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CSOS1_PROMM
ID   CSOS1_PROMM             Reviewed;         103 AA.
AC   Q7V6F7;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Carboxysome shell protein CsoS1 {ECO:0000305};
GN   Name=csoS1 {ECO:0000303|PubMed:25117559}; OrderedLocusNames=PMT_1206;
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] {ECO:0007744|PDB:4OX8}
RP   X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS), SUBUNIT, SUBCELLULAR LOCATION, AND
RP   DOMAIN.
RC   STRAIN=MIT 9313;
RX   PubMed=25117559; DOI=10.1021/sb500226j;
RA   Cai F., Sutter M., Bernstein S.L., Kinney J.N., Kerfeld C.A.;
RT   "Engineering bacterial microcompartment shells: chimeric shell proteins and
RT   chimeric carboxysome shells.";
RL   ACS Synth. Biol. 4:444-453(2015).
CC   -!- FUNCTION: One of the shell proteins of the carboxysome, a polyhedral
CC       inclusion where RuBisCO (ribulose bisphosphate carboxylase, ccbL-ccbS)
CC       is sequestered. Assembles into hexamers which make sheets that form the
CC       facets of the polyhedral carboxysome. {ECO:0000305|PubMed:25117559}.
CC   -!- SUBUNIT: Homohexamer with a small central pore (PubMed:25117559). Forms
CC       a CsoS2-CsoS1-RuBisCO complex (Probable). {ECO:0000269|PubMed:25117559,
CC       ECO:0000305|PubMed:25826651}.
CC   -!- SUBCELLULAR LOCATION: Carboxysome {ECO:0000305|PubMed:25117559}.
CC       Note=This cyanobacterium makes alpha-type carboxysomes, but upon
CC       expression in Synechococcus elongatus PCC 7942 this protein seems to be
CC       incorporated into beta-type carboxysomes.
CC       {ECO:0000269|PubMed:25117559}.
CC   -!- DOMAIN: The tight homohexamer forms a pore with an opening of about 5
CC       Angstroms in diameter. {ECO:0000269|PubMed:25117559}.
CC   -!- SIMILARITY: Belongs to the bacterial microcompartments protein family.
CC       CsoS1 subfamily. {ECO:0000305}.
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DR   EMBL; BX548175; CAE21381.1; -; Genomic_DNA.
DR   RefSeq; WP_011130577.1; NC_005071.1.
DR   PDB; 4OX8; X-ray; 1.90 A; A/B/C/D/E/F=1-103.
DR   PDBsum; 4OX8; -.
DR   AlphaFoldDB; Q7V6F7; -.
DR   SMR; Q7V6F7; -.
DR   STRING; 74547.PMT_1206; -.
DR   PRIDE; Q7V6F7; -.
DR   EnsemblBacteria; CAE21381; CAE21381; PMT_1206.
DR   KEGG; pmt:PMT_1206; -.
DR   eggNOG; COG4577; Bacteria.
DR   HOGENOM; CLU_064903_5_3_3; -.
DR   OMA; QFREGVN; -.
DR   OrthoDB; 1802372at2; -.
DR   Proteomes; UP000001423; Chromosome.
DR   GO; GO:0031470; C:carboxysome; IEA:UniProtKB-SubCell.
DR   GO; GO:0043886; F:structural constituent of carboxysome; IEA:UniProt.
DR   GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-KW.
DR   GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.70.1710; -; 1.
DR   InterPro; IPR020808; Bact_microcomp_CS.
DR   InterPro; IPR000249; BMC_dom.
DR   InterPro; IPR037233; CcmK-like_sf.
DR   InterPro; IPR044872; CcmK/CsoS1_BMC.
DR   Pfam; PF00936; BMC; 1.
DR   SMART; SM00877; BMC; 1.
DR   SUPFAM; SSF143414; SSF143414; 1.
DR   PROSITE; PS01139; BMC_1; 1.
DR   PROSITE; PS51930; BMC_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Bacterial microcompartment; Carbon dioxide fixation;
KW   Carboxysome; Photosynthesis; Reference proteome.
FT   CHAIN           1..103
FT                   /note="Carboxysome shell protein CsoS1"
FT                   /id="PRO_0000201500"
FT   DOMAIN          9..94
FT                   /note="BMC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01278"
FT   STRAND          9..17
FT                   /evidence="ECO:0007829|PDB:4OX8"
FT   HELIX           18..31
FT                   /evidence="ECO:0007829|PDB:4OX8"
FT   STRAND          35..43
FT                   /evidence="ECO:0007829|PDB:4OX8"
FT   STRAND          46..53
FT                   /evidence="ECO:0007829|PDB:4OX8"
FT   HELIX           55..69
FT                   /evidence="ECO:0007829|PDB:4OX8"
FT   STRAND          76..84
FT                   /evidence="ECO:0007829|PDB:4OX8"
FT   HELIX           87..93
FT                   /evidence="ECO:0007829|PDB:4OX8"
SQ   SEQUENCE   103 AA;  10557 MW;  B71DC633A1A9D406 CRC64;
     MASETMGIAL GMIETRGLVP AIEAADAMTK AAEVRLIGRE FVGGGYVTVL VRGETGAVNA
     AVRAGADACE RVGDGLVAAH IIARPHREVE PALGNGNFLG QKD
 
 
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