CCMM_SYNE7
ID CCMM_SYNE7 Reviewed; 539 AA.
AC Q03513; Q31NB6;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Carboxysome assembly protein CcmM {ECO:0000305};
DE Short=CcmM58 {ECO:0000303|PubMed:17675289};
DE Short=M58 {ECO:0000303|PubMed:17675289};
DE AltName: Full=Carbon dioxide concentrating mechanism protein CcmM;
DE AltName: Full=Carboxysome shell associated protein CcmM {ECO:0000303|PubMed:29922315};
GN Name=ccmM {ECO:0000303|PubMed:8491708}; OrderedLocusNames=Synpcc7942_1423;
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 [GENOMIC DNA], DOMAIN, REPEATS, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=PCC 7942 / FACHB-805;
RX PubMed=8491708; DOI=10.1128/jb.175.10.2871-2879.1993;
RA Price G.D., Howitt S.M., Harrison K., Badger M.R.;
RT "Analysis of a genomic DNA region from the cyanobacterium Synechococcus sp.
RT strain PCC7942 involved in carboxysome assembly and function.";
RL J. Bacteriol. 175:2871-2879(1993).
RN [2]
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 [3]
RP LACK OF CARBONIC ANHYDRASE ACTIVITY.
RC STRAIN=PCC 7942 / FACHB-805;
RX DOI=10.1139/b05-057;
RA So A.K., Espie G.S.;
RT "Cyanobacterial carbonic anhydrases.";
RL Can. J. Bot. 83:721-734(2005).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND 2 FORMS OF
RP THE PROTEIN.
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 [5]
RP PROTEIN SEQUENCE OF 217-221, ISOFORMS CCMM58 AND CCMM35, FUNCTION,
RP INTERACTION WITH CARBONIC ANHYDRASE AND RUBISCO, SUBUNIT, SUBCELLULAR
RP LOCATION, DOMAIN, AND DISRUPTION PHENOTYPE.
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 [6]
RP FUNCTION, ISOFORM CCMM35, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF GLU-212 AND 215-THR-VAL-216.
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 [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
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 [8]
RP INTERACTION WITH CCMN.
RC STRAIN=PCC 7942 / FACHB-805;
RX PubMed=22461622; DOI=10.1074/jbc.m112.355305;
RA Kinney J.N., Salmeen A., Cai F., Kerfeld C.A.;
RT "Elucidating essential role of conserved carboxysomal protein CcmN reveals
RT common feature of bacterial microcompartment assembly.";
RL J. Biol. Chem. 287:17729-17736(2012).
RN [9]
RP CARBOXYSOME ASSEMBLY PROCESS, FUNCTION, DOMAIN, AND DISRUPTION PHENOTYPE.
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 [10]
RP FUNCTION, ISOFORM CCMM35, ISOFORM CCMM58, SUBCELLULAR LOCATION, DISRUPTION
RP PHENOTYPE, AND BIOTECHNOLOGY.
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 [11]
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 [12]
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 [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:6HBA, ECO:0007744|PDB:6HBB, ECO:0007744|PDB:6HBC}
RP X-RAY CRYSTALLOGRAPHY (1.20 ANGSTROMS) OF 225-313 REDUCED AND OXIDIZED,
RP STRUCTURE BY ELECTRON MICROSCOPY (2.78 ANGSTROMS) OF 225-313 REDUCED IN
RP COMPLEX WITH RUBISCO, FUNCTION, INTERACTION OF CCMM35 WITH RUBISCO,
RP DISULFIDE BOND, AND MUTAGENESIS OF 251-ARG-ARG-252; CYS-279 AND CYS-395.
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).
CC -!- FUNCTION: Functions as a scaffold protein for the assembly of beta-
CC carboxysomes, initiates carboxysome assembly by coalescing RuBisCO
CC (ribulose bisphosphate carboxylase, rbcL-rbcS) (Probable)
CC (PubMed:24267892). Produced as a full-length (M58) and a shorter form
CC (M35); both forms are required for correct carboxysome assembly and
CC growth (PubMed:20304968). The short form is more abundant
CC (PubMed:17675289, PubMed:20304968, PubMed:28963440, PubMed:31048338).
