ID   CSOSD_HYDCU             Reviewed;         205 AA.
AC   Q31HC6;
DT   10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   25-MAY-2022, entry version 70.
DE   RecName: Full=Carboxysome shell protein CsoS1D;
GN   Name=csoS1D {ECO:0000305}; OrderedLocusNames=Tcr_0851;
OS   Hydrogenovibrio crunogenus (strain DSM 25203 / XCL-2) (Thiomicrospira
OS   crunogena).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Piscirickettsiaceae; Hydrogenovibrio.
OX   NCBI_TaxID=317025;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 25203 / XCL-2;
RX   PubMed=17105352; DOI=10.1371/journal.pbio.0040383;
RA   Scott K.M., Sievert S.M., Abril F.N., Ball L.A., Barrett C.J., Blake R.A.,
RA   Boller A.J., Chain P.S.G., Clark J.A., Davis C.R., Detter C., Do K.F.,
RA   Dobrinski K.P., Faza B.I., Fitzpatrick K.A., Freyermuth S.K., Harmer T.L.,
RA   Hauser L.J., Huegler M., Kerfeld C.A., Klotz M.G., Kong W.W., Land M.,
RA   Lapidus A., Larimer F.W., Longo D.L., Lucas S., Malfatti S.A., Massey S.E.,
RA   Martin D.D., McCuddin Z., Meyer F., Moore J.L., Ocampo L.H. Jr., Paul J.H.,
RA   Paulsen I.T., Reep D.K., Ren Q., Ross R.L., Sato P.Y., Thomas P.,
RA   Tinkham L.E., Zeruth G.T.;
RT   "The genome of deep-sea vent chemolithoautotroph Thiomicrospira crunogena
RT   XCL-2.";
RL   PLoS Biol. 4:1-17(2006).
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. {ECO:0000250|UniProtKB:Q7V2D3}.
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:0000250|UniProtKB:Q7V2D3}.
CC       Note=This bacterium makes alpha-type carboxysomes. {ECO:0000305}.
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   -!- SIMILARITY: Belongs to the EutL/PduB family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01279}.
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DR   EMBL; CP000109; ABB41447.1; -; Genomic_DNA.
DR   RefSeq; WP_011370274.1; NC_007520.2.
DR   AlphaFoldDB; Q31HC6; -.
DR   SMR; Q31HC6; -.
DR   STRING; 317025.Tcr_0851; -.
DR   EnsemblBacteria; ABB41447; ABB41447; Tcr_0851.
DR   KEGG; tcx:Tcr_0851; -.
DR   eggNOG; COG4577; Bacteria.
DR   HOGENOM; CLU_091281_0_0_6; -.
DR   OMA; WIEVAPG; -.
DR   OrthoDB; 1374667at2; -.
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   Pfam; PF00936; BMC; 1.
DR   SMART; SM00877; BMC; 1.
DR   SUPFAM; SSF143414; SSF143414; 1.
DR   PROSITE; PS51931; BMC_CP; 2.
PE   3: Inferred from homology;
KW   Bacterial microcompartment; Carbon dioxide fixation; Carboxysome; Repeat.
FT   CHAIN           1..205
FT                   /note="Carboxysome shell protein CsoS1D"
FT                   /id="PRO_0000452076"
FT   DOMAIN          3..100
FT                   /note="BMC circularly permuted 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01279"
FT   DOMAIN          106..205
FT                   /note="BMC circularly permuted 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01279"
FT   MOTIF           68..69
FT                   /note="Gates the pore"
FT                   /evidence="ECO:0000250|UniProtKB:Q7V2D3"
SQ   SEQUENCE   205 AA;  22682 MW;  D6716B1C2523E8D5 CRC64;
     MIELRTYVFL DSLQPQLASY MATASMGFLP VPGDSSLWIE VAPGMAVHRL SDIALKASNV
     RLGQQIVERA YGSMVIHHRD QSDVLEAGQR ILDHLQTREY DRQQCVVMWN EIIRGVTADH
     ATLINRDNRK GSMILPGQSM FIMETEPAGY IIYAANEAEK AADVTLVEAR AVGAYGRLVM
     CGKEGDITEA ARAANEALKR LTCRS