CSOS2_PARMW
ID CSOS2_PARMW Reviewed; 780 AA.
AC Q7U5I9;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Carboxysome assembly protein CsoS2 {ECO:0000305};
DE AltName: Full=Carboxysome shell protein CsoS2;
GN Name=csoS2 {ECO:0000303|PubMed:31507578}; OrderedLocusNames=SYNW1716;
OS Parasynechococcus marenigrum (strain WH8102).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Parasynechococcus; Parasynechococcus marenigrum.
OX NCBI_TaxID=84588;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WH8102;
RX PubMed=12917641; DOI=10.1038/nature01943;
RA Palenik B., Brahamsha B., Larimer F.W., Land M.L., Hauser L., Chain P.,
RA Lamerdin J.E., Regala W., Allen E.E., McCarren J., Paulsen I.T.,
RA Dufresne A., Partensky F., Webb E.A., Waterbury J.;
RT "The genome of a motile marine Synechococcus.";
RL Nature 424:1037-1042(2003).
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 IDENTIFICATION BY MASS SPECTROMETRY, AND INDUCTION.
RC STRAIN=WH8102;
RX PubMed=31507578; DOI=10.3389/fmicb.2019.01976;
RA Li Y.Y., Chen X.H., Xue C., Zhang H., Sun G., Xie Z.X., Lin L., Wang D.Z.;
RT "Proteomic Response to Rising Temperature in the Marine Cyanobacterium
RT Synechococcus Grown in Different Nitrogen Sources.";
RL Front. Microbiol. 10:1976-1976(2019).
CC -!- FUNCTION: Required for alpha-carboxysome (Cb) assembly, mediates
CC interaction between RuBisCO and the carboxysome shell. The protein is
CC probably 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 -!- INDUCTION: Down-regulated with rising temperature (from 25 to 28
CC degrees Celsius) in both nitrate- and urea-grown cells (at protein
CC level). {ECO:0000269|PubMed:31507578}.
CC -!- DOMAIN: Has 3 domains; the N-terminal domain has 4 short repeats and
CC binds RuBisCO. The central region has 6 longer repeats. The C-terminal
CC domain has 2 repeats and a highly conserved C-terminal peptide. The C-
CC repeats serve as the encapsulation signal for the alpha-carboxysome,
CC and are able to target foreign proteins to this organelle.
CC {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}.
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DR EMBL; BX569693; CAE08231.1; -; Genomic_DNA.
DR RefSeq; WP_011128578.1; NC_005070.1.
DR AlphaFoldDB; Q7U5I9; -.
DR STRING; 84588.SYNW1716; -.
DR EnsemblBacteria; CAE08231; CAE08231; SYNW1716.
DR KEGG; syw:SYNW1716; -.
DR eggNOG; ENOG502Z8T4; Bacteria.
DR HOGENOM; CLU_016451_1_0_3; -.
DR OMA; DEPGTCK; -.
DR OrthoDB; 183361at2; -.
DR Proteomes; UP000001422; Chromosome.
DR GO; GO:0043886; F:structural constituent of carboxysome; IEA:InterPro.
DR InterPro; IPR020990; CSOS2.
DR Pfam; PF12288; CsoS2_M; 2.
PE 1: Evidence at protein level;
KW Repeat.
FT CHAIN 1..780
FT /note="Carboxysome assembly protein CsoS2"
FT /id="PRO_0000452071"
FT REPEAT 5..24
FT /note="N-repeat 1"
FT /evidence="ECO:0000250|UniProtKB:O85041"
FT REPEAT 86..105
FT /note="N-repeat 2"
FT /evidence="ECO:0000250|UniProtKB:O85041"
FT REPEAT 175..194
FT /note="N-repeat 3"
FT /evidence="ECO:0000250|UniProtKB:O85041"
FT REPEAT 213..235
FT /note="N-repeat 4"
FT /evidence="ECO:0000250|UniProtKB:O85041"
FT REPEAT 260..309
FT /note="M-repeat 1"
FT /evidence="ECO:0000250|UniProtKB:O85041"
FT REPEAT 320..369
FT /note="M-repeat 2"
FT /evidence="ECO:0000250|UniProtKB:O85041"
FT REPEAT 378..417
FT /note="M-repeat 3"
FT /evidence="ECO:0000250|UniProtKB:O85041"
FT REPEAT 431..480
FT /note="M-repeat 4"
FT /evidence="ECO:0000250|UniProtKB:O85041"
FT REPEAT 490..535
FT /note="M-repeat 5"
FT /evidence="ECO:0000250|UniProtKB:O85041"
FT REPEAT 541..599
FT /note="M-repeat 6"
FT /evidence="ECO:0000250|UniProtKB:O85041"
FT REPEAT 623..669
FT /note="C-repeat 1"
FT /evidence="ECO:0000250|UniProtKB:O85041"
FT REPEAT 693..726
FT /note="C-repeat 2"
FT /evidence="ECO:0000250|UniProtKB:O85041"
FT REGION 1..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 189..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 226..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 260..608
FT /note="Middle region"
FT /evidence="ECO:0000250|UniProtKB:O85041"
FT REGION 330..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 382..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 609..749
FT /note="C-terminal domain"
FT /evidence="ECO:0000250|UniProtKB:O85041"
FT REGION 631..661
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 686..780
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 750..780
FT /note="C-terminal peptide"
FT /evidence="ECO:0000250|UniProtKB:O85041"
FT COMPBIAS 1..19
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..81
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..116
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..281
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..398
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 631..651
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 708..724
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 755..772
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 780 AA; 81029 MW; F0525F01C1630260 CRC64;
MARLSSRELA LERRKALTTS GKKSSVAAGD GANRVRTASD VRPTRTDAAA AVEPTAPAVS
APVKPTVSFT PASPSSSSHV KPQRHPSRDL VLARRDALSR RGKTADTSRD RNRADVARQT
QAAAPVAASA EEQKTCGCGG KRAAGKVQLS APTTSLKPRS DRRSAAPKRR AIENPSRALV
LARREAMAKH GKTAGKQPTS AAAVARQANP DLTSRELAQQ VRELRTKAGA RNKQSAGATR
PTGPNRHGAK QAAAADAHWK VGESTTSTGQ TVTGTQANRS VKTTGNEAST CRSITGTEYL
GAEVFQTFCQ QAPEPTTPAK VRVTATSHGN RVTGNEVGRS EKVTGDEPGT CKSVTGTEYI
SANQSAAYCG SSQVSQRKVG HSLTQQGRPV SGVMVGRSSS VTGDEAGAGR SLTGDQYLGS
DPLPDGRPAA KVGQSGTLSG TGVTGTLVGR SSQVTGNEFG SCHRVTGDQY ISAEQVNAFC
GSKPEPEAAK VGFSITNRNQ VVSGTRTGRS ERVTGDEPGT CKAVTGTPYA GLENAGQHCG
TSAVQAIRER TPVRLGTPSA AMTGIQPGVG GVMTGDEKGA CEAVTGTPYV GADQLATACG
NEAPAGTDSH GQAPEGAAWT RFSVMSPARA AQQQRDDQGA VTGTSYEQGN RITGPFDLAG
GKVTGTEQFR FDNREFQRRQ FQPTVAVVSE PAEQPASRVT GEGSSTKITG DDWDRGEHVT
GTEGVSARRR NPTRPGPMSA TVPHERKRNE ENEWPVSRVT GSSGNTEKGS LITVSGGARG
