ID   RBL1_HALNC              Reviewed;         473 AA.
AC   O85040; D0KZ92;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   27-MAR-2024, entry version 122.
DE   RecName: Full=Ribulose bisphosphate carboxylase large chain {ECO:0000255|HAMAP-Rule:MF_01338};
DE            Short=RuBisCO large subunit {ECO:0000255|HAMAP-Rule:MF_01338};
DE            EC=4.1.1.39 {ECO:0000255|HAMAP-Rule:MF_01338, ECO:0000269|PubMed:18258595};
DE   AltName: Full=Form 1 RuBisCO {ECO:0000303|PubMed:9696760};
GN   Name=cbbL {ECO:0000255|HAMAP-Rule:MF_01338,
GN   ECO:0000303|PubMed:9696760}; OrderedLocusNames=Hneap_0922;
OS   Halothiobacillus neapolitanus (strain ATCC 23641 / c2) (Thiobacillus
OS   neapolitanus).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC   Halothiobacillaceae; Halothiobacillus.
OX   NCBI_TaxID=555778;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 23641 / c2;
RX   PubMed=9696760; DOI=10.1128/jb.180.16.4133-4139.1998;
RA   Baker S.H., Jin S., Aldrich H.C., Howard G.T., Shively J.M.;
RT   "Insertion mutation of the form I cbbL gene encoding ribulose bisphosphate
RT   carboxylase/oxygenase (RuBisCO) in Thiobacillus neapolitanus results in
RT   expression of form II RuBisCO, loss of carboxysomes, and an increased CO2
RT   requirement for growth.";
RL   J. Bacteriol. 180:4133-4139(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23641 / c2;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Davenport K., Brettin T., Detter J.C., Han C.,
RA   Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Kerfeld C., Cannon G., Heinhort S.;
RT   "Complete sequence of Halothiobacillus neapolitanus c2.";
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX   DOI=10.1007/BF00429407;
RA   Cannon G.C., Shively J.M.;
RT   "Characterization of a Homogenous Preparation of Carboxysomes from
RT   Thiobacillus neapolitanus.";
RL   Arch. Microbiol. 134:52-59(1983).
RN   [4]
RP   SUBCELLULAR LOCATION.
RX   PubMed=16535117; DOI=10.1128/aem.61.9.3256-3260.1995;
RA   English R.S., Jin S., Shively J.M.;
RT   "Use of Electroporation To Generate a Thiobacillus neapolitanus Carboxysome
RT   Mutant.";
RL   Appl. Environ. Microbiol. 61:3256-3260(1995).
RN   [5]
RP   SUBCELLULAR LOCATION.
RX   PubMed=14729686; DOI=10.1128/jb.186.3.623-630.2004;
RA   So A.K., Espie G.S., Williams E.B., Shively J.M., Heinhorst S.,
RA   Cannon G.C.;
RT   "A novel evolutionary lineage of carbonic anhydrase (epsilon class) is a
RT   component of the carboxysome shell.";
RL   J. Bacteriol. 186:623-630(2004).
RN   [6]
RP   PROTEIN ABUNDANCE, AND SUBCELLULAR LOCATION.
RX   DOI=10.1007/7171_023;
RA   Heinhorst S., Cannon G.C., Shively J.M.;
RT   "Carboxysomes and Carboxysome-like Inclusions.";
RL   (In) Shively J.M. (eds.);
RL   Microbiology Monographs, pp.2:141-164, Springer-Verlag, Berlin (2006).
RN   [7]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP   SUBCELLULAR LOCATION.
RC   STRAIN=ATCC 23641 / c2;
RX   PubMed=18258595; DOI=10.1074/jbc.m709285200;
RA   Dou Z., Heinhorst S., Williams E.B., Murin C.D., Shively J.M., Cannon G.C.;
RT   "CO2 fixation kinetics of Halothiobacillus neapolitanus mutant carboxysomes
RT   lacking carbonic anhydrase suggest the shell acts as a diffusional barrier
RT   for CO2.";
RL   J. Biol. Chem. 283:10377-10384(2008).
RN   [8]
RP   FUNCTION, SUBCELLULAR LOCATION, CARBOXYSOME ASSEMBLY PROCESS, REQUIRED FOR
RP   CARBOXYSOMAL TARGETING, DISRUPTION PHENOTYPE, AND BIOTECHNOLOGY.
