CSS4B_HALNC
ID CSS4B_HALNC Reviewed; 81 AA.
AC O85044; D0KZ87;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 63.
DE RecName: Full=Carboxysome shell vertex protein CsoS4B;
GN Name=csoS4B {ECO:0000303|PubMed:18292340};
GN Synonyms=orfB {ECO:0000303|PubMed:9696760}; OrderedLocusNames=Hneap_0917;
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 DISCUSSION OF SEQUENCE.
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).
RN [4]
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 [5]
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 [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:6JY5}
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 1-77, SUBUNIT, 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).
CC -!- FUNCTION: Probably forms vertices in the carboxysome. Has been modeled
CC to induce curvature upon insertion into an otherwise flat hexagonal
CC layer of major carboxysome subunits (Probable). A minor shell protein,
CC only 12 pentamers of CsoS4A/CsoS4B are calculated to be present in each
CC carboxysome. The 2 CsoS4 proteins contribute to the impermeability of
CC the carboxysome to CO(2) (PubMed:19844578). Its central pore is
CC probably too small to allow passage of metabolites; its function might
CC be to anchor different proteins or metabolites to the carboxysome
CC (Probable). {ECO:0000269|PubMed:19844578, 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:31171360}.
CC -!- SUBCELLULAR LOCATION: Carboxysome {ECO:0000269|PubMed:18292340}.
CC Note=Probably forms vertices in the icosahedral carboxysome (By
CC similarity). This bacterium makes alpha-type carboxysomes
CC (PubMed:19844578). {ECO:0000250|UniProtKB:O85043,
CC ECO:0000269|PubMed:19844578}.
CC -!- DOMAIN: Forms a stable homopentamer with a convex and concave side. A
CC short loop (residues 60-69) protrudes above the center of the convex
CC face to different degrees. The tight homopentamer forms a pore with an
CC opening of about 2.9 Angstroms in diameter at its most narrow,
CC surrounded by the amino acids Ser-Gly-Ser-Ala-Ala (one from each
CC subunit). {ECO:0000269|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; AAC32554.1; -; Genomic_DNA.
DR EMBL; CP001801; ACX95760.1; -; Genomic_DNA.
DR RefSeq; WP_012823796.1; NC_013422.1.
DR PDB; 6JY5; X-ray; 2.15 A; A/B/C/D/E=1-77.
DR PDBsum; 6JY5; -.
DR AlphaFoldDB; O85044; -.
DR SMR; O85044; -.
DR STRING; 555778.Hneap_0917; -.
DR EnsemblBacteria; ACX95760; ACX95760; Hneap_0917.
DR KEGG; hna:Hneap_0917; -.
DR eggNOG; COG4576; Bacteria.
DR HOGENOM; CLU_148498_1_0_6; -.
DR OMA; RHACPDN; -.
DR OrthoDB; 1832681at2; -.
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; 2.40.50.220; -; 1.
DR InterPro; IPR014077; CsoS4B.
DR InterPro; IPR004992; EutN_CcmL.
DR InterPro; IPR036677; EutN_CcmL_sf.
DR Pfam; PF03319; EutN_CcmL; 1.
DR SUPFAM; SSF159133; SSF159133; 1.
DR TIGRFAMs; TIGR02704; carboxysome_B; 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..81
FT /note="Carboxysome shell vertex protein CsoS4B"
FT /id="PRO_0000452082"
FT DOMAIN 1..77
FT /note="BMV"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01280"
FT STRAND 2..9
FT /evidence="ECO:0007829|PDB:6JY5"
FT HELIX 17..19
FT /evidence="ECO:0007829|PDB:6JY5"
FT STRAND 24..29
FT /evidence="ECO:0007829|PDB:6JY5"
FT STRAND 34..38
FT /evidence="ECO:0007829|PDB:6JY5"
FT STRAND 48..53
FT /evidence="ECO:0007829|PDB:6JY5"
FT HELIX 54..59
FT /evidence="ECO:0007829|PDB:6JY5"
FT STRAND 60..64
FT /evidence="ECO:0007829|PDB:6JY5"
FT STRAND 69..75
FT /evidence="ECO:0007829|PDB:6JY5"
SQ SEQUENCE 81 AA; 8762 MW; B4D36F9D25ED999F CRC64;
MEVMRVRSDL IATRRIPGLK NISLRVMEDA TGKVSVACDP IGVPEGCWVF TISGSAARFG
VGDFEILTDL TIGGIIDHWV T
