CSOSD_HALNC
ID CSOSD_HALNC Reviewed; 213 AA.
AC D0KZ73;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2009, sequence version 1.
DT 25-MAY-2022, entry version 48.
DE RecName: Full=Carboxysome shell protein CsoS1D {ECO:0000303|PubMed:22184212};
GN Name=csoS1D {ECO:0000303|PubMed:22184212}; OrderedLocusNames=Hneap_0903;
OS Halothiobacillus neapolitanus (strain ATCC 23641 / c2) (Thiobacillus
OS neapolitanus).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC Halothiobacillaceae; Halothiobacillus.
OX NCBI_TaxID=555778;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23641 / c2;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Davenport K., Brettin T., Detter J.C., Han C.,
RA Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Kerfeld C., Cannon G., Heinhort S.;
RT "Complete sequence of Halothiobacillus neapolitanus c2.";
RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, AND BIOTECHNOLOGY.
RC STRAIN=ATCC 23641 / c2;
RX PubMed=22184212; DOI=10.1073/pnas.1108557109;
RA Bonacci W., Teng P.K., Afonso B., Niederholtmeyer H., Grob P., Silver P.A.,
RA Savage D.F.;
RT "Modularity of a carbon-fixing protein organelle.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:478-483(2012).
RN [3]
RP DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 23641 / c2;
RX PubMed=31406332; DOI=10.1038/s41564-019-0520-8;
RA Desmarais J.J., Flamholz A.I., Blikstad C., Dugan E.J., Laughlin T.G.,
RA Oltrogge L.M., Chen A.W., Wetmore K., Diamond S., Wang J.Y., Savage D.F.;
RT "DABs are inorganic carbon pumps found throughout prokaryotic phyla.";
RL Nat. Microbiol. 4:2204-2215(2019).
RN [4]
RP CARBOXYSOME ASSEMBLY, AND BIOTECHNOLOGY.
RX PubMed=33116131; DOI=10.1038/s41467-020-19280-0;
RA Li T., Jiang Q., Huang J., Aitchison C.M., Huang F., Yang M., Dykes G.F.,
RA He H.L., Wang Q., Sprick R.S., Cooper A.I., Liu L.N.;
RT "Reprogramming bacterial protein organelles as a nanoreactor for hydrogen
RT production.";
RL Nat. Commun. 11:5448-5448(2020).
CC -!- FUNCTION: Part of the carboxysome shell, a polyhedral inclusion where
CC RuBisCO (ribulose bisphosphate carboxylase, cbbL-cbbS) is sequestered.
CC It may control transport of RuBisCO reactants in and out of the
CC carboxysome (By similarity). In an E.coli expression system not
CC absolutely necessary, its presence leads to fewer defective
CC carboxysomes, suggesting this subunit may play a role in assembly
CC (PubMed:22184212). {ECO:0000250|UniProtKB:Q7V2D3,
CC ECO:0000269|PubMed:22184212}.
CC -!- FUNCTION: Unlike beta-carboxysomes, alpha-carboxysomes (Cb) can form
CC without cargo protein. CsoS2 is essential for Cb formation and is also
CC capable of targeting foreign proteins to the Cb. The Cb shell assembles
CC with the aid of CsoS2; CsoS1A, CsoS1B and CsoS1C form the majority of
CC the shell while CsoS4A and CsoS4B form vertices. CsoS1D forms
CC pseudohexamers that probably control metabolite flux into and out of
CC the shell. {ECO:0000269|PubMed:33116131}.
CC -!- SUBUNIT: Homotrimer. Forms a dimer of stacked trimers, the same faces
CC interact. Probably forms a CsoS1-CsoS1D-CsoS2 complex.
CC {ECO:0000250|UniProtKB:Q7V2D3}.
CC -!- SUBCELLULAR LOCATION: Carboxysome {ECO:0000305|PubMed:22184212}.
CC Note=This bacterium makes alpha-type carboxysomes.
CC {ECO:0000269|PubMed:22184212}.
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. Each stacked hexamer can form a pore of about 14
CC Angstroms in diameter. Dimerization of the trimers forms a channel-like
CC compartment, accessible via an open pore. This channel may be large
CC enough to accomodate transport of substrates into and out of the
CC carboxysome. {ECO:0000250|UniProtKB:Q7V2D3}.
CC -!- DISRUPTION PHENOTYPE: Not required for growth in ambient air.
CC {ECO:0000269|PubMed:31406332}.
