CSOSA_HALNC
ID CSOSA_HALNC Reviewed; 98 AA.
AC P45689; D0KZ85;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 25-MAY-2022, entry version 101.
DE RecName: Full=Major carboxysome shell protein CsoS1A {ECO:0000303|PubMed:17518518};
GN Name=csoS1A {ECO:0000303|PubMed:9696760};
GN Synonyms=csoS1 {ECO:0000303|PubMed:7934888}; OrderedLocusNames=Hneap_0915;
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], PROTEIN SEQUENCE OF 2-18, FUNCTION, AND
RP SUBCELLULAR LOCATION.
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, AND DISRUPTION PHENOTYPE.
RX PubMed=16535117; DOI=10.1128/aem.61.9.3256-3260.1995;
RA English R.S., Jin S., Shively J.M.;
RT "Use of Electroporation To Generate a Thiobacillus neapolitanus Carboxysome
RT Mutant.";
RL Appl. Environ. Microbiol. 61:3256-3260(1995).
RN [5]
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 [6]
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 [7]
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 [8]
RP ASSEMBLY, AND SUBUNIT.
RC STRAIN=ATCC 23641 / c2;
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 [9]
RP BIOTECHNOLOGY.
RX PubMed=29922315; DOI=10.3389/fpls.2018.00739;
RA Fang Y., Huang F., Faulkner M., Jiang Q., Dykes G.F., Yang M., Liu L.N.;
RT "Engineering and Modulating Functional Cyanobacterial CO2-Fixing
RT Organelles.";
RL Front. Plant Sci. 9:739-739(2018).
RN [10]
RP FUNCTION.
RC STRAIN=ATCC 23641 / c2;
RX PubMed=30193460; DOI=10.1021/acs.jpcb.8b06822;
RA Mahinthichaichan P., Morris D.M., Wang Y., Jensen G.J., Tajkhorshid E.;
RT "Selective Permeability of Carboxysome Shell Pores to Anionic Molecules.";
RL J. Phys. Chem. B 122:9110-9118(2018).
RN [11]
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 [12]
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 [13]
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 [14] {ECO:0007744|PDB:2EWH, ECO:0007744|PDB:2G13}
RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS), FUNCTION, SUBUNIT, AND DOMAIN.
RX PubMed=17518518; DOI=10.1371/journal.pbio.0050144;
RA Tsai Y., Sawaya M.R., Cannon G.C., Cai F., Williams E.B., Heinhorst S.,
RA Kerfeld C.A., Yeates T.O.;
RT "Structural analysis of CsoS1A and the protein shell of the
RT Halothiobacillus neapolitanus carboxysome.";
RL PLoS Biol. 5:e144-e144(2007).
CC -!- FUNCTION: The major shell protein of the carboxysome, a polyhedral
CC inclusion where RuBisCO (ribulose bisphosphate carboxylase, ccbL-ccbS)
CC is sequestered (PubMed:7934888, PubMed:16535117). Assembles into
CC hexamers which make sheets that form the facets of the polyhedral
CC carboxysome (PubMed:17518518). The shell probably limits the diffusion
CC of CO(2) into and out of the carboxysome (Probable). Molecular modeling
CC shows the central pore of this protein is selectively permeable to
CC anions such as HCO(3) rather than CO(2) or O(2) (Probable). There are
CC estimated to be 2970 CsoS1A/CsoS1C proteins per carboxysome (the
CC proteins differ by only 1 residue) (Ref.5).
CC {ECO:0000269|PubMed:16535117, ECO:0000269|PubMed:17518518,
CC ECO:0000269|PubMed:7934888, ECO:0000269|Ref.5,
CC ECO:0000305|PubMed:18258595, ECO:0000305|PubMed:30193460}.
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:25826651, ECO:0000269|PubMed:33116131}.
CC -!- SUBUNIT: Homohexamer with a small central pore; the concave side is
CC mostly positive electrostatic potential, whereas the convex side is
CC mostly negative electrostatic potential (PubMed:17518518). Forms a
CC CsoS2-CsoS1-RuBisCO complex (Probable). Interacts with the N-terminus
CC (residues 1-136) of RuBisCO (CbbL) (PubMed:30305640).
CC {ECO:0000269|PubMed:17518518, ECO:0000269|PubMed:30305640,
CC ECO:0000305|PubMed:25826651}.