CC Despite its strong similarity to gamma-class carbonic anhydrase (CA) it
CC does not have detectable CA activity (Ref.3).
CC {ECO:0000269|PubMed:17675289, ECO:0000269|PubMed:20304968,
CC ECO:0000269|PubMed:24267892, ECO:0000269|PubMed:28963440,
CC ECO:0000269|PubMed:31048338, ECO:0000269|Ref.3,
CC ECO:0000305|PubMed:17675289, ECO:0000305|PubMed:20304968}.
CC -!- FUNCTION: [Isoform CcmM35]: The M35 isoform is able to condense RuBisCO
CC into a liquid matrix; the presence of disulfide bonds in M35 reduces
CC affinity for RuBisCO, while mutating all 4 Cys to Ser causes a 4-fold
CC increase in doubling time, more than 15% increase in CO(2) requirement,
CC and abnormal carboxysomes. {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
CC plus other less abundant CcmK proteins via CcmN's encapsulation
CC peptide. Shell formation requires CcmK proteins and CcmO. CcmL caps the
CC otherwise elongated carboxysome. Once fully encapsulated carboxysomes
CC are formed, they migrate within the cell probably via interactions with
CC the cytoskeleton. {ECO:0000269|PubMed:24267892,
CC ECO:0000269|PubMed:28963440, ECO:0000269|PubMed:30675061}.
CC -!- SUBUNIT: [Isoform CcmM58]: Probably a homotrimer (Probable). Purifies
CC from carboxysomes in complex with both RuBisCO subunits and carbonic
CC anhydrase (ccaA); the complex is probably associated with the
CC carboxysome shell (PubMed:17675289). Interacts with CcmN
CC (PubMed:22461622). Binds holo-RuBisCO (RbcL(8)-RbcS(8)) via its SSUL
CC domains; the SSUL domain binds close to the equitorial domain of
CC RuBisCO between RbcL dimers, with 1 M35 protein per dimer
CC (PubMed:30675061). {ECO:0000269|PubMed:17675289,
CC ECO:0000269|PubMed:22461622, ECO:0000269|PubMed:30675061,
CC ECO:0000305|PubMed:17675289}.
CC -!- SUBUNIT: [Isoform CcmM35]: The short form purifies from carboxysomes in
CC complex with both RuBisCO subunits; the complex is probably associated
CC with the carboxysome shell. {ECO:0000269|PubMed:17675289}.
CC -!- SUBCELLULAR LOCATION: Carboxysome {ECO:0000269|PubMed:17675289,
CC ECO:0000269|PubMed:20304968, ECO:0000269|PubMed:28616951,
CC ECO:0000269|PubMed:31048338, ECO:0000269|Ref.4}. Note=This
CC cyanobacterium makes beta-type carboxysomes (Ref.4). Both isoforms are
CC found equally distributed in the interior of the carboxysome
CC (PubMed:28963440). {ECO:0000269|PubMed:28963440, ECO:0000269|Ref.4}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=CcmM58 {ECO:0000269|PubMed:20304968, ECO:0000305|PubMed:17675289};
CC IsoId=Q03513-1; Sequence=Displayed;
CC Name=CcmM35 {ECO:0000269|PubMed:20304968, ECO:0000305|PubMed:17675289};
CC IsoId=Q03513-2; Sequence=VSP_060771, VSP_060772;
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 719 units (both forms are included in this measure) of this
CC protein per carboxysome, the numbers decrease under low light and high
CC CO(2), and increase under high light (at protein level).
CC {ECO:0000269|PubMed:31048338}.
