MAMK_MAGSA
ID MAMK_MAGSA Reviewed; 347 AA.
AC Q2W8Q6;
DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Actin-like protein MamK {ECO:0000303|PubMed:16373532};
DE EC=3.6.1.- {ECO:0000269|PubMed:23204522, ECO:0000269|PubMed:24957623};
DE AltName: Full=Magnetosome cytoskeleton protein MamK {ECO:0000305};
GN Name=mamK; OrderedLocusNames=amb0965;
OS Magnetospirillum magneticum (strain AMB-1 / ATCC 700264).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Magnetospirillum.
OX NCBI_TaxID=342108;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SUBCELLULAR LOCATION.
RC STRAIN=AMB-1 / ATCC 700264;
RX PubMed=16303747; DOI=10.1093/dnares/dsi002;
RA Matsunaga T., Okamura Y., Fukuda Y., Wahyudi A.T., Murase Y., Takeyama H.;
RT "Complete genome sequence of the facultative anaerobic magnetotactic
RT bacterium Magnetospirillum sp. strain AMB-1.";
RL DNA Res. 12:157-166(2005).
RN [2]
RP FUNCTION, EXPRESSION IN E.COLI, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP 1-MET--VAL-25.
RC STRAIN=AMB-1 / ATCC 700264;
RX PubMed=17085581; DOI=10.1073/pnas.0603760103;
RA Pradel N., Santini C.L., Bernadac A., Fukumori Y., Wu L.F.;
RT "Biogenesis of actin-like bacterial cytoskeletal filaments destined for
RT positioning prokaryotic magnetic organelles.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:17485-17489(2006).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=AMB-1 / ATCC 700264;
RX PubMed=16373532; DOI=10.1126/science.1123231;
RA Komeili A., Li Z., Newman D.K., Jensen G.J.;
RT "Magnetosomes are cell membrane invaginations organized by the actin-like
RT protein MamK.";
RL Science 311:242-245(2006).
RN [4]
RP FUNCTION, INTERACTION WITH MCP10, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP 1-MET--VAL-25.
RC STRAIN=AMB-1 / ATCC 700264;
RX PubMed=20471399; DOI=10.1016/j.jmb.2010.05.011;
RA Philippe N., Wu L.F.;
RT "An MCP-like protein interacts with the MamK cytoskeleton and is involved
RT in magnetotaxis in Magnetospirillum magneticum AMB-1.";
RL J. Mol. Biol. 400:309-322(2010).
RN [5]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=AMB-1 / ATCC 700264;
RX PubMed=20161777; DOI=10.1371/journal.pone.0009151;
RA Rioux J.B., Philippe N., Pereira S., Pignol D., Wu L.F., Ginet N.;
RT "A second actin-like MamK protein in Magnetospirillum magneticum AMB-1
RT encoded outside the genomic magnetosome island.";
RL PLoS ONE 5:E9151-E9151(2010).
RN [6]
RP PROBABLE OPERON, AND DISRUPTION PHENOTYPE.
RC STRAIN=AMB-1 / ATCC 700264;
RX PubMed=20212111; DOI=10.1073/pnas.0914439107;
RA Murat D., Quinlan A., Vali H., Komeili A.;
RT "Comprehensive genetic dissection of the magnetosome gene island reveals
RT the step-wise assembly of a prokaryotic organelle.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:5593-5598(2010).
RN [7]
RP FUNCTION, ACTIVITY REGULATION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP GLU-143 AND ASP-161.
RC STRAIN=AMB-1 / ATCC 700264;
RX PubMed=21883528; DOI=10.1111/j.1365-2958.2011.07815.x;
RA Draper O., Byrne M.E., Li Z., Keyhani S., Barrozo J.C., Jensen G.,
RA Komeili A.;
RT "MamK, a bacterial actin, forms dynamic filaments in vivo that are
RT regulated by the acidic proteins MamJ and LimJ.";
RL Mol. Microbiol. 82:342-354(2011).
RN [8]
RP MINIMAL MAGNETOSOME ISLAND.
