RBL_SYNE7
ID RBL_SYNE7 Reviewed; 472 AA.
AC Q31NB3;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
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:24585024};
GN Name=cbbL {ECO:0000255|HAMAP-Rule:MF_01338};
GN Synonyms=rbcL {ECO:0000255|HAMAP-Rule:MF_01338,
GN ECO:0000303|PubMed:17675289}; OrderedLocusNames=Synpcc7942_1426;
OS Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS R2).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=1140;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7942 / FACHB-805;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC STRAIN=PCC 7942 / FACHB-805;
RX DOI=10.1139/b05-058;
RA Long B.M., Price G.D., Badger M.R.;
RT "Proteomic assessment of an established technique for carboxysome
RT enrichment from Synechococcus PCC7942.";
RL Can. J. Bot. 83:746-757(2005).
RN [3]
RP INTERACTION WITH CCMM, AND SUBCELLULAR LOCATION.
RC STRAIN=PCC 7942 / FACHB-805;
RX PubMed=17675289; DOI=10.1074/jbc.m703896200;
RA Long B.M., Badger M.R., Whitney S.M., Price G.D.;
RT "Analysis of carboxysomes from Synechococcus PCC7942 reveals multiple
RT Rubisco complexes with carboxysomal proteins CcmM and CcaA.";
RL J. Biol. Chem. 282:29323-29335(2007).
RN [4]
RP SUBCELLULAR LOCATION.
RC STRAIN=PCC 7942 / FACHB-805;
RX PubMed=20304968; DOI=10.1104/pp.110.154948;
RA Long B.M., Tucker L., Badger M.R., Price G.D.;
RT "Functional cyanobacterial beta-carboxysomes have an absolute requirement
RT for both long and short forms of the CcmM protein.";
RL Plant Physiol. 153:285-293(2010).
RN [5]
RP SUBCELLULAR LOCATION.
RC STRAIN=PCC 7942 / FACHB-805;
RX PubMed=22928045; DOI=10.1371/journal.pone.0043871;
RA Rae B.D., Long B.M., Badger M.R., Price G.D.;
RT "Structural determinants of the outer shell of beta-carboxysomes in
RT Synechococcus elongatus PCC 7942: roles for CcmK2, K3-K4, CcmO, and CcmL.";
RL PLoS ONE 7:e43871-e43871(2012).
RN [6]
RP CARBOXYSOME ASSEMBLY PROCESS.
RC STRAIN=PCC 7942 / FACHB-805;
RX PubMed=24267892; DOI=10.1016/j.cell.2013.10.044;
RA Cameron J.C., Wilson S.C., Bernstein S.L., Kerfeld C.A.;
RT "Biogenesis of a bacterial organelle: the carboxysome assembly pathway.";
RL Cell 155:1131-1140(2013).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RC STRAIN=PCC 7942 / FACHB-805;
RX PubMed=24585024; DOI=10.1007/s11120-014-9986-7;
RA Nishimura T., Yamaguchi O., Takatani N., Maeda S., Omata T.;
RT "In vitro and in vivo analyses of the role of the carboxysomal beta-type
RT carbonic anhydrase of the cyanobacterium Synechococcus elongatus in
RT carboxylation of ribulose-1,5-bisphosphate.";
RL Photosyn. Res. 121:151-157(2014).
RN [8]
RP RUBISCO FOLDING AND ASSEMBLY, INTERACTION WITH RAF1, AND SUBUNIT.
RC STRAIN=PCC 7942 / FACHB;
RX PubMed=26237510; DOI=10.1038/nsmb.3062;
RA Hauser T., Bhat J.Y., Milicic G., Wendler P., Hartl F.U., Bracher A.,
RA Hayer-Hartl M.;
RT "Structure and mechanism of the Rubisco-assembly chaperone Raf1.";
RL Nat. Struct. Mol. Biol. 22:720-728(2015).
RN [9]
RP SUBCELLULAR LOCATION.