CC -!- DOMAIN: In the N-terminus has a gamma-class carbonic anhydrase-like
CC domain (CA), while the C-terminus has 3 repeats that are similar to the
CC small subunit of RuBisCO (rbcS), called SSUL. The SSUL are connected by
CC flexible linkers. The N-terminal domain forms a scaffold on which CA
CC and maybe other carboxysomal proteins assemble, while the C-terminus
CC binds RuBisCO (PubMed:8491708) (Probable). At least 2 SSUL domains are
CC required for initiation of carboxysome assembly (PubMed:24267892).
CC Isolated reduced and oxidized CcmM35 binds holo-RuBisCO (RbcL(8)-
CC RbcS(8)) but neither subunit octamer alone; RuBisCO has a higher
CC affinity for reduced M35 (PubMed:30675061).
CC {ECO:0000269|PubMed:24267892, ECO:0000269|PubMed:30675061,
CC ECO:0000269|PubMed:8491708, ECO:0000305|PubMed:17675289}.
CC -!- PTM: Identified as 2 proteins of 58 and 38 kDa by mass spectrometry,
CC called M58 and M35, the shorter protein is translated starting at Val-
CC 216. Protease inhibitors do not alter the appearance of M35 (Ref.4,
CC PubMed:20304968). In isolated carboxysomes M35 is 4-5 fold more
CC abundant. The first amino acid (equivalent to Val-216) is not seen in
CC Edman degradation, while Tyr-219 and Gln-222 may be post-
CC translationally modified (PubMed:17675289).
CC {ECO:0000269|PubMed:17675289, ECO:0000269|PubMed:20304968,
CC ECO:0000269|Ref.4}.
CC -!- DISRUPTION PHENOTYPE: Single gene deletion does not form normal
CC carboxysomes, and does not grow in normal air but in 2% CO(2), called a
CC high-CO(2) requiring phenotype, HCR. CcmK2 and RuBisCO are targeted to
CC an abnormal large polar body in some studies, RuBisCO is soluble in
CC others (PubMed:8491708, PubMed:17675289, PubMed:20304968,
CC PubMed:22928045, PubMed:28963440). When ccmL-ccmM-ccmN-ccmO are deleted
CC no carboxysomes form, cells are HCR and RuBisCO is soluble
CC (PubMed:8491708). {ECO:0000269|PubMed:17675289,
CC ECO:0000269|PubMed:20304968, ECO:0000269|PubMed:22928045,
CC ECO:0000269|PubMed:28963440, ECO:0000269|PubMed:8491708}.
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 (PubMed:29922315). Large fluorescent tags can be
CC attached simultaneously to both termini of this protein (adding about
CC 60 kDa) and do not prevent carboxysome formation, showing proteins can
CC be targeted to carboxysomes by fusion to endogenous proteins
CC (PubMed:28963440). {ECO:0000269|PubMed:28963440,
CC ECO:0000269|PubMed:29922315}.
CC -!- MISCELLANEOUS: The M35 form (short form) is translated from the
CC internal start codon Val-216 (gtg), under control of an internal Shine-
CC Dalgarno sequence. Silent mutation of the codon for Val-216 to a non-
CC start codon (i.e. gtg to gtc) leads to low level expression of the M35
CC form, and abnormal carboxysomes which contain the expected proteins,
CC but does not grow in normal air. A strain that has a stop codon at
CC residue 215 makes abnormal carboxysomes which contain the expected
CC proteins, trace amounts of the N-terminus and is HCR, while a strain
CC that expresses only M35 has only RuBisCO in the abnormal carboxysomes
CC and is HCR. {ECO:0000269|PubMed:20304968}.
CC -!- SIMILARITY: Belongs to the gamma-class carbonic anhydrase family.
CC {ECO:0000305}.
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DR EMBL; M96929; AAA27306.1; -; Genomic_DNA.
DR EMBL; CP000100; ABB57453.1; -; Genomic_DNA.
DR PIR; D36904; D36904.
DR RefSeq; WP_011378029.1; NC_007604.1.
DR PDB; 6HBA; X-ray; 1.65 A; A/B=225-313.
