CSOS2_PROMM
ID CSOS2_PROMM Reviewed; 792 AA.
AC Q7V6G0;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 25-MAY-2022, entry version 73.
DE RecName: Full=Carboxysome assembly protein CsoS2 {ECO:0000303|PubMed:25826651};
DE AltName: Full=Carboxysome shell protein CsoS2;
GN Name=csoS2 {ECO:0000303|PubMed:25826651}; OrderedLocusNames=PMT_1203;
OS Prochlorococcus marinus (strain MIT 9313).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=74547;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 9313;
RX PubMed=12917642; DOI=10.1038/nature01947;
RA Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A.,
RA Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L.,
RA Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C.,
RA Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R.,
RA Chisholm S.W.;
RT "Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche
RT differentiation.";
RL Nature 424:1042-1047(2003).
RN [2]
RP FUNCTION, SUBUNIT, AND DOMAIN.
RC STRAIN=MIT 9313;
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 [3]
RP PUTATIVE 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).
CC -!- FUNCTION: Required for alpha-carboxysome (Cb) assembly, mediates
CC interaction between RuBisCO and the Cb shell. The protein is probably
CC intrinsically disordered (Probable). 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 (By similarity). {ECO:0000250|UniProtKB:O85041,
CC ECO:0000305|PubMed:25826651}.
CC -!- SUBUNIT: Probably interacts with the carboxysome major shell protein
CC CsoS1 via the N-terminal domain; this complex probably also interacts
CC with RuBisCO. {ECO:0000305|PubMed:25826651}.
CC -!- SUBCELLULAR LOCATION: Carboxysome {ECO:0000305}. Note=This bacterium
CC makes alpha-type carboxysomes. {ECO:0000269|PubMed:25826651}.
CC -!- DOMAIN: Has 3 domains; the N-terminal domain has 4 short repeats, the
CC central region has 6 longer repeats (Probable). The C-terminal domain
CC has 2 repeats and a highly conserved C-terminal peptide. The C-repeats
CC serve as the encapsulation signal for the alpha-carboxysome, and are
CC able to target foreign proteins to this organelle (By similarity).
CC {ECO:0000250|UniProtKB:O85041, ECO:0000305|PubMed:25826651}.
CC -!- PTM: Has been suggested to undergo ribosomal frameshifting, as does its
CC ortholog in H.neapolitanus. The exact position of the putative
CC frameshift is not given, but it would probably occur in the sixth M-
CC repeat and remove the C-terminus. {ECO:0000305|PubMed:26608811}.
CC -!- SIMILARITY: Belongs to the CsoS2 family. {ECO:0000305}.
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DR EMBL; BX548175; CAE21378.1; -; Genomic_DNA.
DR RefSeq; WP_011130574.1; NC_005071.1.
DR AlphaFoldDB; Q7V6G0; -.
DR STRING; 74547.PMT_1203; -.
DR EnsemblBacteria; CAE21378; CAE21378; PMT_1203.
DR KEGG; pmt:PMT_1203; -.
DR eggNOG; ENOG502Z8T4; Bacteria.
DR HOGENOM; CLU_016451_1_0_3; -.
DR OMA; DEPGTCK; -.
DR OrthoDB; 183361at2; -.
DR Proteomes; UP000001423; Chromosome.
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; 2.
PE 1: Evidence at protein level;
KW Bacterial microcompartment; Carbon dioxide fixation; Carboxysome;
KW Reference proteome; Repeat.