RC   STRAIN=ATCC 23641 / c2;
RX   PubMed=18974784; DOI=10.1371/journal.pone.0003570;
RA   Menon B.B., Dou Z., Heinhorst S., Shively J.M., Cannon G.C.;
RT   "Halothiobacillus neapolitanus carboxysomes sequester heterologous and
RT   chimeric RubisCO species.";
RL   PLoS ONE 3:e3570-e3570(2008).
RN   [9]
RP   BIOTECHNOLOGY.
RC   STRAIN=ATCC 23641 / c2;
RX   PubMed=22184212; DOI=10.1073/pnas.1108557109;
RA   Bonacci W., Teng P.K., Afonso B., Niederholtmeyer H., Grob P., Silver P.A.,
RA   Savage D.F.;
RT   "Modularity of a carbon-fixing protein organelle.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:478-483(2012).
RN   [10]
RP   SUBUNIT.
RC   STRAIN=ATCC 23641 / c2;
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   [11]
RP   BIOTECHNOLOGY.
RX   PubMed=29922315; DOI=10.3389/fpls.2018.00739;
RA   Fang Y., Huang F., Faulkner M., Jiang Q., Dykes G.F., Yang M., Liu L.N.;
RT   "Engineering and Modulating Functional Cyanobacterial CO2-Fixing
RT   Organelles.";
RL   Front. Plant Sci. 9:739-739(2018).
RN   [12]
RP   INTERACTION WITH CSOS1A; CSOS1B AND CSOS1C, DOMAIN, AND BIOTECHNOLOGY.
RC   STRAIN=ATCC 23641 / c2;
RX   PubMed=30305640; DOI=10.1038/s41598-018-33074-x;
RA   Liu Y., He X., Lim W., Mueller J., Lawrie J., Kramer L., Guo J., Niu W.;
RT   "Deciphering molecular details in the assembly of alpha-type carboxysome.";
RL   Sci. Rep. 8:15062-15062(2018).
RN   [13]
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 23641 / c2;
RX   PubMed=31406332; DOI=10.1038/s41564-019-0520-8;
RA   Desmarais J.J., Flamholz A.I., Blikstad C., Dugan E.J., Laughlin T.G.,
RA   Oltrogge L.M., Chen A.W., Wetmore K., Diamond S., Wang J.Y., Savage D.F.;
RT   "DABs are inorganic carbon pumps found throughout prokaryotic phyla.";
RL   Nat. Microbiol. 4:2204-2215(2019).
RN   [14] {ECO:0007744|PDB:1SVD}
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RA   Kerfeld C.A., Sawaya M.R., Pashkov I., Cannon G., Williams E., Tran K.,
RA   Yeates T.O.;
RT   "The structure of Halothiobacillus neapolitanus Rubisco.";
RL   Submitted (APR-2005) to the PDB data bank.
RN   [15] {ECO:0007744|PDB:6UEW}
RP   X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF HOLOENZYME, INTERACTION WITH
RP   CSOS2, AND MUTAGENESIS OF TYR-72 AND PHE-346.
RX   PubMed=32123388; DOI=10.1038/s41594-020-0387-7;
RA   Oltrogge L.M., Chaijarasphong T., Chen A.W., Bolin E.R., Marqusee S.,
RA   Savage D.F.;
RT   "Multivalent interactions between CsoS2 and Rubisco mediate alpha-
RT   carboxysome formation.";
RL   Nat. Struct. Mol. Biol. 27:281-287(2020).
CC   -!- FUNCTION: RuBisCO catalyzes two reactions: the carboxylation of D-
CC       ribulose 1,5-bisphosphate, the primary event in carbon dioxide
CC       fixation, as well as the oxidative fragmentation of the pentose
CC       substrate. Both reactions occur simultaneously and in competition at
CC       the same active site (By similarity) (Ref.3, PubMed:18258595,
CC       PubMed:18974784). There are estimated to be 270 RuBisCO
CC       heterohexadecamers per carboxysome (Ref.6). {ECO:0000255|HAMAP-
CC       Rule:MF_01338, ECO:0000269|PubMed:18258595,
CC       ECO:0000269|PubMed:18974784, ECO:0000269|Ref.3, ECO:0000269|Ref.6}.