RC STRAIN=PCC 7942 / FACHB-805;
RX PubMed=28963440; DOI=10.1091/mbc.e17-01-0069;
RA Niederhuber M.J., Lambert T.J., Yapp C., Silver P.A., Polka J.K.;
RT "Superresolution microscopy of the beta-carboxysome reveals a homogeneous
RT matrix.";
RL Mol. Biol. Cell 28:2734-2745(2017).
RN [10]
RP SUBCELLULAR LOCATION.
RC STRAIN=PCC 7942 / FACHB-805;
RX PubMed=28616951; DOI=10.1039/c7nr02524f;
RA Faulkner M., Rodriguez-Ramos J., Dykes G.F., Owen S.V., Casella S.,
RA Simpson D.M., Beynon R.J., Liu L.N.;
RT "Direct characterization of the native structure and mechanics of
RT cyanobacterial carboxysomes.";
RL Nanoscale 9:10662-10673(2017).
RN [11]
RP BIOTECHNOLOGY.
RC STRAIN=PCC 7942 / FACHB-805;
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 SUBUNIT.
RC STRAIN=PCC 7942 / FACHB-805;
RX PubMed=30389782; DOI=10.1104/pp.18.01217;
RA Huang F., Vasieva O., Sun Y., Faulkner M., Dykes G.F., Zhao Z., Liu L.N.;
RT "Roles of RbcX in Carboxysome Biosynthesis in the Cyanobacterium
RT Synechococcus elongatus PCC7942.";
RL Plant Physiol. 179:184-194(2019).
RN [13]
RP SUBCELLULAR LOCATION, AND INDUCTION.
RC STRAIN=PCC 7942 / FACHB-805;
RX PubMed=31048338; DOI=10.1105/tpc.18.00787;
RA Sun Y., Wollman A.J.M., Huang F., Leake M.C., Liu L.N.;
RT "Single-Organelle Quantification Reveals Stoichiometric and Structural
RT Variability of Carboxysomes Dependent on the Environment.";
RL Plant Cell 31:1648-1664(2019).
RN [14] {ECO:0007744|PDB:6HBC}
RP STRUCTURE BY ELECTRON MICROSCOPY (2.78 ANGSTROMS) IN COMPLEX WITH SMALL
RP SUBUNIT AND CCMM35, FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RC STRAIN=PCC 7942 / FACHB-805;
RX PubMed=30675061; DOI=10.1038/s41586-019-0880-5;
RA Wang H., Yan X., Aigner H., Bracher A., Nguyen N.D., Hee W.Y., Long B.M.,
RA Price G.D., Hartl F.U., Hayer-Hartl M.;
RT "Rubisco condensate formation by CcmM in beta-carboxysome biogenesis.";
RL Nature 566:131-135(2019).
RN [15] {ECO:0007744|PDB:6SMH}
RP STRUCTURE BY ELECTRON MICROSCOPY (4.30 ANGSTROMS) OF 19-465 IN COMPLEX WITH
RP RAF1, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND
RP RUBISCO FOLDING AND ASSEMBLY.
RC STRAIN=PCC 7942 / FACHB-805;
RX PubMed=32636267; DOI=10.1073/pnas.2007990117;
RA Huang F., Kong W.W., Sun Y., Chen T., Dykes G.F., Jiang Y.L., Liu L.N.;
RT "Rubisco accumulation factor 1 (Raf1) plays essential roles in mediating
RT Rubisco assembly and carboxysome biogenesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 117:17418-17428(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 in the photorespiration process. Both reactions occur
CC simultaneously and in competition at the same active site.
CC {ECO:0000255|HAMAP-Rule:MF_01338, ECO:0000269|PubMed:24585024,
CC ECO:0000269|PubMed:30675061}.
