CSOSC_HALNC
ID CSOSC_HALNC Reviewed; 98 AA.
AC P45688; D0KZ86;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=Carboxysome shell protein CsoS1C {ECO:0000303|PubMed:19690376};
GN Name=csoS1C {ECO:0000303|PubMed:9696760};
GN Synonyms=Orf1 {ECO:0000303|PubMed:7934888}; OrderedLocusNames=Hneap_0916;
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 [GENOMIC DNA].
RC STRAIN=ATCC 23641 / c2;
RX PubMed=7934888; DOI=10.1111/j.1365-2958.1994.tb01052.x;
RA English R.S., Lorbach S.C., Qin X., Shively J.M.;
RT "Isolation and characterization of a carboxysome shell gene from
RT Thiobacillus neapolitanus.";
RL Mol. Microbiol. 12:647-654(1994).
RN [2]
RP SEQUENCE REVISION TO 69-98.
RC STRAIN=ATCC 23641 / c2;
RX PubMed=9696760; DOI=10.1128/jb.180.16.4133-4139.1998;
RA Baker S.H., Jin S., Aldrich H.C., Howard G.T., Shively J.M.;
RT "Insertion mutation of the form I cbbL gene encoding ribulose bisphosphate
RT carboxylase/oxygenase (RuBisCO) in Thiobacillus neapolitanus results in
RT expression of form II RuBisCO, loss of carboxysomes, and an increased CO2
RT requirement for growth.";
RL J. Bacteriol. 180:4133-4139(1998).
RN [3]
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 [4]
RP FUNCTION, PROTEIN ABUNDANCE, AND SUBCELLULAR LOCATION.
RX DOI=10.1007/7171_023;
RA Heinhorst S., Cannon G.C., Shively J.M.;
RT "Carboxysomes and Carboxysome-like Inclusions.";
RL (In) Shively J.M. (eds.);
RL Microbiology Monographs, pp.2:141-164, Springer-Verlag, Berlin (2006).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 23641 / c2;
RX PubMed=18258595; DOI=10.1074/jbc.m709285200;
RA Dou Z., Heinhorst S., Williams E.B., Murin C.D., Shively J.M., Cannon G.C.;
RT "CO2 fixation kinetics of Halothiobacillus neapolitanus mutant carboxysomes
RT lacking carbonic anhydrase suggest the shell acts as a diffusional barrier
RT for CO2.";
RL J. Biol. Chem. 283:10377-10384(2008).
RN [6]
RP 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 [7]
RP INTERACTION WITH CBBL, AND BIOTECHNOLOGY.
RC STRAIN=ATCC 23641 / c2;
RX PubMed=30305640; DOI=10.1038/s41598-018-33074-x;
RA Liu Y., He X., Lim W., Mueller J., Lawrie J., Kramer L., Guo J., Niu W.;
RT "Deciphering molecular details in the assembly of alpha-type carboxysome.";
RL Sci. Rep. 8:15062-15062(2018).
RN [8]
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 [9]
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).
RN [10] {ECO:0007744|PDB:3H8Y}
RP X-RAY CRYSTALLOGRAPHY (2.51 ANGSTROMS), FUNCTION, SUBUNIT, AND DOMAIN.
RX PubMed=19690376; DOI=10.1107/s0907444909025153;
RA Tsai Y., Sawaya M.R., Yeates T.O.;
RT "Analysis of lattice-translocation disorder in the layered hexagonal
RT structure of carboxysome shell protein CsoS1C.";
RL Acta Crystallogr. D 65:980-988(2009).
CC -!- FUNCTION: One of shell proteins of the carboxysome, a polyhedral
CC inclusion where RuBisCO (ribulose bisphosphate carboxylase, ccbL-ccbS)
CC is sequestered. Assembles into hexamers which make sheets that form the
CC facets of the polyhedral carboxysome (Probable). The shell probably
CC limits the diffusion of CO(2) into and out of the carboxysome
CC (Probable). There are estimated to be 2970 CsoS1A/CsoS1C proteins per
CC carboxysome (the proteins differ by only 1 residue) (Ref.4).
CC {ECO:0000269|Ref.4, ECO:0000305|PubMed:18258595,
CC ECO:0000305|PubMed:19690376}.
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: Homohexamer with a small central pore (PubMed:19690376).