RC STRAIN=AMB-1 / ATCC 700264;
RX PubMed=22716969; DOI=10.1111/j.1365-2958.2012.08132.x;
RA Murat D., Falahati V., Bertinetti L., Csencsits R., Koernig A., Downing K.,
RA Faivre D., Komeili A.;
RT "The magnetosome membrane protein, MmsF, is a major regulator of magnetite
RT biomineralization in Magnetospirillum magneticum AMB-1.";
RL Mol. Microbiol. 85:684-699(2012).
RN [9]
RP INDUCTION.
RC STRAIN=AMB-1 / ATCC 700264;
RX PubMed=25048532; DOI=10.1111/1574-6968.12541;
RA Taoka A., Eguchi Y., Mise S., Oestreicher Z., Uno F., Fukumori Y.;
RT "A magnetosome-associated cytochrome MamP is critical for magnetite crystal
RT growth during the exponential growth phase.";
RL FEMS Microbiol. Lett. 358:21-29(2014).
RN [10]
RP FUNCTION, ATPASE ACTIVITY, FORMS FILAMENTS, BIOPHYSICOCHEMICAL PROPERTIES,
RP INTERACTION WITH MAMK, SUBUNIT, SUBCELLULAR LOCATION, INDUCTION, DISRUPTION
RP PHENOTYPE, AND MUTAGENESIS OF GLU-143.
RC STRAIN=AMB-1 / ATCC 700264;
RX PubMed=24957623; DOI=10.1128/jb.01674-14;
RA Abreu N., Mannoubi S., Ozyamak E., Pignol D., Ginet N., Komeili A.;
RT "Interplay between two bacterial actin homologs, MamK and MamK-Like, is
RT required for the alignment of magnetosome organelles in Magnetospirillum
RT magneticum AMB-1.";
RL J. Bacteriol. 196:3111-3121(2014).
RN [11]
RP SUBCELLULAR LOCATION.
RC STRAIN=AMB-1 / ATCC 700264;
RX PubMed=27481925; DOI=10.1128/jb.00280-16;
RA Arakaki A., Kikuchi D., Tanaka M., Yamagishi A., Yoda T., Matsunaga T.;
RT "Comparative subcellular localization analysis of magnetosome proteins
RT reveals a unique localization behavior of Mms6 protein onto magnetite
RT crystals.";
RL J. Bacteriol. 198:2794-2802(2016).
RN [12]
RP STRUCTURE BY ELECTRON MICROSCOPY (12.0 ANGSTROMS), FUNCTION, ATPASE
RP ACTIVITY, FORMS FILAMENTS, SUBUNIT, AND MUTAGENESIS OF GLU-143.
RC STRAIN=AMB-1 / ATCC 700264;
RX PubMed=23204522; DOI=10.1074/jbc.m112.417030;
RA Ozyamak E., Kollman J., Agard D.A., Komeili A.;
RT "The bacterial actin MamK: in vitro assembly behavior and filament
RT architecture.";
RL J. Biol. Chem. 288:4265-4277(2013).
RN [13]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=AMB-1 / ATCC 700264;
RX PubMed=26884433; DOI=10.1128/mbio.01898-15;
RA Cornejo E., Subramanian P., Li Z., Jensen G.J., Komeili A.;
RT "Dynamic Remodeling of the Magnetosome Membrane Is Triggered by the
RT Initiation of Biomineralization.";
RL MBio 7:E01898-E01898(2016).
RN [14]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLU-143 AND ASP-161.
RC STRAIN=AMB-1 / ATCC 700264;
RX PubMed=28790202; DOI=10.1128/mbio.00679-17;
RA Taoka A., Kiyokawa A., Uesugi C., Kikuchi Y., Oestreicher Z., Morii K.,
RA Eguchi Y., Fukumori Y.;
RT "Tethered Magnets Are the Key to Magnetotaxis: Direct Observations of
RT Magnetospirillum magneticum AMB-1 Show that MamK Distributes Magnetosome
RT Organelles Equally to Daughter Cells.";
RL MBio 8:0-0(2017).