CC -!- FUNCTION: Beta-carboxysome assembly initiates when soluble RuBisCO is
CC condensed into a liquid matrix in a pre-carboxysome by the RbcS-like
CC domains of probably both CcmM58 and CcmM35. CcmN interacts with the N-
CC terminus of CcmM58, and then recruits the CcmK2 major shell protein via
CC CcmN's encapsulation peptide. Shell formation requires CcmK proteins
CC and CcmO. CcmL caps the otherwise elongated carboxysome. Once fully
CC encapsulated carboxysomes are formed, they migrate within the cell
CC probably via interactions with the cytoskeleton.
CC {ECO:0000269|PubMed:24267892, ECO:0000269|PubMed:30675061}.
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:24585024,
CC ECO:0000269|PubMed:30675061, ECO:0000269|PubMed:32636267};
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-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=58 uM for D-ribulose 1,5-bisphosphate
CC {ECO:0000269|PubMed:32636267};
CC -!- SUBUNIT: Heterohexadecamer of 8 large chains and 8 small chains;
CC disulfide-linked (Probable). The disulfide link is formed within the
CC large subunit homodimers (Probable). Isolated reduced and oxidized M35
CC binds holo-RuBisCO (RbcL(8)-RbcS(8)) but neither subunit octamer alone;
CC RuBisCO has a higher affinity for reduced M35. M35 binds RuBisCO via
CC its SSUL domains; the SSUL domain binds close to the equitorial domain
CC of RuBisCO between RbcL dimers, with 1 M35 protein per dimer
CC (PubMed:30675061). Colocalizes with RbcX throughout carboxysome
CC formation (PubMed:30389782). {ECO:0000269|PubMed:17675289,
CC ECO:0000269|PubMed:30389782, ECO:0000269|PubMed:30675061,
CC ECO:0000305|PubMed:17675289, ECO:0000305|PubMed:30675061,
CC ECO:0000305|PubMed:32636267}.
CC -!- SUBCELLULAR LOCATION: Carboxysome {ECO:0000255|HAMAP-Rule:MF_01338,
CC ECO:0000269|PubMed:17675289, ECO:0000269|PubMed:20304968,
CC ECO:0000269|PubMed:22928045, ECO:0000269|PubMed:24585024,
CC ECO:0000269|PubMed:28616951, ECO:0000269|PubMed:28963440,
CC ECO:0000269|PubMed:31048338, ECO:0000269|Ref.2}. Note=The CcmM short
CC form (M35) purifies from carboxysomes in complex with both RuBisCO
CC subunits; a second complex with full-length CcmM and RuBisCO also
CC includes carbonic anhydrase (CA, ccaA). RuBisCO-CcmM complexes are
CC probably associated with the carboxysome shell (PubMed:17675289). In
CC the carboxysome RuBisCO is organized into a paracrystalline array
CC (PubMed:28616951). This cyanobacterium makes beta-type carboxysomes
CC (PubMed:22928045). {ECO:0000269|PubMed:17675289,
CC ECO:0000269|PubMed:22928045, ECO:0000269|PubMed:28616951}.
CC -!- INDUCTION: Carboxysome size and components vary with growth conditions.
CC When grown in ambient air at medium light (50 uE meter(-2) second(-1))
CC there are 853 RuBisCO complexes (RbcL8S8) per carboxysome (measured
CC using the small subunit), the numbers decrease under low light and high
CC CO(2), and increase under high light (at protein level).
CC {ECO:0000305|PubMed:31048338}.
CC -!- PTM: The disulfide bond which can form in the large chain dimeric
CC partners within the hexadecamer appears to be associated with oxidative
CC stress and protein turnover. {ECO:0000255|HAMAP-Rule:MF_01338}.
CC -!- BIOTECHNOLOGY: Heterologous expression of 12 carboxysomal genes in
CC E.coli (ccaA, ccmK2, ccmK3, ccmK4, ccmL, ccmM, ccmN, ccmO, ccmP, rbcL,
CC rbcS, rbcX) leads to the formation of bodies that resemble
CC carboxysomes, have densely packed paracrystalline arrays and RuBisCO
CC activity. These structures open the door to generating carboxysomes in
CC plant cells to increase their photosynthesis and productivity, as well
CC as tailoring bacterial microcompartments to specific metabolic needs
CC and molecule delivery. {ECO:0000269|PubMed:29922315}.
