CSOS2_HYDCU
ID CSOS2_HYDCU Reviewed; 662 AA.
AC Q31HD7;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 25-MAY-2022, entry version 63.
DE RecName: Full=Carboxysome assembly protein CsoS2;
DE AltName: Full=Carboxysome shell protein CsoS2 {ECO:0000303|PubMed:28115547};
GN Name=csoS2 {ECO:0000303|PubMed:28115547}; OrderedLocusNames=Tcr_0840;
OS Hydrogenovibrio crunogenus (strain DSM 25203 / XCL-2) (Thiomicrospira
OS crunogena).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC Piscirickettsiaceae; Hydrogenovibrio.
OX NCBI_TaxID=317025;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25203 / XCL-2;
RX PubMed=17105352; DOI=10.1371/journal.pbio.0040383;
RA Scott K.M., Sievert S.M., Abril F.N., Ball L.A., Barrett C.J., Blake R.A.,
RA Boller A.J., Chain P.S.G., Clark J.A., Davis C.R., Detter C., Do K.F.,
RA Dobrinski K.P., Faza B.I., Fitzpatrick K.A., Freyermuth S.K., Harmer T.L.,
RA Hauser L.J., Huegler M., Kerfeld C.A., Klotz M.G., Kong W.W., Land M.,
RA Lapidus A., Larimer F.W., Longo D.L., Lucas S., Malfatti S.A., Massey S.E.,
RA Martin D.D., McCuddin Z., Meyer F., Moore J.L., Ocampo L.H. Jr., Paul J.H.,
RA Paulsen I.T., Reep D.K., Ren Q., Ross R.L., Sato P.Y., Thomas P.,
RA Tinkham L.E., Zeruth G.T.;
RT "The genome of deep-sea vent chemolithoautotroph Thiomicrospira crunogena
RT XCL-2.";
RL PLoS Biol. 4:1-17(2006).
RN [2]
RP PROBABLY NO RIBOSOMAL FRAMESHIFT.
RX PubMed=26608811; DOI=10.1016/j.jmb.2015.11.017;
RA Chaijarasphong T., Nichols R.J., Kortright K.E., Nixon C.F., Teng P.K.,
RA Oltrogge L.M., Savage D.F.;
RT "Programmed Ribosomal Frameshifting Mediates Expression of the alpha-
RT Carboxysome.";
RL J. Mol. Biol. 428:153-164(2016).
RN [3]
RP SUBCELLULAR LOCATION, AND INDUCTION.
RC STRAIN=DSM 25203 / XCL-2;
RX PubMed=28115547; DOI=10.1128/jb.00871-16;
RG USF MCB4404L;
RA Mangiapia M., Brown T.W., Chaput D., Haller E., Harmer T.L., Hashemy Z.,
RA Keeley R., Leonard J., Mancera P., Nicholson D., Stevens S., Wanjugi P.,
RA Zabinski T., Pan C., Scott K.M.;
RT "Proteomic and Mutant Analysis of the CO2 Concentrating Mechanism of
RT Hydrothermal Vent Chemolithoautotroph Thiomicrospira crunogena.";
RL J. Bacteriol. 199:0-0(2017).
CC -!- FUNCTION: Required for alpha-carboxysome (Cb) assembly, mediates
CC interaction between RuBisCO and the Cb shell. The protein is probably
CC intrinsically disordered. The C-terminal repeats act as the
CC encapsulation signal to target proteins to the Cb; they are necessary
CC and sufficient to target both CsoS2 and foreign proteins to the Cb. The
CC N-terminal repeats of this protein bind simultaneously to both subunits
CC of RuBisCO. Probably also interacts with the major shell proteins
CC (CsoS1); that interaction would increase the local concentration of
CC CsoS2 so that it can condense RuBisCO and full carboxysomes can be
CC formed. {ECO:0000250|UniProtKB:O85041}.
CC -!- SUBUNIT: Interacts via its N-terminal repeats with RuBisCO. Interacts
CC with the major shell protein CsoS1. {ECO:0000250|UniProtKB:O85041}.
CC -!- SUBCELLULAR LOCATION: Carboxysome {ECO:0000305|PubMed:28115547}.
CC Note=This bacterium makes alpha-type carboxysomes. {ECO:0000305}.
CC -!- INDUCTION: Induced by growth in low levels of dissolved inorganic
CC carbon (at protein level). {ECO:0000269|PubMed:28115547}.
CC -!- DOMAIN: Has 3 domains; the N-terminal domain has 3 short repeats and
CC binds RuBisCO. The central region has 5 longer repeats. The C-terminal
CC domain has 1 repeat (compared to orthologs) and a highly conserved C-
CC terminal peptide. The C-repeat serves as the encapsulation signal for
CC the alpha-carboxysome, and is able to target foreign proteins to this
CC organelle. {ECO:0000250|UniProtKB:O85041}.
CC -!- PTM: Unlike H.neapolitanus and predictions for P.marinus strain MIT
CC 9313, this protein is not thought to have ribosomal frameshifting.