RN [15] {ECO:0007744|PDB:5LJV, ECO:0007744|PDB:5LJW}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 1-347 IN COMPLEX WITH ADP AND ATP
RP ANALOG, SUBUNIT, DOMAIN, AND MUTAGENESIS OF ALA-278.
RC STRAIN=AMB-1 / ATCC 700264;
RX PubMed=27821762; DOI=10.1073/pnas.1612034113;
RA Lowe J., He S., Scheres S.H., Savva C.G.;
RT "X-ray and cryo-EM structures of monomeric and filamentous actin-like
RT protein MamK reveal changes associated with polymerization.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:13396-13401(2016).
RN [16] {ECO:0007744|PDB:5JYG}
RP STRUCTURE BY ELECTRON MICROSCOPY (6.50 ANGSTROMS) IN COMPLEX WITH ADP,
RP FUNCTION, FORMS FILAMENTS, SUBUNIT, AND MUTAGENESIS OF 240-LYS--VAL-242.
RX PubMed=27391173; DOI=10.1002/pro.2979;
RA Bergeron J.R., Hutto R., Ozyamak E., Hom N., Hansen J., Draper O.,
RA Byrne M.E., Keyhani S., Komeili A., Kollman J.M.;
RT "Structure of the magnetosome-associated actin-like MamK filament at
RT subnanometer resolution.";
RL Protein Sci. 26:93-102(2017).
CC -!- FUNCTION: Protein with ATPase activity which forms dynamic cytoplasmic
CC filaments (probably with paralog MamK-like) that organize magnetosomes
CC into long chains running parallel to the long axis of the cell
CC (Probable) (PubMed:21883528, PubMed:28790202, PubMed:23204522,
CC PubMed:24957623). Turnover of MamK filaments is probably promoted by
CC MamK-like, which provides a monomer pool (PubMed:24957623). Forms
CC twisted filaments in the presence of ATP or GTP (PubMed:20161777,
CC PubMed:23204522, PubMed:27391173). Serves to close gaps between
CC magnetosomes in the chain (PubMed:26884433). Interaction with MCP10 is
CC involved in controlling the response to magnetic fields, possibly by
CC controlling flagellar rotation (PubMed:20471399). Expression in E.coli
CC yields a filament in the cell's longitudinal axis; the protein
CC nucleates at several sites and one extremity of the filament is located
CC at the cell pole (PubMed:17085581, PubMed:20161777).
CC {ECO:0000269|PubMed:17085581, ECO:0000269|PubMed:20161777,
CC ECO:0000269|PubMed:20471399, ECO:0000269|PubMed:21883528,
CC ECO:0000269|PubMed:23204522, ECO:0000269|PubMed:24957623,
CC ECO:0000269|PubMed:26884433, ECO:0000269|PubMed:27391173,
CC ECO:0000269|PubMed:28790202, ECO:0000305|PubMed:16373532}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:23204522, ECO:0000269|PubMed:24957623};
CC -!- ACTIVITY REGULATION: Filament turnover is promoted by MamJ and/or LimJ
CC which have overlapping function; at least one other protein is required
CC for turnover. MamK filament dynamics are probably required for the
CC assembly or maintenance of the magnetosome chain.
CC {ECO:0000269|PubMed:21883528}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=143 uM for ATP {ECO:0000269|PubMed:24957623};
CC -!- SUBUNIT: Forms cytoplasmic filaments (PubMed:20471399, PubMed:23204522,
CC PubMed:27821762, PubMed:27391173). Filaments are parallel (polar) and
CC double-helical (PubMed:23204522, PubMed:27821762, PubMed:27391173).