CC -!- SUBCELLULAR LOCATION: Carboxysome {ECO:0000269|PubMed:18258595,
CC ECO:0000269|PubMed:7934888, ECO:0000305|PubMed:29922315}. Note=This
CC bacterium makes alpha-type carboxysomes. {ECO:0000269|PubMed:17518518,
CC ECO:0000269|PubMed:18258595, ECO:0000269|Ref.5}.
CC -!- DOMAIN: The tight homohexamer forms a pore with an opening of about 4
CC Angstroms in diameter which is positively charged.
CC {ECO:0000269|PubMed:17518518}.
CC -!- DISRUPTION PHENOTYPE: Does not grow in ambient air, has a wild-type
CC growth rate in 5% CO(2), called a high-CO(2) requiring phenotype, hcr.
CC Fewer carboxysomes are present, RuBisCO is found to be soluble rather
CC than in the carboxysome. Required for growth in ambient air
CC (PubMed:31406332). {ECO:0000269|PubMed:16535117,
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). When this gene is expressed in S.elongatus PCC 7942
CC it colocalizes with its beta-carboxysomes, suggesting there a range of
CC modular possibilites for the carboxysome constituent proteins. These
CC experiments open the door to generating carboxysomes in plant cells to
CC increase their photosynthesis and productivity, as well as tailoring
CC bacterial microcompartments to specific metabolic needs and molecule
CC delivery. {ECO:0000269|PubMed:22184212, ECO:0000269|PubMed:29922315,
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; AAC32556.1; -; Genomic_DNA.
DR EMBL; CP001801; ACX95758.1; -; Genomic_DNA.
DR PIR; S49415; S49415.
DR RefSeq; WP_012823794.1; NC_013422.1.
DR PDB; 2EWH; X-ray; 1.40 A; A=1-98.
DR PDB; 2G13; X-ray; 1.61 A; A=1-98.
DR PDB; 7CKB; EM; 3.24 A; B0/B1/B2/B3/B4/B5/B6/B7/B8/B9/BA/BB/BC/BD/BE/BF/BG/BH/BI/BJ/BK/BL/BM/BN/BO/BP/BQ/BR/BS/BT=1-98.
DR PDB; 7CKC; EM; 2.90 A; B0/B1/B2/B3/B4/B5/B6/B7/B8/B9/BA/BB/BC/BD/BE/BF/BG/BH/BI/BJ/BK/BL/BM/BN/BO/BP/BQ/BR/BS/BT=1-98.
DR PDBsum; 2EWH; -.
DR PDBsum; 2G13; -.
DR PDBsum; 7CKB; -.
DR PDBsum; 7CKC; -.
DR AlphaFoldDB; P45689; -.
DR SMR; P45689; -.
DR DIP; DIP-29435N; -.
DR STRING; 555778.Hneap_0915; -.
DR EnsemblBacteria; ACX95758; ACX95758; Hneap_0915.
DR KEGG; hna:Hneap_0915; -.
DR eggNOG; COG4577; Bacteria.
DR HOGENOM; CLU_064903_5_3_6; -.
DR OMA; QFREGVN; -.
DR OrthoDB; 1802372at2; -.
DR EvolutionaryTrace; P45689; -.
DR Proteomes; UP000009102; Chromosome.
DR GO; GO:0031470; C:carboxysome; IDA:UniProtKB.
DR GO; GO:0043886; F:structural constituent of carboxysome; IDA:UniProtKB.
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; Direct protein sequencing; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7934888"
FT CHAIN 2..98
FT /note="Major carboxysome shell protein CsoS1A"
FT /id="PRO_0000201512"
FT DOMAIN 8..93
FT /note="BMC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01278"
FT STRAND 8..16
FT /evidence="ECO:0007829|PDB:2EWH"
FT HELIX 17..30
FT /evidence="ECO:0007829|PDB:2EWH"
FT STRAND 31..42
FT /evidence="ECO:0007829|PDB:2EWH"
FT STRAND 45..52
FT /evidence="ECO:0007829|PDB:2EWH"
FT HELIX 54..68
FT /evidence="ECO:0007829|PDB:2EWH"
FT STRAND 75..83
FT /evidence="ECO:0007829|PDB:2EWH"
FT HELIX 86..89
FT /evidence="ECO:0007829|PDB:2EWH"
SQ SEQUENCE 98 AA; 9963 MW; F16D0BDF1AB1EACD CRC64;
MADVTGIALG MIETRGLVPA IEAADAMTKA AEVRLVGRQF VGGGYVTVLV RGETGAVNAA
VRAGADACER VGDGLVAAHI IARVHSEVEN ILPKAPQA