CC   -!- FUNCTION: Alpha-carboxysomes are able to assemble in the absence of
CC       RuBisCO, unlike beta-carboxysomes. The RuBisCO large subunit is
CC       required for enzyme integration into carboxysomes; replacing it with
CC       the carboxysomally targeted gene (Tcr_0838, AC Q31HD9) of H.crungenus
CC       places RuBisCO in the carboxysome, while the non-carboxysomal large
CC       subunit of H.crungenus (Tcr_0427, AC Q31IK0) is not incorporated in the
CC       carboxysome. {ECO:0000269|PubMed:18974784}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 (2R)-3-phosphoglycerate + 2 H(+) = CO2 + D-ribulose 1,5-
CC         bisphosphate + H2O; Xref=Rhea:RHEA:23124, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57870,
CC         ChEBI:CHEBI:58272; EC=4.1.1.39; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01338, ECO:0000269|PubMed:18258595,
CC         ECO:0000269|PubMed:18974784, ECO:0000269|Ref.3};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-ribulose 1,5-bisphosphate + O2 = (2R)-3-phosphoglycerate +
CC         2-phosphoglycolate + 2 H(+); Xref=Rhea:RHEA:36631, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:57870, ChEBI:CHEBI:58033,
CC         ChEBI:CHEBI:58272; Evidence={ECO:0000255|HAMAP-Rule:MF_01338,
CC         ECO:0000269|Ref.3};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01338};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01338};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=163.7 uM for CO(2);
CC         Vmax=2.9 umol/min/mg enzyme {ECO:0000269|PubMed:18258595};
CC         Note=For enzyme freed from the carboxysome.
CC         {ECO:0000269|PubMed:18258595};
CC   -!- SUBUNIT: Heterohexadecamer of 8 large chains and 8 small chains (By
CC       similarity) (Ref.14). Forms a CsoS2-CsoS1-RuBisCO complex (Probable).
CC       The N-terminus (residues 1-136) interacts with shell proteins CsoS1A,
CC       CsoS1B and CsoS1C (PubMed:30305640). Holo-RuBisCO interacts with the N-
CC       terminal repeats of CsoS2; binding is sensitive to ionic strength. A
CC       fusion of a single N-terminal repeat to the C-terminus of the large
CC       subunit of RuBisCO (cbbL) shows the repeat can lie between a CbbL
CC       dimer, making minor contacts to CbbS; thus each RuBisCO holoenzyme
CC       could bind 8 repeats (PubMed:32123388). {ECO:0000255|HAMAP-
CC       Rule:MF_01338, ECO:0000269|PubMed:30305640,
CC       ECO:0000269|PubMed:32123388, ECO:0000269|Ref.14,
CC       ECO:0000305|PubMed:25826651}.
CC   -!- SUBCELLULAR LOCATION: Carboxysome {ECO:0000269|PubMed:14729686,
CC       ECO:0000269|PubMed:18974784, ECO:0000269|Ref.3,
CC       ECO:0000305|PubMed:16535117}. Note=When the major carboxysomal shell
CC       protein CsoS1A is disrupted most RuBisCO is found in the soluble
CC       (cytoplasmic) fraction (PubMed:16535117). Most protein is found in the
CC       carboxysome interior and not associated with the shell
CC       (PubMed:14729686). This bacterium makes alpha-type carboxysomes (Ref.6,
CC       PubMed:18258595). {ECO:0000269|PubMed:14729686,
CC       ECO:0000269|PubMed:16535117, ECO:0000269|PubMed:18258595,
CC       ECO:0000269|Ref.6}.
CC   -!- INDUCTION: Produced when grown in air or in air supplemented with 5%
CC       CO(2) (at protein level). Part of the cbbL-cbbS operon.
CC       {ECO:0000269|PubMed:9696760}.
CC   -!- DOMAIN: The N-terminus (minimally 1-122, fragment 1-136 does not bind
CC       any better) interacts with the shell proteins CsoS1A, CsoS1B and
CC       CsoS1C. A slightly longer fragment of the N-terminus (residues 1-136)
CC       is required for targeting to carboxysomes, and will direct foreign
CC       proteins to the carboxysome, with reduced efficiency compared to the
CC       whole protein. {ECO:0000269|PubMed:30305640}.