CC MamK subunits from each of the two strands are juxtaposed, each monomer
CC binds ADP (PubMed:27821762, PubMed:27391173). At cell poles and septa
CC interacts with methyl-accepting chemotaxis protein Amb0944 (MCP10)
CC (PubMed:20471399). Forms filaments with MamK-like protein
CC (PubMed:24957623). {ECO:0000269|PubMed:20471399,
CC ECO:0000269|PubMed:23204522, ECO:0000269|PubMed:24957623,
CC ECO:0000269|PubMed:27391173, ECO:0000269|PubMed:27821762}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16373532,
CC ECO:0000305|PubMed:20471399}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:16373532, ECO:0000269|PubMed:17085581,
CC ECO:0000269|PubMed:20471399, ECO:0000269|PubMed:21883528,
CC ECO:0000269|PubMed:24957623, ECO:0000269|PubMed:27481925}. Magnetosome
CC membrane {ECO:0000305|PubMed:16303747}; Peripheral membrane protein
CC {ECO:0000305}. Note=Tagged protein forms straight lines extending along
CC most of the cell associated with its inner curvature, in the correct
CC position to be filaments that are seen associated with magnetosomes
CC (PubMed:17085581, PubMed:16373532, PubMed:20471399, PubMed:27481925,
CC PubMed:21883528). Colocalizes in filaments with paralog MamK-like
CC (PubMed:24957623). {ECO:0000269|PubMed:16373532,
CC ECO:0000269|PubMed:17085581, ECO:0000269|PubMed:20471399,
CC ECO:0000269|PubMed:21883528, ECO:0000269|PubMed:24957623,
CC ECO:0000269|PubMed:27481925}.
CC -!- INDUCTION: Constitutively expressed, levels remain the same over 144
CC hours of growth (at protein level) (PubMed:25048532). Expressed during
CC exponential phase in static growth conditions (PubMed:20161777).
CC Expressed during late exponential phase in the presence and absence of
CC the mamK-like gene (PubMed:24957623). Part of the probable 18 gene
CC mamAB operon (Probable). {ECO:0000269|PubMed:20161777,
CC ECO:0000269|PubMed:24957623, ECO:0000269|PubMed:25048532,
CC ECO:0000305|PubMed:20212111}.
CC -!- DOMAIN: Domains close around the active site upon filament formation,
CC which probably enhances nucleotide hydrolysis (PubMed:27821762).
CC Nucleotide-binding also probably induces domain movement (Probable).
CC {ECO:0000269|PubMed:27821762, ECO:0000305|PubMed:27391173}.
CC -!- DISRUPTION PHENOTYPE: Magnetosomes are dispersed in groups of 2-3
CC throughout the cytoplasm, no evidence of magnetosome-associated
CC filaments. Cells form magnetite and turn in magnetic fields
CC (PubMed:16373532, PubMed:26884433). Unanchored magnetosomes move
CC randomly in the cytoplasm. Magnetosomes are unevenly segregated to
CC daughter cells (PubMed:28790202). About 45% reduction in magnetosome
CC alignment; a double mamK-mamK-like deletion has a 65% reduction in
CC magnetosome alignment. MamK-like protein forms many fewer filaments
CC (PubMed:24957623). Another paper shows deletion of mamK to yield
CC approximately wild-type magnetosomes (PubMed:20161777). Deletion of
CC genes mamH to mamV (amb0961 to amb0978) gives cells with no
CC magnetosomes and no magnetic response (PubMed:20212111).
CC {ECO:0000269|PubMed:16373532, ECO:0000269|PubMed:20161777,
CC ECO:0000269|PubMed:20212111, ECO:0000269|PubMed:24957623,
CC ECO:0000269|PubMed:26884433, ECO:0000269|PubMed:28790202}.
CC -!- MISCELLANEOUS: This bacteria makes up to 20 cubo-octahedral
CC magnetosomes of about 45 nm in diameter which contain membrane-bound
CC crystals of magnetite (Fe(3)O(4)). {ECO:0000305}.
CC -!- MISCELLANEOUS: Expression of just the minimal mamAB gene cluster
CC (amb0961 to amb0978), including this gene, is sufficient to form a
CC minimal magnetosome chain with small magnetite particles.
CC {ECO:0000269|PubMed:22716969}.
CC -!- MISCELLANEOUS: In the related bacteria M.gryphiswaldense strain MSR-1
CC the magnetosome position moves from cell pole to mid cell during
CC cytokinesis. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the FtsA/MreB family. MamK subfamily.
CC {ECO:0000305|PubMed:16373532}.
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DR EMBL; AP007255; BAE49769.1; -; Genomic_DNA.