DR PDB; 6HBB; X-ray; 1.20 A; A/B=225-313.
DR PDB; 6HBC; EM; 2.78 A; A=225-313.
DR PDB; 7D6C; X-ray; 2.89 A; 1/2=1-209.
DR PDB; 7O4Z; X-ray; 1.67 A; A=1-181.
DR PDB; 7O54; X-ray; 1.63 A; A=1-181.
DR PDBsum; 6HBA; -.
DR PDBsum; 6HBB; -.
DR PDBsum; 6HBC; -.
DR PDBsum; 7D6C; -.
DR PDBsum; 7O4Z; -.
DR PDBsum; 7O54; -.
DR AlphaFoldDB; Q03513; -.
DR SMR; Q03513; -.
DR STRING; 1140.Synpcc7942_1423; -.
DR PRIDE; Q03513; -.
DR EnsemblBacteria; ABB57453; ABB57453; Synpcc7942_1423.
DR KEGG; syf:Synpcc7942_1423; -.
DR eggNOG; COG0663; Bacteria.
DR eggNOG; COG4451; Bacteria.
DR HOGENOM; CLU_019008_0_0_3; -.
DR OMA; RFKTKSW; -.
DR OrthoDB; 448757at2; -.
DR BioCyc; SYNEL:SYNPCC7942_1423-MON; -.
DR GO; GO:0031470; C:carboxysome; IDA:UniProtKB.
DR GO; GO:0043886; F:structural constituent of carboxysome; IDA:UniProtKB.
DR GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-KW.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR Gene3D; 3.30.190.10; -; 3.
DR InterPro; IPR017156; CcmM.
DR InterPro; IPR000894; RuBisCO_ssu_dom.
DR InterPro; IPR036385; RuBisCO_ssu_sf.
DR InterPro; IPR011004; Trimer_LpxA-like_sf.
DR Pfam; PF00101; RuBisCO_small; 3.
DR PIRSF; PIRSF037250; CcmM; 1.
DR SMART; SM00961; RuBisCO_small; 3.
DR SUPFAM; SSF51161; SSF51161; 1.
DR SUPFAM; SSF55239; SSF55239; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative initiation; Bacterial microcompartment;
KW Carbon dioxide fixation; Carboxysome; Direct protein sequencing;
KW Disulfide bond; Photosynthesis; Repeat.
FT CHAIN 1..539
FT /note="Carboxysome assembly protein CcmM"
FT /id="PRO_0000077473"
FT REPEAT 226..397
FT /note="RbcS-like repeat 1, SSUL1"
FT /evidence="ECO:0000269|PubMed:30675061,
FT ECO:0000269|PubMed:8491708"
FT REPEAT 341..425
FT /note="RbcS-like repeat 2, SSUL2"
FT /evidence="ECO:0000269|PubMed:8491708,
FT ECO:0000305|PubMed:30675061"
FT REPEAT 453..539
FT /note="RbcS-like repeat 3, SSUL3"
FT /evidence="ECO:0000269|PubMed:8491708,
FT ECO:0000305|PubMed:30675061"
FT REGION 1..214
FT /note="Carbonic anhydrase-like domain"
FT /evidence="ECO:0000305|PubMed:17675289"
FT REGION 194..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 427..459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..459
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 261..279
FT /evidence="ECO:0000269|PubMed:30675061,
FT ECO:0007744|PDB:6HBA"
FT DISULFID 377..395
FT /evidence="ECO:0000305|PubMed:30675061"
FT VAR_SEQ 1..215
FT /note="Missing (in isoform CcmM35)"
FT /evidence="ECO:0000269|PubMed:17675289,
FT ECO:0000269|PubMed:20304968"
FT /id="VSP_060771"
FT VAR_SEQ 216
FT /note="V -> M (in isoform CcmM35)"
FT /evidence="ECO:0000305|PubMed:17675289"
FT /id="VSP_060772"
FT MUTAGEN 212
FT /note="E->S: Low level expression of the M35 form, abnormal
FT carboxysomes which contain the expected proteins, cells are
FT HCR, alters the Shine-Dalgarno sequence of M35."