CC Interacts with the N-terminus (residues 1-136) of RuBisCO (CbbL)
CC (PubMed:30305640). {ECO:0000269|PubMed:19690376,
CC ECO:0000269|PubMed:30305640}.
CC -!- SUBCELLULAR LOCATION: Carboxysome {ECO:0000269|PubMed:18258595,
CC ECO:0000305|PubMed:19690376}. Note=This bacterium makes alpha-type
CC carboxysomes. {ECO:0000269|PubMed:18258595, ECO:0000269|Ref.4,
CC ECO:0000305}.
CC -!- DOMAIN: The tight homohexamer forms a pore with an opening of about 2
CC Angstroms in diameter which is positively charged.
CC {ECO:0000269|PubMed:19690376}.
CC -!- DISRUPTION PHENOTYPE: 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, PubMed:30305640).
CC Artificial Cb assembly in E.coli requires csoS2-csoS4A-csoS4B-csoS1C-
CC csoS1A-csoS1B-csoS1D (but not the gene for carbonic anhydrase, csoS3).
CC Targeting proteins to the organelle requires at least one of the CsoS2
CC C-repeats; 3 repeats gives the best localization. A nanoreactor of the
CC Cb shell proteins has been engineered which generates H(2) using a
CC ferredoxin-hydrogenase fusion (AC P07839-Q9FYU1) and a
CC flavodoxin/ferredoxin--NADP reductase (AC A0A0K3QZA5) targeted
CC separately to the Cb; the hydrogenase has first to be matured and
CC activated by HydGXEF (AC Q8EAH9, Q8EAH8, Q8EAH7 and Q8EAH6
CC respectively). Encapsulation increases H(2) production about 20% during
CC anaerobic growth, and over 4-fold more during aerobic growth
CC (PubMed:33116131). {ECO:0000269|PubMed:22184212,
CC ECO:0000269|PubMed:30305640, ECO:0000269|PubMed:33116131}.
CC -!- SIMILARITY: Belongs to the bacterial microcompartments protein family.
CC CsoS1 subfamily. {ECO:0000305}.
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DR EMBL; AF038430; AAC32555.1; -; Genomic_DNA.
DR EMBL; CP001801; ACX95759.1; -; Genomic_DNA.
DR PIR; S49414; S49414.
DR RefSeq; WP_012823795.1; NC_013422.1.
DR PDB; 3H8Y; X-ray; 2.51 A; A=1-98.
DR PDBsum; 3H8Y; -.
DR AlphaFoldDB; P45688; -.
DR SMR; P45688; -.
DR STRING; 555778.Hneap_0916; -.
DR EnsemblBacteria; ACX95759; ACX95759; Hneap_0916.
DR KEGG; hna:Hneap_0916; -.
DR eggNOG; COG4577; Bacteria.
DR HOGENOM; CLU_064903_5_3_6; -.
DR OMA; HSEVEMI; -.
DR OrthoDB; 1802372at2; -.
DR EvolutionaryTrace; P45688; -.
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; -; 1.
DR InterPro; IPR020808; Bact_microcomp_CS.
DR InterPro; IPR000249; BMC_dom.
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; Reference proteome.
FT CHAIN 1..98
FT /note="Carboxysome shell protein CsoS1C"
FT /id="PRO_0000201514"
FT DOMAIN 8..93
FT /note="BMC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01278"
FT STRAND 8..16
FT /evidence="ECO:0007829|PDB:3H8Y"
FT HELIX 17..30
FT /evidence="ECO:0007829|PDB:3H8Y"
FT STRAND 34..40
FT /evidence="ECO:0007829|PDB:3H8Y"
FT STRAND 45..52
FT /evidence="ECO:0007829|PDB:3H8Y"
FT HELIX 54..68
FT /evidence="ECO:0007829|PDB:3H8Y"
FT STRAND 75..83
FT /evidence="ECO:0007829|PDB:3H8Y"
FT HELIX 86..89
FT /evidence="ECO:0007829|PDB:3H8Y"
SQ SEQUENCE 98 AA; 9919 MW; 8107CCAF6DB19AC8 CRC64;
MAAVTGIALG MIETRGLVPA IEAADAMTKA AEVRLVGRQF VGGGYVTVLV RGETGAVNAA
VRAGADACER VGDGLVAAHI IARVHSEVEN ILPKAPEA
