CSS4A_HALNC
ID CSS4A_HALNC Reviewed; 83 AA.
AC O85043; D0KZ88;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 72.
DE RecName: Full=Carboxysome shell vertex protein CsoS4A;
GN Name=csoS4A {ECO:0000303|PubMed:18292340};
GN Synonyms=orfA {ECO:0000303|PubMed:9696760}; OrderedLocusNames=Hneap_0918;
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=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 [2]
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 [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 23641 / c2;
RX PubMed=19844578; DOI=10.1371/journal.pone.0007521;
RA Cai F., Menon B.B., Cannon G.C., Curry K.J., Shively J.M., Heinhorst S.;
RT "The pentameric vertex proteins are necessary for the icosahedral
RT carboxysome shell to function as a CO2 leakage barrier.";
RL PLoS ONE 4:e7521-e7521(2009).
RN [4]
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 [5]
RP DISCUSSION OF SEQUENCE, AND DOMAIN.
RX PubMed=31171360; DOI=10.1016/j.bbrc.2019.05.047;
RA Zhao Y.Y., Jiang Y.L., Chen Y., Zhou C.Z., Li Q.;
RT "Crystal structure of pentameric shell protein CsoS4B of Halothiobacillus
RT neapolitanus alpha-carboxysome.";
RL Biochem. Biophys. Res. Commun. 515:510-515(2019).
RN [6]
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 [7]
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 [8] {ECO:0007744|PDB:2RCF}
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS), FUNCTION, SUBUNIT, SUBCELLULAR
RP LOCATION, AND DOMAIN.
RX PubMed=18292340; DOI=10.1126/science.1151458;
RA Tanaka S., Kerfeld C.A., Sawaya M.R., Cai F., Heinhorst S., Cannon G.C.,
RA Yeates T.O.;
RT "Atomic-level models of the bacterial carboxysome shell.";
RL Science 319:1083-1086(2008).
CC -!- FUNCTION: Probably forms vertices in the carboxysome, a polyhedral
CC inclusion where RuBisCO (ribulose bisphosphate carboxylase, cbbL-cbbS)
CC is sequestered. Has been modeled to induce curvature upon insertion
CC into an otherwise flat hexagonal layer of major carboxysome subunits
CC (Probable). A minor shell protein, only 12 pentamers of CsoS4A/CsoS4B
CC are calculated to be present in each carboxysome. The 2 CsoS4 proteins
CC contribute to the impermeability of the carboxysome to CO(2)
CC (PubMed:19844578). {ECO:0000269|PubMed:19844578,
CC ECO:0000305|PubMed:18292340}.
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: Homopentamer. {ECO:0000269|PubMed:18292340}.
CC -!- SUBCELLULAR LOCATION: Carboxysome {ECO:0000269|PubMed:19844578,
CC ECO:0000305|PubMed:18292340}. Note=Probably forms vertices in the
CC polyhedral carboxysome (Probable). This bacterium makes alpha-type
CC carboxysomes (PubMed:19844578). {ECO:0000269|PubMed:19844578,
CC ECO:0000305|PubMed:18292340}.
CC -!- DOMAIN: The tight homopentamer forms a pore with an opening of about
CC 3.5 Angstroms in diameter which is positively charged
CC (PubMed:18292340). A short loop (residues 30-33) protrudes above the
CC center of the concave face to different degrees (Probable).
CC {ECO:0000269|PubMed:18292340, ECO:0000305|PubMed:31171360}.
CC -!- DISRUPTION PHENOTYPE: A double csoS4a-csoS4B disruption does not grow
CC in ambient air, has a wild-type growth rate in 5% CO(2), called a high-
CC CO(2) requiring phenotype, hcr. It does not grow to the same cell
CC density as wild-type. 1/3 fewer carboxysomes are seen per cell, about
CC 13% of which are elongated. The carboxysome shell is more permeable
CC than usual to inorganic carbon. Required for growth in ambient air
CC (PubMed:31406332). {ECO:0000269|PubMed:19844578,
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 CcmL/EutN family. CsoS4 subfamily.
CC {ECO:0000305}.
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DR EMBL; AF038430; AAC32553.1; -; Genomic_DNA.
DR EMBL; CP001801; ACX95761.1; -; Genomic_DNA.
DR RefSeq; WP_012823797.1; NC_013422.1.
DR PDB; 2RCF; X-ray; 2.15 A; A/B/C/D/E=1-83.
DR PDB; 7CKB; EM; 3.24 A; A0/A1/A2/A3/A4/A5/A6/A7/A8/A9/AA/AB/AC/AD/AE/AF/AG/AH/AI/AJ/AK/AL/AM/AN/AO/AP/AQ/AR/AS/AT=1-83.
DR PDB; 7CKC; EM; 2.90 A; A0/A1/A2/A3/A4/A5/A6/A7/A8/A9/AA/AB/AC/AD/AE/AF/AG/AH/AI/AJ/AK/AL/AM/AN/AO/AP/AQ/AR/AS/AT=1-83.
DR PDBsum; 2RCF; -.
DR PDBsum; 7CKB; -.
DR PDBsum; 7CKC; -.
DR AlphaFoldDB; O85043; -.
DR SMR; O85043; -.
DR STRING; 555778.Hneap_0918; -.
DR EnsemblBacteria; ACX95761; ACX95761; Hneap_0918.
DR KEGG; hna:Hneap_0918; -.
DR eggNOG; COG4576; Bacteria.
DR HOGENOM; CLU_148498_1_0_6; -.
DR OMA; GCKPGDW; -.
DR OrthoDB; 1832681at2; -.
DR EvolutionaryTrace; O85043; -.
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; cd01614; EutN_CcmL; 1.
DR Gene3D; 2.40.50.220; -; 1.
DR InterPro; IPR014076; CsoS4A.
DR InterPro; IPR004992; EutN_CcmL.
DR InterPro; IPR036677; EutN_CcmL_sf.
DR Pfam; PF03319; EutN_CcmL; 1.
DR SUPFAM; SSF159133; SSF159133; 1.
DR TIGRFAMs; TIGR02703; carboxysome_A; 1.
DR PROSITE; PS51932; BMV; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Bacterial microcompartment; Carbon dioxide fixation;
KW Carboxysome; Reference proteome.
FT CHAIN 1..83
FT /note="Carboxysome shell vertex protein CsoS4A"
FT /id="PRO_0000452079"
FT DOMAIN 1..78
FT /note="BMV"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01280"
FT STRAND 2..9
FT /evidence="ECO:0007829|PDB:2RCF"
FT STRAND 12..15
FT /evidence="ECO:0007829|PDB:2RCF"
FT STRAND 24..30
FT /evidence="ECO:0007829|PDB:2RCF"
FT STRAND 36..42
FT /evidence="ECO:0007829|PDB:2RCF"
FT STRAND 49..54
FT /evidence="ECO:0007829|PDB:2RCF"
FT HELIX 57..61
FT /evidence="ECO:0007829|PDB:2RCF"
FT STRAND 70..76
FT /evidence="ECO:0007829|PDB:2RCF"
SQ SEQUENCE 83 AA; 8891 MW; 249647EAAA6A1967 CRC64;
MKIMQVEKTL VSTNRIADMG HKPLLVVWEK PGAPRQVAVD AIGCIPGDWV LCVGSSAARE
AAGSKSYPSD LTIIGIIDQW NGE
