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 27-MAR-2024, entry version 95. 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}; GN OrderedLocusNames=Hneap_0916; OS Halothiobacillus neapolitanus (strain ATCC 23641 / c2) (Thiobacillus OS neapolitanus). OC Bacteria; Pseudomonadota; 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}. 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; 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 KEGG; hna:Hneap_0916; -. DR eggNOG; COG4577; Bacteria. DR HOGENOM; CLU_064903_5_3_6; -. DR OrthoDB; 9812608at2; -. 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 CDD; cd07058; BMC_CsoS1; 1. 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 PANTHER; PTHR33941:SF11; BACTERIAL MICROCOMPARTMENT SHELL PROTEIN PDUJ; 1. DR PANTHER; PTHR33941; PROPANEDIOL UTILIZATION PROTEIN PDUA; 1. DR Pfam; PF00936; BMC; 1. DR SMART; SM00877; BMC; 1. DR SUPFAM; SSF143414; CcmK-like; 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 //