CSOSD_PROMP
ID CSOSD_PROMP Reviewed; 256 AA.
AC Q7V2D3;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Carboxysome shell protein CsoS1D {ECO:0000303|PubMed:19328811};
GN Name=csoS1D {ECO:0000303|PubMed:19328811}; OrderedLocusNames=PMM0547;
OS Prochlorococcus marinus subsp. pastoris (strain CCMP1986 / NIES-2087 /
OS MED4).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=59919;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP1986 / NIES-2087 / MED4;
RX PubMed=12917642; DOI=10.1038/nature01947;
RA Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A.,
RA Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L.,
RA Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C.,
RA Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R.,
RA Chisholm S.W.;
RT "Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche
RT differentiation.";
RL Nature 424:1042-1047(2003).
RN [2]
RP PROTEIN ABUNDANCE, AND SUBCELLULAR LOCATION.
RC STRAIN=CCMP1986 / NIES-2087 / MED4;
RX PubMed=22155772; DOI=10.1128/jb.06444-11;
RA Roberts E.W., Cai F., Kerfeld C.A., Cannon G.C., Heinhorst S.;
RT "Isolation and characterization of the Prochlorococcus carboxysome reveal
RT the presence of the novel shell protein CsoS1D.";
RL J. Bacteriol. 194:787-795(2012).
RN [3]
RP SUBUNIT.
RC STRAIN=CCMP1986 / NIES-2087 / MED4;
RX PubMed=25826651; DOI=10.3390/life5021141;
RA Cai F., Dou Z., Bernstein S.L., Leverenz R., Williams E.B., Heinhorst S.,
RA Shively J., Cannon G.C., Kerfeld C.A.;
RT "Advances in Understanding Carboxysome Assembly in Prochlorococcus and
RT Synechococcus Implicate CsoS2 as a Critical Component.";
RL Life 5:1141-1171(2015).
RN [4] {ECO:0007744|PDB:3F56, ECO:0007744|PDB:3FCH}
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS), POSSIBLE FUNCTION, IDENTIFICATION,
RP SUBUNIT, SUBCELLULAR LOCATION, AND DOMAIN.
RC STRAIN=CCMP1986 / NIES-2087 / MED4;
RX PubMed=19328811; DOI=10.1016/j.jmb.2009.03.056;
RA Klein M.G., Zwart P., Bagby S.C., Cai F., Chisholm S.W., Heinhorst S.,
RA Cannon G.C., Kerfeld C.A.;
RT "Identification and structural analysis of a novel carboxysome shell
RT protein with implications for metabolite transport.";
RL J. Mol. Biol. 392:319-333(2009).
CC -!- FUNCTION: Part of the carboxysome shell, a polyhedral inclusion where
CC RuBisCO (ribulose bisphosphate carboxylase, cbbL-cbbS) is sequestered
CC (Probable) (PubMed:22155772). It may control transport of RuBisCO
CC reactants in and out of the carboxysome (Probable). There are estimated
CC to be 6 CsoS1D hexamers per carboxysome (PubMed:22155772).
CC {ECO:0000269|PubMed:22155772, ECO:0000305|PubMed:19328811}.
CC -!- SUBUNIT: Homotrimer. Forms a dimer of stacked trimers, the same faces
CC interact (PubMed:19328811). A CsoS1-CsoS1D-CsoS2 complex can be
CC isolated following expression in E.coli (PubMed:25826651).
CC {ECO:0000269|PubMed:19328811, ECO:0000269|PubMed:25826651}.
CC -!- SUBCELLULAR LOCATION: Carboxysome {ECO:0000269|PubMed:22155772,
CC ECO:0000305|PubMed:19328811}. Note=Fractionates with shell proteins
CC (PubMed:22155772). This bacterium makes alpha-type carboxysomes
CC (PubMed:19328811). {ECO:0000269|PubMed:19328811,
CC ECO:0000269|PubMed:22155772}.
CC -!- DOMAIN: Contains 2 BMC domains, trimerizes in a staggered manner to
CC give a hexamer; each subunit in one trimer interacts with 2 subunits in
CC the facing trimer. In each stacked hexamer one trimer forms a pore of
CC about 14 Angstroms in diameter; open-closed and open-open trimers are
CC seen in crystals. Glu-120 forms a salt bridge with Arg-121 of the
CC adjacent subunit to close the pore. Dimerization of the trimers forms a
CC channel-like compartment (volume 13,610 Angstroms(3)), accessible via
CC an open pore. This channel may be large enough to accomodate transport
CC of substrates into and out of the carboxysome.
CC {ECO:0000269|PubMed:19328811}.