CC   -!- DISRUPTION PHENOTYPE: Does not grow in air, grows poorly in air
CC       supplemented with 5% CO(2), a high-CO(2) requiring phenotype (hcr), has
CC       apolar effect on expression of downstream cbbS. Expresses type II but
CC       not type I RuBisCO, does not form carboxysomes but instead smaller,
CC       empty cytoplasmic inclusions (PubMed:9696760). A double ccbL-ccbS
CC       deletion is hcr and forms empty but otherwise normal appearing
CC       carboxysomes (PubMed:18974784). Required for growth in ambient air
CC       (PubMed:31406332). {ECO:0000269|PubMed:18974784,
CC       ECO:0000269|PubMed:31406332, ECO:0000269|PubMed:9696760}.
CC   -!- BIOTECHNOLOGY: Expression of 10 genes for alpha-carboxysome (Cb)
CC       proteins (cbbL-cbbS-csoS2-csoS3-csoS4A-csoS4B-csoS1C-csoS1A-csoS1B-
CC       csoS1D) in E.coli generates compartments that resemble Cb, contain
CC       RuBisCO and have its catalytic activity, showing it is possible to make
CC       artificial, functional Cb using these 10 genes. Cargo proteins can be
CC       targeted to these organelles (PubMed:22184212, PubMed:30305640). Alpha-
CC       carboxysomes are assembled in the complete absence of this enzyme in
CC       this bacteria, suggesting carboxysome-based microcompartments can be
CC       designed for applications such as custom chemical reactors or delivery
CC       vehicles (PubMed:18974784). When this gene is expressed in S.elongatus
CC       PCC 7942 it colocalizes with its beta-carboxysomes, suggesting there a
CC       range of modular possibilites for the carboxysome constituent proteins.
CC       These experiments open the door to generating carboxysomes in plant
CC       cells to increase their photosynthesis and productivity, as well as
CC       tailoring bacterial microcompartments to specific metabolic needs and
CC       molecule delivery (PubMed:29922315). {ECO:0000269|PubMed:18974784,
CC       ECO:0000269|PubMed:22184212, ECO:0000269|PubMed:29922315,
CC       ECO:0000269|PubMed:30305640}.
CC   -!- MISCELLANEOUS: The basic functional RuBisCO is composed of a large
CC       chain homodimer in a 'head-to-tail' conformation. In form I RuBisCO
CC       this homodimer is arranged in a barrel-like tetramer with the small
CC       subunits forming a tetrameric 'cap' on each end of the 'barrel'.
CC       {ECO:0000255|HAMAP-Rule:MF_01338}.
CC   -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type I
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01338}.
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DR   EMBL; AF038430; AAC32549.1; -; Genomic_DNA.
DR   EMBL; CP001801; ACX95765.1; -; Genomic_DNA.
DR   RefSeq; WP_012823801.1; NC_013422.1.
DR   PDB; 1SVD; X-ray; 1.80 A; A=1-473.
DR   PDB; 6UEW; X-ray; 2.40 A; A/C/E/G=2-473.
DR   PDB; 7SMK; EM; 1.98 A; A=2-473.
DR   PDB; 7SNV; EM; 2.07 A; A=2-473.
DR   PDB; 7ZBT; EM; 3.30 A; A/B/C/D/E/F/G/H=1-473.
DR   PDBsum; 1SVD; -.
DR   PDBsum; 6UEW; -.
DR   PDBsum; 7SMK; -.
DR   PDBsum; 7SNV; -.
DR   PDBsum; 7ZBT; -.
DR   AlphaFoldDB; O85040; -.
DR   EMDB; EMD-14590; -.
DR   EMDB; EMD-25201; -.
DR   EMDB; EMD-25228; -.
DR   SMR; O85040; -.
DR   STRING; 555778.Hneap_0922; -.
DR   KEGG; hna:Hneap_0922; -.
DR   eggNOG; COG1850; Bacteria.
DR   HOGENOM; CLU_031450_2_0_6; -.
DR   OrthoDB; 9770811at2; -.
DR   BRENDA; 4.1.1.39; 6349.
DR   EvolutionaryTrace; O85040; -.
DR   Proteomes; UP000009102; Chromosome.
DR   GO; GO:0031470; C:carboxysome; IEA:UniProtKB-SubCell.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.20.20.110; Ribulose bisphosphate carboxylase, large subunit, C-terminal domain; 1.
DR   Gene3D; 3.30.70.150; RuBisCO large subunit, N-terminal domain; 1.
DR   HAMAP; MF_01338; RuBisCO_L_type1; 1.
DR   InterPro; IPR033966; RuBisCO.