CC -!- MISCELLANEOUS: RuBisCO folding and assembly commences when the nascent
CC large subunit folds with the help of chaperonin GroEL-GroES. Both RbcX
CC and Raf1 help folded RbcL release from the chaperonin and dimerize;
CC dimeric Raf1 binds to RbcL(2) leading to an RbcL8-Raf1(8) complex. RbcS
CC displaces Raf1, resulting in holoenzyme formation.
CC {ECO:0000269|PubMed:26237510, ECO:0000269|PubMed:32636267,
CC ECO:0000305|PubMed:30389782}.
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; CP000100; ABB57456.1; -; Genomic_DNA.
DR RefSeq; WP_011242444.1; NC_007604.1.
DR PDB; 6HBC; EM; 2.78 A; B/C=1-472.
DR PDB; 6SMH; EM; 4.30 A; A/B/C/D/E/F/G/H=19-465.
DR PDBsum; 6HBC; -.
DR PDBsum; 6SMH; -.
DR AlphaFoldDB; Q31NB3; -.
DR SMR; Q31NB3; -.
DR STRING; 1140.Synpcc7942_1426; -.
DR PRIDE; Q31NB3; -.
DR EnsemblBacteria; ABB57456; ABB57456; Synpcc7942_1426.
DR KEGG; syf:Synpcc7942_1426; -.
DR eggNOG; COG1850; Bacteria.
DR HOGENOM; CLU_031450_2_0_3; -.
DR OMA; IHGHPDG; -.
DR OrthoDB; 848380at2; -.
DR BioCyc; SYNEL:SYNPCC7942_1426-MON; -.
DR GO; GO:0031470; C:carboxysome; IDA:UniProtKB.
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:0009853; P:photorespiration; IEA:UniProtKB-KW.
DR GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-UniRule.
DR CDD; cd08212; RuBisCO_large_I; 1.
DR Gene3D; 3.20.20.110; -; 1.
DR Gene3D; 3.30.70.150; -; 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; PTHR42704; 1.
DR Pfam; PF00016; RuBisCO_large; 1.
DR Pfam; PF02788; RuBisCO_large_N; 1.
DR SFLD; SFLDS00014; RuBisCO; 1.
DR SUPFAM; SSF51649; SSF51649; 1.
DR SUPFAM; SSF54966; SSF54966; 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; Disulfide bond; Lyase; Magnesium;
KW Metal-binding; Monooxygenase; Oxidoreductase; Photorespiration;
KW Photosynthesis.
FT CHAIN 1..472
FT /note="Ribulose bisphosphate carboxylase large chain"
FT /id="PRO_0000251463"
FT ACT_SITE 172
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT ACT_SITE 291
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 120
FT /ligand="substrate"
FT /note="in homodimeric partner"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 170
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 174
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 198
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 200
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 201
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 292
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 324
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 376
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT SITE 331
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT MOD_RES 198
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT DISULFID 244
FT /note="Interchain; in linked form"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT HELIX 18..21
FT /evidence="ECO:0007829|PDB:6HBC"