CC -!- SIMILARITY: Belongs to the EutL/PduB family. {ECO:0000255|PROSITE-
CC ProRule:PRU01279}.
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DR EMBL; BX548174; CAE19006.1; -; Genomic_DNA.
DR RefSeq; WP_011132182.1; NC_005072.1.
DR PDB; 3F56; X-ray; 2.30 A; A/B/C/D/E/F=1-256.
DR PDB; 3FCH; X-ray; 2.20 A; A/B=1-256.
DR PDBsum; 3F56; -.
DR PDBsum; 3FCH; -.
DR AlphaFoldDB; Q7V2D3; -.
DR SMR; Q7V2D3; -.
DR STRING; 59919.PMM0547; -.
DR EnsemblBacteria; CAE19006; CAE19006; PMM0547.
DR KEGG; pmm:PMM0547; -.
DR eggNOG; COG4577; Bacteria.
DR HOGENOM; CLU_091281_0_0_3; -.
DR OMA; WIEVAPG; -.
DR OrthoDB; 1374667at2; -.
DR EvolutionaryTrace; Q7V2D3; -.
DR Proteomes; UP000001026; Chromosome.
DR GO; GO:0031470; C:carboxysome; IEA:UniProtKB-SubCell.
DR GO; GO:0043886; F:structural constituent of carboxysome; IEA:UniProt.
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; -; 2.
DR InterPro; IPR044870; BMC_CP.
DR InterPro; IPR000249; BMC_dom.
DR InterPro; IPR037233; CcmK-like_sf.
DR Pfam; PF00936; BMC; 1.
DR SMART; SM00877; BMC; 1.
DR SUPFAM; SSF143414; SSF143414; 1.
DR PROSITE; PS51931; BMC_CP; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Bacterial microcompartment; Carbon dioxide fixation;
KW Carboxysome; Photosynthesis; Repeat.
FT CHAIN 1..256
FT /note="Carboxysome shell protein CsoS1D"
FT /id="PRO_0000452077"
FT DOMAIN 55..157
FT /note="BMC circularly permuted 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01279"
FT DOMAIN 158..256
FT /note="BMC circularly permuted 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01279"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 120..121
FT /note="Gates the pore"
FT /evidence="ECO:0000269|PubMed:19328811,
FT ECO:0007744|PDB:3F56"
FT HELIX 51..53
FT /evidence="ECO:0007829|PDB:3F56"
FT STRAND 55..64
FT /evidence="ECO:0007829|PDB:3FCH"
FT HELIX 67..76
FT /evidence="ECO:0007829|PDB:3FCH"
FT STRAND 87..95
FT /evidence="ECO:0007829|PDB:3FCH"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:3FCH"
FT HELIX 99..108
FT /evidence="ECO:0007829|PDB:3FCH"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:3F56"
FT STRAND 113..118
FT /evidence="ECO:0007829|PDB:3FCH"
FT STRAND 124..131
FT /evidence="ECO:0007829|PDB:3FCH"
FT HELIX 133..147
FT /evidence="ECO:0007829|PDB:3FCH"
FT HELIX 151..153
FT /evidence="ECO:0007829|PDB:3F56"
FT STRAND 161..167
FT /evidence="ECO:0007829|PDB:3FCH"
FT HELIX 170..177
FT /evidence="ECO:0007829|PDB:3FCH"
FT TURN 178..180
FT /evidence="ECO:0007829|PDB:3FCH"
FT STRAND 191..199
FT /evidence="ECO:0007829|PDB:3FCH"
FT HELIX 200..202
FT /evidence="ECO:0007829|PDB:3FCH"
FT HELIX 203..213
FT /evidence="ECO:0007829|PDB:3FCH"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:3FCH"
FT STRAND 224..234
FT /evidence="ECO:0007829|PDB:3FCH"
FT HELIX 236..251
FT /evidence="ECO:0007829|PDB:3FCH"
SQ SEQUENCE 256 AA; 27510 MW; BEBEAC1007018260 CRC64;
MEPTSSLNRG DRKKGSSLVT GSEVQSQSNG ASCFITTDSE KSLVSRQASQ VEQIELRTYV
FLDSLQPQLA AYMGTVSRGF LPIPGDSCLW MEVSPGMAVH RVTDIALKAS NVRLGQMIVE
RAFGSLALYH KDQSTVLHSG DVVLDAIGSE VRKRTKPSTS WTEVICAITP DHAVLINRQN
RSGSMIQSGM SMFILETEPA GYVLKAANEA EKSANITIID VKAVGAFGRL TLAGKEGDVE
EAAAAAIRAI DQISNY
