CSOS2_PROMP
ID CSOS2_PROMP Reviewed; 765 AA.
AC Q7V2C8;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 25-MAY-2022, entry version 72.
DE RecName: Full=Carboxysome assembly protein CsoS2 {ECO:0000305};
DE AltName: Full=Carboxysome shell protein CsoS2 {ECO:0000303|PubMed:22155772};
GN Name=csoS2 {ECO:0000303|PubMed:22155772}; OrderedLocusNames=PMM0552;
OS Prochlorococcus marinus subsp. pastoris (strain CCMP1986 / NIES-2087 /
OS MED4).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=59919;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP1986 / NIES-2087 / MED4;
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 PROTEIN ABUNDANCE, AND SUBCELLULAR LOCATION.
RC STRAIN=CCMP1986 / NIES-2087 / MED4;
RX PubMed=22155772; DOI=10.1128/jb.06444-11;
RA Roberts E.W., Cai F., Kerfeld C.A., Cannon G.C., Heinhorst S.;
RT "Isolation and characterization of the Prochlorococcus carboxysome reveal
RT the presence of the novel shell protein CsoS1D.";
RL J. Bacteriol. 194:787-795(2012).
RN [3]
RP FUNCTION, SUBUNIT, AND DOMAIN.
RC STRAIN=CCMP1986 / NIES-2087 / MED4;
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 [4]
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).
CC -!- FUNCTION: Required for alpha-carboxysome (Cb) assembly, mediates
CC interaction between RuBisCO and the Cb shell. The protein is probably
CC highly flexible (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). There are estimated to be 163 CsoS2 proteins
CC per carboxysome; unlike H.neapolitanus only 1 form is seen
CC (PubMed:22155772). {ECO:0000250|UniProtKB:O85041,
CC ECO:0000269|PubMed:22155772, ECO:0000305|PubMed:25826651}.
CC -!- SUBUNIT: Probably interacts with the carboxysome major shell protein
CC CsoS1 via the N-terminal domain (Probable). A CsoS1-CsoS1D-CsoS2
CC complex can be isolated following expression in E.coli
CC (PubMed:25826651). Interacts via its N-terminal repeats with RuBisCO
CC (By similarity). {ECO:0000250|UniProtKB:O85041,
CC ECO:0000269|PubMed:25826651, ECO:0000305|PubMed:25826651}.
CC -!- SUBCELLULAR LOCATION: Carboxysome {ECO:0000269|PubMed:22155772}.
CC Note=This bacterium makes alpha-type carboxysomes.
CC {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: Unlike H.neapolitanus and predictions for P.marinus strain MIT
CC 9313, this protein is not thought to have ribosomal frameshifting.
CC {ECO:0000305, ECO:0000305|PubMed:26608811}.
CC -!- SIMILARITY: Belongs to the CsoS2 family. {ECO:0000305}.
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DR EMBL; BX548174; CAE19011.1; -; Genomic_DNA.
DR RefSeq; WP_011132186.1; NC_005072.1.
DR AlphaFoldDB; Q7V2C8; -.
DR STRING; 59919.PMM0552; -.
DR EnsemblBacteria; CAE19011; CAE19011; PMM0552.
DR KEGG; pmm:PMM0552; -.
DR eggNOG; ENOG502Z8T4; Bacteria.
DR HOGENOM; CLU_016451_1_0_3; -.
DR OMA; DEPGTCK; -.
DR OrthoDB; 183361at2; -.
DR Proteomes; UP000001026; 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 GO; GO:0015979; P:photosynthesis; 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;
KW Photosynthesis; Repeat.