DR   InterPro; IPR020878; RuBisCo_large_chain_AS.
DR   InterPro; IPR000685; RuBisCO_lsu_C.
DR   InterPro; IPR036376; RuBisCO_lsu_C_sf.
DR   InterPro; IPR017443; RuBisCO_lsu_fd_N.
DR   InterPro; IPR036422; RuBisCO_lsu_N_sf.
DR   InterPro; IPR020888; RuBisCO_lsuI.
DR   PANTHER; PTHR42704; RIBULOSE BISPHOSPHATE CARBOXYLASE; 1.
DR   PANTHER; PTHR42704:SF9; RIBULOSE BISPHOSPHATE CARBOXYLASE LARGE CHAIN; 1.
DR   Pfam; PF00016; RuBisCO_large; 1.
DR   Pfam; PF02788; RuBisCO_large_N; 1.
DR   SFLD; SFLDG01052; RuBisCO; 1.
DR   SFLD; SFLDS00014; RuBisCO; 1.
DR   SFLD; SFLDG00301; RuBisCO-like_proteins; 1.
DR   SUPFAM; SSF51649; RuBisCo, C-terminal domain; 1.
DR   SUPFAM; SSF54966; RuBisCO, large subunit, small (N-terminal) domain; 1.
DR   PROSITE; PS00157; RUBISCO_LARGE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Bacterial microcompartment; Calvin cycle;
KW   Carbon dioxide fixation; Carboxysome; Lyase; Magnesium; Metal-binding;
KW   Monooxygenase; Oxidoreductase; Reference proteome.
FT   CHAIN           1..473
FT                   /note="Ribulose bisphosphate carboxylase large chain"
FT                   /id="PRO_0000062660"
FT   REGION          1..136
FT                   /note="Necessary and sufficient to target proteins to
FT                   carboxysomes, interacts with shell proteins"
FT                   /evidence="ECO:0000269|PubMed:30305640"
FT   ACT_SITE        168
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   ACT_SITE        287
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   BINDING         116
FT                   /ligand="substrate"
FT                   /note="in homodimeric partner"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   BINDING         166
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   BINDING         170
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   BINDING         194
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /note="via carbamate group"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   BINDING         196
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   BINDING         197
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   BINDING         288
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   BINDING         320
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   BINDING         372
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   SITE            327
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   MOD_RES         194
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   MUTAGEN         72
FT                   /note="Y->A: No longer binds N-repeats in CsoS2A; when
FT                   associated with A-346 and 'A-96' in CbbS."
FT                   /evidence="ECO:0000269|PubMed:32123388"
FT   MUTAGEN         72
FT                   /note="Y->R: No longer binds N-repeats in CsoS2A."
FT                   /evidence="ECO:0000269|PubMed:32123388"
FT   MUTAGEN         346
FT                   /note="F->A: No longer binds N-repeats in CsoS2A; when
FT                   associated with A-72 and 'A-96' in CbbS."
FT                   /evidence="ECO:0000269|PubMed:32123388"
FT   HELIX           14..17
FT                   /evidence="ECO:0007829|PDB:7SMK"
FT   STRAND          28..37
FT                   /evidence="ECO:0007829|PDB:1SVD"
FT   HELIX           43..53
FT                   /evidence="ECO:0007829|PDB:1SVD"
FT   TURN            54..56
FT                   /evidence="ECO:0007829|PDB:1SVD"
FT   STRAND          59..61
FT                   /evidence="ECO:0007829|PDB:7SMK"
FT   HELIX           63..67
FT                   /evidence="ECO:0007829|PDB:1SVD"
FT   TURN            70..72
FT                   /evidence="ECO:0007829|PDB:1SVD"
FT   STRAND          76..83