CC {ECO:0000305|PubMed:26608811}.
CC -!- SIMILARITY: Belongs to the CsoS2 family. {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; CP000109; ABB41436.1; -; Genomic_DNA.
DR RefSeq; WP_011370263.1; NC_007520.2.
DR AlphaFoldDB; Q31HD7; -.
DR STRING; 317025.Tcr_0840; -.
DR EnsemblBacteria; ABB41436; ABB41436; Tcr_0840.
DR KEGG; tcx:Tcr_0840; -.
DR eggNOG; ENOG502Z8T4; Bacteria.
DR HOGENOM; CLU_016451_0_0_6; -.
DR OMA; DEPGTCK; -.
DR OrthoDB; 183361at2; -.
DR GO; GO:0031470; C:carboxysome; IEA:UniProtKB-SubCell.
DR GO; GO:0043886; F:structural constituent of carboxysome; IEA:InterPro.
DR GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-KW.
DR InterPro; IPR020990; CSOS2.
DR Pfam; PF12288; CsoS2_M; 1.
PE 1: Evidence at protein level;
KW Bacterial microcompartment; Carbon dioxide fixation; Carboxysome; Repeat.
FT CHAIN 1..662
FT /note="Carboxysome assembly protein CsoS2"
FT /id="PRO_0000452068"
FT REPEAT 8..27
FT /note="N-repeat 1"
FT /evidence="ECO:0000250|UniProtKB:O85041"
FT REPEAT 58..72
FT /note="N-repeat 2"
FT /evidence="ECO:0000250|UniProtKB:O85041"
FT REPEAT 147..168
FT /note="N-repeat 3"
FT /evidence="ECO:0000250|UniProtKB:O85041"
FT REPEAT 228..278
FT /note="M-repeat 1"
FT /evidence="ECO:0000250|UniProtKB:O85041"
FT REPEAT 288..338
FT /note="M-repeat 2"
FT /evidence="ECO:0000250|UniProtKB:O85041"
FT REPEAT 388..436
FT /note="M-repeat 3"
FT /evidence="ECO:0000250|UniProtKB:O85041"
FT REPEAT 446..491
FT /note="M-repeat 4"
FT /evidence="ECO:0000250|UniProtKB:O85041"
FT REPEAT 496..550
FT /note="M-repeat 5"
FT /evidence="ECO:0000250|UniProtKB:O85041"
FT REPEAT 564..572
FT /note="C-repeat 1"
FT /evidence="ECO:0000250|UniProtKB:O85041"
FT REGION 1..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1..227
FT /note="N-terminal domain"
FT /evidence="ECO:0000250|UniProtKB:O85041"
FT REGION 228..559
FT /note="Middle region"
FT /evidence="ECO:0000250|UniProtKB:O85041"
FT REGION 277..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 342..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 560..631
FT /note="C-terminal domain"
FT /evidence="ECO:0000250|UniProtKB:O85041"
FT REGION 588..607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 619..662
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 632..662
FT /note="C-terminal peptide"
FT /evidence="ECO:0000250|UniProtKB:O85041"
FT COMPBIAS 106..136
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..152
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..251
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 278..322
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..408
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 626..654
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 662 AA; 68177 MW; 49E6C9F5EF30864D CRC64;
MSTSNAQSGR AAAIARRNAQ VKGKGYTASA APAAPRKPAA PVAEPVVAAA PAPSQPSRSR
RKVSVAPTAT PAASAAGREA AKLKRQQQKN GKSSAGAANA MPHPKAKAKQ KPEEPIVEPR
QAKAEKPTKR SERRTGVKPQ VASQQPSGRL QSKAYRKAQA KGKAGQEAFK SNGSSQSGAK
AKLANPDAST REIAQQVRAE RCAQGKTCST GGSRPMRKRR NAKEAPQKVG ESQTLHGQSV
SGTQVGQGEK KMTGSESGAC QLVSGTEYLG AEEFSKNCDV QPTPQPAKVT QTQTTRGQVV
SGSTKVGRSD KMTGNETGTC SAITGTEYLP ADQSKMYCGE TPAKSKATGF SVMSQATQKS
EQKVTGGDSR KSQSTTFKPK NPASAPHKVM PSQTAKGNTT TGSQVGRLES VTGGERGSCH
AVTGTGYQGA EEAKACDMPM TETADKVTAS GTAGGQKVTG DRSGAYYGMT GAEAGDCKTI
TGTSYTGTEQ FQFCSVDEQN EMKVRQRKGA NPSISGVQPG PQGLTGAQKG ACELVTGSHY
QGGDQTAMVC DSTNAAAPGE SDFPAMIGQA QPAFSTNEVE PMVDEGSKIT GDGWDRGSKV
TGTDGPWAAQ RNASIRGVAG QSPMGASQYR PVNNEVPMSP ITGSSGNTDT GAKVTLSGGA
RA