FT CHAIN 1..792
FT /note="Carboxysome assembly protein CsoS2"
FT /id="PRO_0000452069"
FT REPEAT 7..22
FT /note="N-repeat 1"
FT /evidence="ECO:0000269|PubMed:25826651"
FT REPEAT 94..109
FT /note="N-repeat 2"
FT /evidence="ECO:0000269|PubMed:25826651"
FT REPEAT 187..202
FT /note="N-repeat 3"
FT /evidence="ECO:0000269|PubMed:25826651"
FT REPEAT 225..240
FT /note="N-repeat 4"
FT /evidence="ECO:0000269|PubMed:25826651"
FT REPEAT 270..319
FT /note="M-repeat 1"
FT /evidence="ECO:0000269|PubMed:25826651"
FT REPEAT 330..379
FT /note="M-repeat 2"
FT /evidence="ECO:0000269|PubMed:25826651"
FT REPEAT 388..427
FT /note="M-repeat 3"
FT /evidence="ECO:0000269|PubMed:25826651"
FT REPEAT 441..490
FT /note="M-repeat 4"
FT /evidence="ECO:0000269|PubMed:25826651"
FT REPEAT 500..549
FT /note="M-repeat 5"
FT /evidence="ECO:0000269|PubMed:25826651"
FT REPEAT 560..609
FT /note="M-repeat 6"
FT /evidence="ECO:0000269|PubMed:25826651"
FT REPEAT 633..678
FT /note="C-repeat 1"
FT /evidence="ECO:0000269|PubMed:26608811"
FT REPEAT 703..738
FT /note="C-repeat 2"
FT /evidence="ECO:0000269|PubMed:26608811"
FT REGION 1..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1..235
FT /note="N-terminal domain"
FT /evidence="ECO:0000305|PubMed:25826651"
FT REGION 240..615
FT /note="Middle region"
FT /evidence="ECO:0000305|PubMed:25826651"
FT REGION 280..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 338..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 608..662
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 616..792
FT /note="C-terminal domain"
FT /evidence="ECO:0000305|PubMed:25826651"
FT REGION 687..792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 763..792
FT /note="C-terminal peptide (CTP)"
FT /evidence="ECO:0000305|PubMed:26608811"
FT COMPBIAS 1..19
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..126
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..217
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..240
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 614..662
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 695..717
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 765..785
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 792 AA; 83727 MW; A0D43E0014EA844D CRC64;
MAKQSSRELA LERRKALSNS GKKSTTLNGS SPNRIRTASD ARLTRTDQSF VKAGKESVQL
TAPKREQLDT SFVASRESSG ASRRQVKTIR NSSRELVLAR RDELSRRGQP AAKSKDRTRA
EVEKISSKVS QQDAAKKQVN DLASDQKGVD ESSSKSLKSL DTVSRLSSRN STSRPSAKRR
SIQNPSRALV LARREAQSKH GKTAANQPTS AASVARQGDP DLSSREISQR VRELRSKSGA
TGKKRSGACR PCGPNRNGSK QAVAADAHWK VGLSETSTGQ VVTGTQANRS SKTTGNEAST
CRSITGTQYL GSEVFDTFCQ SAPQPGQPLK VAVTNTSHGN RVTGNEVGRS EKVTGDEPGT
CKTLTGTEYI SANQANQYCG VSQPSPRKVG QSVTEDGRKV SGVMVGRSEK VTGDEAGSNR
QLTGDQYLGV DPLPEGRSAE KVGSFNTLRG AGVTGTNVAR SEYVTGNEPG SCKRVTGDEY
VGPQQYNTFC GGKPNPEAAK VGLSLTNKSQ TVSGTLTGRS ELVTGDEPGT CKAVTGTPYS
GVEQASGWCD TNSVREIQDR TPKLLGTPGA VMTGLQPGVG GVMTGAEKGA CEPLTGTPYV
GGDQLVQACG SDAPAGSNDH QGSSESSPWT HFSVQSPARA MQLQRDPRSG VTGTSYEQGS
QITGPFNMAV DKITGTEQFR FDRKQRHFKS VPVEATPNDV SQTRPESRVT GEGQSAGLNI
TGDDWDRSER VTGTEGASAR RRNPTRPGPM SAMPAADLKR NEEVSQPMSR VTGSSGNTDQ
GSLITVSGGA RG