FT /evidence="ECO:0000269|PubMed:20304968"
FT MUTAGEN 215..216
FT /note="TV->NL: Low level expression of the M35 form,
FT abnormal carboxysomes which contain the expected proteins,
FT cells are HCR, removes the start codon of M35."
FT /evidence="ECO:0000269|PubMed:20304968"
FT MUTAGEN 251..252
FT /note="RR->DD: Prevents RuBisCO condensation."
FT /evidence="ECO:0000269|PubMed:30675061"
FT MUTAGEN 279
FT /note="C->S: About 2-fold increased doubling time, about
FT 15% increase in CO(2) requirement."
FT /evidence="ECO:0000269|PubMed:30675061"
FT MUTAGEN 395
FT /note="C->S: About 2-fold increased doubling time, about
FT 15% increase in CO(2) requirement."
FT /evidence="ECO:0000269|PubMed:30675061"
FT STRAND 31..38
FT /evidence="ECO:0007829|PDB:7O54"
FT STRAND 49..55
FT /evidence="ECO:0007829|PDB:7O54"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:7O54"
FT STRAND 71..74
FT /evidence="ECO:0007829|PDB:7O54"
FT STRAND 87..92
FT /evidence="ECO:0007829|PDB:7O54"
FT STRAND 103..110
FT /evidence="ECO:0007829|PDB:7O54"
FT STRAND 121..127
FT /evidence="ECO:0007829|PDB:7O54"
FT STRAND 138..141
FT /evidence="ECO:0007829|PDB:7O54"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:7O54"
FT HELIX 159..163
FT /evidence="ECO:0007829|PDB:7O54"
FT HELIX 170..179
FT /evidence="ECO:0007829|PDB:7O54"
FT HELIX 227..238
FT /evidence="ECO:0007829|PDB:6HBB"
FT STRAND 242..248
FT /evidence="ECO:0007829|PDB:6HBB"
FT HELIX 250..254
FT /evidence="ECO:0007829|PDB:6HBB"
FT HELIX 269..282
FT /evidence="ECO:0007829|PDB:6HBB"
FT TURN 283..285
FT /evidence="ECO:0007829|PDB:6HBB"
FT STRAND 286..293
FT /evidence="ECO:0007829|PDB:6HBB"
FT TURN 295..297
FT /evidence="ECO:0007829|PDB:6HBB"
FT STRAND 300..307
FT /evidence="ECO:0007829|PDB:6HBB"
SQ SEQUENCE 539 AA; 57833 MW; 0DA37466B4BCB76B CRC64;
MPSPTTVPVA TAGRLAEPYI DPAAQVHAIA SIIGDVRIAA GVRVAAGVSI RADEGAPFQV
GKESILQEGA VIHGLEYGRV LGDDQADYSV WIGQRVAITH KALIHGPAYL GDDCFVGFRS
TVFNARVGAG SVIMMHALVQ DVEIPPGRYV PSGAIITTQQ QADRLPEVRP EDREFARHII
GSPPVIVRST PAATADFHST PTPSPLRPSS SEATTVSAYN GQGRLSSEVI TQVRSLLNQG
YRIGTEHADK RRFRTSSWQP CAPIQSTNER QVLSELENCL SEHEGEYVRL LGIDTNTRSR
VFEALIQRPD GSVPESLGSQ PVAVASGGGR QSSYASVSGN LSAEVVNKVR NLLAQGYRIG
TEHADKRRFR TSSWQSCAPI QSSNERQVLA ELENCLSEHE GEYVRLLGID TASRSRVFEA
LIQDPQGPVG SAKAAAAPVS SATPSSHSYT SNGSSSSDVA GQVRGLLAQG YRISAEVADK
RRFQTSSWQS LPALSGQSEA TVLPALESIL QEHKGKYVRL IGIDPAARRR VAELLIQKP