FT                   /evidence="ECO:0007829|PDB:1SVD"
FT   STRAND          86..96
FT                   /evidence="ECO:0007829|PDB:1SVD"
FT   HELIX           98..100
FT                   /evidence="ECO:0007829|PDB:1SVD"
FT   HELIX           106..114
FT                   /evidence="ECO:0007829|PDB:1SVD"
FT   HELIX           117..119
FT                   /evidence="ECO:0007829|PDB:1SVD"
FT   STRAND          123..132
FT                   /evidence="ECO:0007829|PDB:1SVD"
FT   HELIX           135..138
FT                   /evidence="ECO:0007829|PDB:1SVD"
FT   HELIX           148..155
FT                   /evidence="ECO:0007829|PDB:1SVD"
FT   STRAND          162..166
FT                   /evidence="ECO:0007829|PDB:1SVD"
FT   STRAND          170..172
FT                   /evidence="ECO:0007829|PDB:1SVD"
FT   HELIX           175..187
FT                   /evidence="ECO:0007829|PDB:1SVD"
FT   STRAND          191..194
FT                   /evidence="ECO:0007829|PDB:1SVD"
FT   STRAND          200..202
FT                   /evidence="ECO:0007829|PDB:1SVD"
FT   HELIX           207..225
FT                   /evidence="ECO:0007829|PDB:1SVD"
FT   STRAND          230..234
FT                   /evidence="ECO:0007829|PDB:1SVD"
FT   HELIX           240..253
FT                   /evidence="ECO:0007829|PDB:1SVD"
FT   STRAND          257..261
FT                   /evidence="ECO:0007829|PDB:1SVD"
FT   TURN            262..265
FT                   /evidence="ECO:0007829|PDB:1SVD"
FT   HELIX           267..280
FT                   /evidence="ECO:0007829|PDB:1SVD"
FT   STRAND          283..287
FT                   /evidence="ECO:0007829|PDB:1SVD"
FT   HELIX           291..295
FT                   /evidence="ECO:0007829|PDB:1SVD"
FT   STRAND          300..302
FT                   /evidence="ECO:0007829|PDB:1SVD"
FT   HELIX           304..314
FT                   /evidence="ECO:0007829|PDB:1SVD"
FT   STRAND          317..320
FT                   /evidence="ECO:0007829|PDB:1SVD"
FT   TURN            324..326
FT                   /evidence="ECO:0007829|PDB:7SMK"
FT   HELIX           329..331
FT                   /evidence="ECO:0007829|PDB:1SVD"
FT   HELIX           333..343
FT                   /evidence="ECO:0007829|PDB:1SVD"
FT   STRAND          345..347
FT                   /evidence="ECO:0007829|PDB:1SVD"
FT   HELIX           351..353
FT                   /evidence="ECO:0007829|PDB:1SVD"
FT   STRAND          368..374
FT                   /evidence="ECO:0007829|PDB:1SVD"
FT   HELIX           377..379
FT                   /evidence="ECO:0007829|PDB:1SVD"
FT   HELIX           380..387
FT                   /evidence="ECO:0007829|PDB:1SVD"
FT   STRAND          389..394
FT                   /evidence="ECO:0007829|PDB:1SVD"
FT   HELIX           397..400
FT                   /evidence="ECO:0007829|PDB:1SVD"
FT   HELIX           406..425
FT                   /evidence="ECO:0007829|PDB:1SVD"
FT   TURN            430..433
FT                   /evidence="ECO:0007829|PDB:1SVD"
FT   HELIX           434..442
FT                   /evidence="ECO:0007829|PDB:1SVD"
FT   HELIX           446..455
FT                   /evidence="ECO:0007829|PDB:1SVD"
SQ   SEQUENCE   473 AA;  52636 MW;  B84D2EDE46CAF7D8 CRC64;
     MAVKKYSAGV KEYRQTYWMP EYTPLDSDIL ACFKITPQPG VDREEAAAAV AAESSTGTWT
     TVWTDLLTDM DYYKGRAYRI EDVPGDDAAF YAFIAYPIDL FEEGSVVNVF TSLVGNVFGF
     KAVRGLRLED VRFPLAYVKT CGGPPHGIQV ERDKMNKYGR PLLGCTIKPK LGLSAKNYGR
     AVYECLRGGL DFTKDDENIN SQPFMRWRDR FLFVQDATET AEAQTGERKG HYLNVTAPTP
     EEMYKRAEFA KEIGAPIIMH DYITGGFTAN TGLAKWCQDN GVLLHIHRAM HAVIDRNPNH
     GIHFRVLTKI LRLSGGDHLH TGTVVGKLEG DRASTLGWID LLRESFIPED RSRGIFFDQD
     WGSMPGVFAV ASGGIHVWHM PALVNIFGDD SVLQFGGGTL GHPWGNAAGA AANRVALEAC
     VEARNQGRDI EKEGKEILTA AAQHSPELKI AMETWKEIKF EFDTVDKLDT QNR
//