DR RefSeq; WP_011383398.1; NC_007626.1.
DR PDB; 5JYG; EM; 6.50 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=1-347.
DR PDB; 5LJV; EM; 3.65 A; A/B/C/D/E/F=1-347.
DR PDB; 5LJW; X-ray; 1.80 A; A/B=1-347.
DR PDBsum; 5JYG; -.
DR PDBsum; 5LJV; -.
DR PDBsum; 5LJW; -.
DR AlphaFoldDB; Q2W8Q6; -.
DR SMR; Q2W8Q6; -.
DR STRING; 342108.amb0965; -.
DR EnsemblBacteria; BAE49769; BAE49769; amb0965.
DR KEGG; mag:amb0965; -.
DR HOGENOM; CLU_052037_3_0_5; -.
DR OMA; VVSEPFM; -.
DR OrthoDB; 410781at2; -.
DR Proteomes; UP000007058; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IDA:UniProtKB.
DR GO; GO:0110146; C:magnetosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0110148; P:biomineralization; IMP:UniProtKB.
DR InterPro; IPR004000; Actin.
DR InterPro; IPR043129; ATPase_NBD.
DR SMART; SM00268; ACTIN; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Biomineralization; Cytoplasm; Cytoskeleton;
KW GTP-binding; Hydrolase; Magnesium; Magnetosome; Membrane; Metal-binding;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..347
FT /note="Actin-like protein MamK"
FT /id="PRO_0000447774"
FT BINDING 9
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:27821762,
FT ECO:0007744|PDB:5LJW"
FT BINDING 20..21
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:27391173,
FT ECO:0000269|PubMed:27821762, ECO:0007744|PDB:5JYG,
FT ECO:0007744|PDB:5LJW"
FT BINDING 76
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:27391173,
FT ECO:0000269|PubMed:27821762, ECO:0007744|PDB:5JYG,
FT ECO:0007744|PDB:5LJW"
FT BINDING 143
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:27821762,
FT ECO:0007744|PDB:5LJV"
FT BINDING 164..166
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:27391173,
FT ECO:0000269|PubMed:27821762, ECO:0000305|PubMed:21883528,
FT ECO:0007744|PDB:5JYG, ECO:0007744|PDB:5LJW"
FT BINDING 218..222
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:27391173,
FT ECO:0000269|PubMed:27821762, ECO:0007744|PDB:5JYG,
FT ECO:0007744|PDB:5LJW"
FT BINDING 289
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:27391173,
FT ECO:0000269|PubMed:27821762, ECO:0007744|PDB:5JYG,
FT ECO:0007744|PDB:5LJW"
FT MUTAGEN 1..25
FT /note="Missing: Protein localizes to cell poles in E.coli,
FT no longer forms filaments. No longer interacts with MCP10
FT in vivo."
FT /evidence="ECO:0000269|PubMed:17085581,
FT ECO:0000269|PubMed:20471399"
FT MUTAGEN 143
FT /note="E->A: Wild-type subcellular location, MamK filaments
FT no longer dynamic. Protein polymerizes rapidly in vitro,
FT has lost ATPase activity, filaments no longer disassemble.
FT Only partially restores magnetosome distribution."
FT /evidence="ECO:0000269|PubMed:21883528,
FT ECO:0000269|PubMed:23204522, ECO:0000269|PubMed:24957623,
FT ECO:0000269|PubMed:28790202"
FT MUTAGEN 161
FT /note="D->A: Wild-type subcellular location, MamK filaments
FT no longer dynamic. Only partially restores magnetosome
FT distribution."
FT /evidence="ECO:0000269|PubMed:21883528,
FT ECO:0000269|PubMed:28790202"
FT MUTAGEN 240..242
FT /note="KPV->APE: Filament nucleation is very slow, will
FT assemble in vitro when seeded with wild-type protein. Does
FT not form filaments in vivo."
FT /evidence="ECO:0000269|PubMed:27391173"
FT MUTAGEN 278
FT /note="A->D: No longer polymerizes, used for X-ray
FT crystallography."