FT CHAIN 1..765
FT /note="Carboxysome assembly protein CsoS2"
FT /id="PRO_0000452070"
FT REPEAT 7..22
FT /note="N-repeat 1"
FT /evidence="ECO:0000269|PubMed:25826651"
FT REPEAT 79..94
FT /note="N-repeat 2"
FT /evidence="ECO:0000269|PubMed:25826651"
FT REPEAT 158..173
FT /note="N-repeat 3"
FT /evidence="ECO:0000269|PubMed:25826651"
FT REPEAT 196..211
FT /note="N-repeat 4"
FT /evidence="ECO:0000269|PubMed:25826651"
FT REPEAT 240..289
FT /note="M-repeat 1"
FT /evidence="ECO:0000269|PubMed:25826651"
FT REPEAT 300..349
FT /note="M-repeat 2"
FT /evidence="ECO:0000269|PubMed:25826651"
FT REPEAT 358..397
FT /note="M-repeat 3"
FT /evidence="ECO:0000269|PubMed:25826651"
FT REPEAT 411..460
FT /note="M-repeat 4"
FT /evidence="ECO:0000269|PubMed:25826651"
FT REPEAT 470..519
FT /note="M-repeat 5"
FT /evidence="ECO:0000269|PubMed:25826651"
FT REPEAT 530..580
FT /note="M-repeat 6"
FT /evidence="ECO:0000269|PubMed:25826651"
FT REPEAT 604..648
FT /note="C-repeat 1"
FT /evidence="ECO:0000250|UniProtKB:O85041"
FT REPEAT 677..711
FT /note="C-repeat 2"
FT /evidence="ECO:0000250|UniProtKB:O85041"
FT REGION 1..215
FT /note="N-terminal domain"
FT /evidence="ECO:0000305|PubMed:25826651"
FT REGION 1..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 165..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 216..586
FT /note="Middle region"
FT /evidence="ECO:0000305|PubMed:25826651"
FT REGION 306..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 367..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 589..734
FT /note="C-terminal domain"
FT /evidence="ECO:0000305|PubMed:25826651"
FT REGION 611..637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 656..765
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 735..765
FT /note="C-terminal peptide"
FT /evidence="ECO:0000250|UniProtKB:O85041"
FT COMPBIAS 1..34
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..78
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..208
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..398
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 611..629
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 657..683
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 741..757
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 765 AA; 81882 MW; E3007FE45C462C42 CRC64;
MSTKTSREIA LERRKAMSDG GKKAALHSSS TKDRVRSSQD INSTGATSSN KKVLTSPSKS
NIPANKIARK STSSKLSSKE LGIERRKAMS THGKSAINSS DRTRTDVKSD IKVNKVISTE
KPQALKDHNN NIKDNQVVKQ NIKRRINQKR KPITNTSRDI VLARREAQSK HGKSASKQNT
SAASLARRGD PDLSSREISQ RVRELRSKTG STSKQGNGKC RPCGPNKNGS KLNIADASWK
VGKSETDSGQ TVTGTQANRS LKTTGNEAST CRTVTGTQYM GAEVTGQFCQ DKPKYKQPIR
ASVTTTTSGN KVTGNEVGRS EKVTGDEPGT CKNLTGTEYI SANQSKKYCG EVIKKPSKVM
QSITTDGLKV SGSLPGRSSL VTGDESGSGK QLTGDQYLGS EPSPKGKSFE KVGSYDTLNG
NNVTGTGVGR SDYVTGNEYG SCKNLTGDEY IGSQQYEKFC GSTPKPEARK VGLSLSSKSN
LISGTMTGRS KIVTGDEPGS CKVLTGTPYA GLDQINDNCN AEIADDMKSR ATVNSGNNSN
ARLTGLQPGI GGVMTGATKG SCKNLTGTPY IGGDQFLSNC ETPPNDASYA NQEKSASNSW
KEFSVNSPSR EKYSAKNTEG VTGNRYEDSS KITGPFDMAE DKVTGTEQFR FEPNKNMTYK
QKMKQEESQN IDIPTDKKEP SKITGEGQSA GNITGDDWDR GDKVTGTEGV SARKRNPSRA
GFMGAMPPVD NKRNDETEKP DFLITGSSGN TRDGQLVTFS GGARG