CC -!- BIOTECHNOLOGY: Expression of 10 genes for alpha-carboxysome (Cb)
CC proteins (cbbL-cbbS-csoS2-csoS3-csoS4A-csoS4B-csoS1C-csoS1A-csoS1B-
CC csoS1D) in E.coli generates compartments that resemble Cb, contain
CC RuBisCO and have its catalytic activity, showing it is possible to make
CC artificial, functional Cb using these 10 genes. Cargo proteins can be
CC targeted to these organelles (PubMed:22184212). Artificial Cb assembly
CC in E.coli requires csoS2-csoS4A-csoS4B-csoS1C-csoS1A-csoS1B-csoS1D (but
CC not the gene for carbonic anhydrase, csoS3). Targeting proteins to the
CC organelle requires at least one of the CsoS2 C-repeats; 3 repeats gives
CC the best localization. A nanoreactor of the Cb shell proteins has been
CC engineered which generates H(2) using a ferredoxin-hydrogenase fusion
CC (AC P07839-Q9FYU1) and a flavodoxin/ferredoxin--NADP reductase (AC
CC A0A0K3QZA5) targeted separately to the Cb; the hydrogenase has first to
CC be matured and activated by HydGXEF (AC Q8EAH9, Q8EAH8, Q8EAH7 and
CC Q8EAH6 respectively). Encapsulation increases H(2) production about 20%
CC during anaerobic growth, and over 4-fold more during aerobic growth
CC (PubMed:33116131). {ECO:0000269|PubMed:22184212,
CC ECO:0000269|PubMed:33116131}.
CC -!- SIMILARITY: Belongs to the EutL/PduB family. {ECO:0000255|PROSITE-
CC ProRule:PRU01279}.
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DR EMBL; CP001801; ACX95746.1; -; Genomic_DNA.
DR RefSeq; WP_012823782.1; NC_013422.1.
DR PDB; 7DHQ; X-ray; 2.70 A; A/B/C/D/E/F=1-213.
DR PDBsum; 7DHQ; -.
DR AlphaFoldDB; D0KZ73; -.
DR SMR; D0KZ73; -.
DR STRING; 555778.Hneap_0903; -.
DR EnsemblBacteria; ACX95746; ACX95746; Hneap_0903.
DR KEGG; hna:Hneap_0903; -.
DR eggNOG; COG4577; Bacteria.
DR HOGENOM; CLU_091281_0_0_6; -.
DR OMA; WIEVAPG; -.
DR OrthoDB; 1374667at2; -.
DR Proteomes; UP000009102; Chromosome.
DR GO; GO:0031470; C:carboxysome; IEA:UniProtKB-SubCell.
DR GO; GO:0015977; P:carbon fixation; 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 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; Reference proteome; Repeat.
FT CHAIN 1..213
FT /note="Carboxysome shell protein CsoS1D"
FT /id="PRO_0000452075"
FT DOMAIN 5..106
FT /note="BMC circularly permuted 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01279"
FT DOMAIN 108..213
FT /note="BMC circularly permuted 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01279"
FT MOTIF 70..71
FT /note="Gates the pore"
FT /evidence="ECO:0000250|UniProtKB:Q7V2D3"
FT STRAND 5..14
FT /evidence="ECO:0007829|PDB:7DHQ"
FT HELIX 17..26
FT /evidence="ECO:0007829|PDB:7DHQ"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:7DHQ"
FT STRAND 37..45
FT /evidence="ECO:0007829|PDB:7DHQ"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:7DHQ"
FT HELIX 49..59
FT /evidence="ECO:0007829|PDB:7DHQ"
FT STRAND 63..69
FT /evidence="ECO:0007829|PDB:7DHQ"
FT STRAND 74..82
FT /evidence="ECO:0007829|PDB:7DHQ"
FT HELIX 83..97
FT /evidence="ECO:0007829|PDB:7DHQ"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:7DHQ"
FT STRAND 108..115
FT /evidence="ECO:0007829|PDB:7DHQ"
FT HELIX 120..128
FT /evidence="ECO:0007829|PDB:7DHQ"
FT STRAND 140..150
FT /evidence="ECO:0007829|PDB:7DHQ"
FT HELIX 153..163
FT /evidence="ECO:0007829|PDB:7DHQ"
FT STRAND 167..172
FT /evidence="ECO:0007829|PDB:7DHQ"
FT STRAND 178..184
FT /evidence="ECO:0007829|PDB:7DHQ"
FT HELIX 186..205
FT /evidence="ECO:0007829|PDB:7DHQ"
SQ SEQUENCE 213 AA; 23451 MW; 12BD98417A6A61E9 CRC64;
MNNIDLRVYS FIDSLQPQLA SYLATSSQGF LPVPGDACLW IEVAPGMAVH RLSDIALKAT
NVRLGEQVVE RAFGSMEIHY RNQSDVLASG EAVLREINHA QEDRLPCRIA WKEIIRAITP
DHATLINRQL RKGSMLLPGK SMFILETEPA GYIVQAANEA EKAAHVTLID VRAFGNFGRL
TMMGSEAETE EAMRAAEATI ASINARARRA EGF