FT /evidence="ECO:0000269|PubMed:27821762"
FT HELIX 5..9
FT /evidence="ECO:0007829|PDB:5LJW"
FT STRAND 10..18
FT /evidence="ECO:0007829|PDB:5LJW"
FT STRAND 20..27
FT /evidence="ECO:0007829|PDB:5LJW"
FT STRAND 32..37
FT /evidence="ECO:0007829|PDB:5LJW"
FT STRAND 39..44
FT /evidence="ECO:0007829|PDB:5LJW"
FT HELIX 45..51
FT /evidence="ECO:0007829|PDB:5LJW"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:5LJW"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:5LJW"
FT HELIX 59..63
FT /evidence="ECO:0007829|PDB:5LJW"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:5LJW"
FT STRAND 68..71
FT /evidence="ECO:0007829|PDB:5LJW"
FT TURN 76..78
FT /evidence="ECO:0007829|PDB:5LJW"
FT HELIX 84..100
FT /evidence="ECO:0007829|PDB:5LJW"
FT STRAND 108..115
FT /evidence="ECO:0007829|PDB:5LJW"
FT HELIX 121..131
FT /evidence="ECO:0007829|PDB:5LJW"
FT TURN 132..134
FT /evidence="ECO:0007829|PDB:5LJW"
FT STRAND 135..142
FT /evidence="ECO:0007829|PDB:5LJW"
FT HELIX 143..150
FT /evidence="ECO:0007829|PDB:5LJW"
FT STRAND 155..162
FT /evidence="ECO:0007829|PDB:5LJW"
FT STRAND 167..172
FT /evidence="ECO:0007829|PDB:5LJW"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:5LJW"
FT HELIX 179..181
FT /evidence="ECO:0007829|PDB:5LJW"
FT STRAND 182..186
FT /evidence="ECO:0007829|PDB:5LJW"
FT HELIX 189..203
FT /evidence="ECO:0007829|PDB:5LJW"
FT HELIX 211..221
FT /evidence="ECO:0007829|PDB:5LJW"
FT STRAND 232..237
FT /evidence="ECO:0007829|PDB:5LJW"
FT STRAND 240..245
FT /evidence="ECO:0007829|PDB:5LJW"
FT HELIX 247..255
FT /evidence="ECO:0007829|PDB:5LJW"
FT HELIX 258..269
FT /evidence="ECO:0007829|PDB:5LJW"
FT HELIX 274..276
FT /evidence="ECO:0007829|PDB:5LJW"
FT HELIX 277..280
FT /evidence="ECO:0007829|PDB:5LJW"
FT STRAND 284..288
FT /evidence="ECO:0007829|PDB:5LJW"
FT HELIX 289..292
FT /evidence="ECO:0007829|PDB:5LJW"
FT HELIX 296..303
FT /evidence="ECO:0007829|PDB:5LJW"
FT TURN 304..307
FT /evidence="ECO:0007829|PDB:5LJW"
FT STRAND 312..314
FT /evidence="ECO:0007829|PDB:5LJW"
FT TURN 318..320
FT /evidence="ECO:0007829|PDB:5LJW"
FT HELIX 321..332
FT /evidence="ECO:0007829|PDB:5LJW"
SQ SEQUENCE 347 AA; 37614 MW; 9E59787DB21CB5B6 CRC64;
MSEGEGQAKN RLFLGIDLGT SHTAVMSSRG KKFLLKSVVG YPKDVIGLKL LGRPYVVGDE
AFEMRSYLDI RYPLQDGVLS EISDRDIEVA RHLLTHVVKS AEPGPNDEIC AVIGVPARAS
AANKALLLKM AQEVVHTALV VSEPFMVGYG LDKLINTIIV DIGAGTTDIC ALKGTVPGPE
DQVTLTKAGN YVDERLQNAI LERHPELQMN VNVACAVKEQ FSFVGTPTEV ASFEFRAAGK
PVRADVTEPV KIACEALMPD IIESIETLLR SFQPEYQATV LQNIVFAGGG SRIRGLAAYV
KEKLRPFGDA NVTCVKDPTF DGCRGALRLA EELPPQYWRQ LGDVSGS