FT STRAND 33..41
FT /evidence="ECO:0007829|PDB:6HBC"
FT HELIX 47..57
FT /evidence="ECO:0007829|PDB:6HBC"
FT TURN 58..60
FT /evidence="ECO:0007829|PDB:6HBC"
FT HELIX 67..71
FT /evidence="ECO:0007829|PDB:6HBC"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:6HBC"
FT STRAND 80..86
FT /evidence="ECO:0007829|PDB:6HBC"
FT STRAND 94..100
FT /evidence="ECO:0007829|PDB:6HBC"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:6HBC"
FT HELIX 110..117
FT /evidence="ECO:0007829|PDB:6HBC"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:6HBC"
FT STRAND 127..136
FT /evidence="ECO:0007829|PDB:6HBC"
FT HELIX 139..142
FT /evidence="ECO:0007829|PDB:6HBC"
FT HELIX 151..159
FT /evidence="ECO:0007829|PDB:6HBC"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:6HBC"
FT STRAND 172..175
FT /evidence="ECO:0007829|PDB:6HBC"
FT HELIX 179..191
FT /evidence="ECO:0007829|PDB:6HBC"
FT STRAND 195..198
FT /evidence="ECO:0007829|PDB:6HBC"
FT STRAND 204..206
FT /evidence="ECO:0007829|PDB:6HBC"
FT HELIX 211..229
FT /evidence="ECO:0007829|PDB:6HBC"
FT STRAND 234..238
FT /evidence="ECO:0007829|PDB:6HBC"
FT HELIX 244..256
FT /evidence="ECO:0007829|PDB:6HBC"
FT STRAND 260..265
FT /evidence="ECO:0007829|PDB:6HBC"
FT HELIX 266..269
FT /evidence="ECO:0007829|PDB:6HBC"
FT HELIX 271..284
FT /evidence="ECO:0007829|PDB:6HBC"
FT STRAND 287..291
FT /evidence="ECO:0007829|PDB:6HBC"
FT HELIX 295..299
FT /evidence="ECO:0007829|PDB:6HBC"
FT STRAND 302..306
FT /evidence="ECO:0007829|PDB:6HBC"
FT HELIX 308..318
FT /evidence="ECO:0007829|PDB:6HBC"
FT STRAND 321..324
FT /evidence="ECO:0007829|PDB:6HBC"
FT HELIX 336..347
FT /evidence="ECO:0007829|PDB:6HBC"
FT STRAND 349..351
FT /evidence="ECO:0007829|PDB:6HBC"
FT HELIX 355..357
FT /evidence="ECO:0007829|PDB:6HBC"
FT STRAND 372..378
FT /evidence="ECO:0007829|PDB:6HBC"
FT TURN 381..383
FT /evidence="ECO:0007829|PDB:6HBC"
FT HELIX 384..391
FT /evidence="ECO:0007829|PDB:6HBC"
FT STRAND 396..398
FT /evidence="ECO:0007829|PDB:6HBC"
FT HELIX 401..404
FT /evidence="ECO:0007829|PDB:6HBC"
FT HELIX 410..429
FT /evidence="ECO:0007829|PDB:6HBC"
FT TURN 434..436
FT /evidence="ECO:0007829|PDB:6HBC"
FT HELIX 438..445
FT /evidence="ECO:0007829|PDB:6HBC"
FT TURN 446..448
FT /evidence="ECO:0007829|PDB:6HBC"
FT HELIX 450..458
FT /evidence="ECO:0007829|PDB:6HBC"
SQ SEQUENCE 472 AA; 52448 MW; CDD8519AA9D493C9 CRC64;
MPKTQSAAGY KAGVKDYKLT YYTPDYTPKD TDLLAAFRFS PQPGVPADEA GAAIAAESST
GTWTTVWTDL LTDMDRYKGK CYHIEPVQGE ENSYFAFIAY PLDLFEEGSV TNILTSIVGN
VFGFKAIRSL RLEDIRFPVA LVKTFQGPPH GIQVERDLLN KYGRPMLGCT IKPKLGLSAK
NYGRAVYECL RGGLDFTKDD ENINSQPFQR WRDRFLFVAD AIHKSQAETG EIKGHYLNVT
APTCEEMMKR AEFAKELGMP IIMHDFLTAG FTANTTLAKW CRDNGVLLHI HRAMHAVIDR
QRNHGIHFRV LAKCLRLSGG DHLHSGTVVG KLEGDKASTL GFVDLMREDH IEADRSRGVF
FTQDWASMPG VLPVASGGIH VWHMPALVEI FGDDSVLQFG GGTLGHPWGN APGATANRVA
LEACVQARNE GRDLYREGGD ILREAGKWSP ELAAALDLWK EIKFEFETMD KL
