genome sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
RN [2] {ECO:0007744|PDB:5VGU}
RP X-RAY CRYSTALLOGRAPHY (1.81 ANGSTROMS), SUBUNIT, SUBCELLULAR LOCATION, AND
RP DOMAIN.
RC STRAIN=PCC 7418;
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).
CC -!- FUNCTION: A probably essential, minor shell protein of the carboxysome,
CC a polyhedral inclusion where RuBisCO (ribulose bisphosphate
CC carboxylase, rbcL-rbcS) is sequestered. Hexamers form sheets that form
CC the facets of the polyhedral carboxysome. In PCC 7418 there are several
CC CcmK paralogs with presumably functional differences. This subunit can
CC probably make both homohexamers and heterohexamers with CcmK3. Both
CC hexamers can also make dodecamers, formation depends on buffer
CC conditions. {ECO:0000269|PubMed:30389783}.
CC -!- SUBUNIT: Crystallizes as a homohexamer. Interacts stably with CcmK3,
CC forming heterohexamers that can make dodecamers. Heterohexamers have a
CC 1:2 CcmK3:CcmK4 stoichiometry. Upon expression in E.coli forms large
CC aggregates. {ECO:0000269|PubMed:30389783}.
CC -!- SUBCELLULAR LOCATION: Carboxysome {ECO:0000255|HAMAP-Rule:MF_00854,
CC ECO:0000305|PubMed:30389783}. Note=This cyanobacterium makes beta-type
CC carboxysomes. {ECO:0000305}.
CC -!- DOMAIN: The tight homohexamer forms a small pore which is positively
CC charged. {ECO:0000255|HAMAP-Rule:MF_00854,
CC ECO:0000269|PubMed:30389783}.
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; CP003945; AFZ42581.1; -; Genomic_DNA.
DR RefSeq; WP_015224459.1; NC_019779.1.
DR PDB; 5VGU; X-ray; 1.81 A; A/B/C/D/E/F=1-117.
DR PDBsum; 5VGU; -.
DR AlphaFoldDB; K9Y6N7; -.
DR SMR; K9Y6N7; -.
DR STRING; 65093.PCC7418_0347; -.
DR EnsemblBacteria; AFZ42581; AFZ42581; PCC7418_0347.
DR KEGG; hao:PCC7418_0347; -.
DR PATRIC; fig|65093.3.peg.363; -.
DR eggNOG; COG4577; Bacteria.
DR HOGENOM; CLU_064903_5_0_3; -.
DR OMA; ESWVIIP; -.
DR OrthoDB; 1802372at2; -.
DR Proteomes; UP000010481; Chromosome.
DR GO; GO:0031470; C:carboxysome; IEA:UniProtKB-SubCell.
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; 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; 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..117
FT /note="Carboxysome shell protein CcmK4"
FT /id="PRO_0000451238"
FT DOMAIN 5..91
FT /note="BMC"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00854"
FT STRAND 4..13
FT /evidence="ECO:0007829|PDB:5VGU"
FT HELIX 14..27
FT /evidence="ECO:0007829|PDB:5VGU"
FT STRAND 28..39
FT /evidence="ECO:0007829|PDB:5VGU"
FT STRAND 42..49
FT /evidence="ECO:0007829|PDB:5VGU"
FT HELIX 51..65
FT /evidence="ECO:0007829|PDB:5VGU"
FT STRAND 72..81
FT /evidence="ECO:0007829|PDB:5VGU"
FT HELIX 84..89
FT /evidence="ECO:0007829|PDB:5VGU"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:5VGU"
FT HELIX 99..104
FT /evidence="ECO:0007829|PDB:5VGU"
SQ SEQUENCE 117 AA; 12602 MW; F2C56EEE49FBEB74 CRC64;
MSLDAVGSLE TKGFPGVLAA ADAMVKTGRV TLVGYIRAGS ARFTIIIRGD VSEVKTAMDA
GIHAVDKAYG AALETWVIIP RPHENVECVL PIAYNENVER FRESTERPLI GSSQNRS
