MNTR_BACSU
ID MNTR_BACSU Reviewed; 142 AA.
AC P54512;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=HTH-type transcriptional regulator MntR {ECO:0000255|HAMAP-Rule:MF_00732, ECO:0000305};
DE AltName: Full=Manganese transport regulator {ECO:0000255|HAMAP-Rule:MF_00732, ECO:0000303|PubMed:16533030};
DE AltName: Full=Manganese(II) metalloregulatory protein MntR {ECO:0000303|PubMed:14580210};
GN Name=mntR {ECO:0000255|HAMAP-Rule:MF_00732, ECO:0000303|PubMed:10760146};
GN Synonyms=yqhN; OrderedLocusNames=BSU24520;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / JH642;
RX PubMed=8969508; DOI=10.1099/13500872-142-11-3103;
RA Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M.,
RA Kobayashi Y.;
RT "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the
RT Bacillus subtilis genome containing the skin element and many sporulation
RT genes.";
RL Microbiology 142:3103-3111(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP SEQUENCE REVISION TO 81.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=168;
RX PubMed=10760146; DOI=10.1046/j.1365-2958.2000.01811.x;
RA Que Q., Helmann J.D.;
RT "Manganese homeostasis in Bacillus subtilis is regulated by MntR, a
RT bifunctional regulator related to the diphtheria toxin repressor family of
RT proteins.";
RL Mol. Microbiol. 35:1454-1468(2000).
RN [5]
RP ACTIVITY REGULATION, DNA-BINDING, AND SUBUNIT.
RX PubMed=14580210; DOI=10.1021/bi0350248;
RA Lieser S.A., Davis T.C., Helmann J.D., Cohen S.M.;
RT "DNA-binding and oligomerization studies of the manganese(II)
RT metalloregulatory protein MntR from Bacillus subtilis.";
RL Biochemistry 42:12634-12642(2003).
RN [6]
RP FUNCTION, AND DNA-BINDING.
RX PubMed=12950915; DOI=10.1046/j.1365-2958.2003.03648.x;
RA Guedon E., Moore C.M., Que Q., Wang T., Ye R.W., Helmann J.D.;
RT "The global transcriptional response of Bacillus subtilis to manganese
RT involves the MntR, Fur, TnrA and sigmaB regulons.";
RL Mol. Microbiol. 49:1477-1491(2003).
RN [7]
RP FUNCTION, DNA-BINDING, AND DISRUPTION PHENOTYPE.
RX PubMed=27748968; DOI=10.1111/mmi.13554;
RA Huang X., Shin J.H., Pinochet-Barros A., Su T.T., Helmann J.D.;
RT "Bacillus subtilis MntR coordinates the transcriptional regulation of
RT manganese uptake and efflux systems.";
RL Mol. Microbiol. 103:253-268(2017).
RN [8] {ECO:0007744|PDB:1ON1, ECO:0007744|PDB:1ON2}
RP X-RAY CRYSTALLOGRAPHY (1.61 ANGSTROMS) OF WILD-TYPE AND MUTANT MET-8 IN
RP COMPLEX WITH MANGANESE, SUBUNIT, DOMAIN, AND MUTAGENESIS OF ASP-8.
RX PubMed=12847518; DOI=10.1038/nsb951;
RA Glasfeld A., Guedon E., Helmann J.D., Brennan R.G.;
RT "Structure of the manganese-bound manganese transport regulator of Bacillus
RT subtilis.";
RL Nat. Struct. Biol. 10:652-657(2003).
RN [9] {ECO:0007744|PDB:2EV0, ECO:0007744|PDB:2EV5, ECO:0007744|PDB:2EV6, ECO:0007744|PDB:2F5C, ECO:0007744|PDB:2F5D, ECO:0007744|PDB:2F5E, ECO:0007744|PDB:2F5F}
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEXES WITH CADMIUM; CALCIUM;
RP MANGANESE AND ZINC, DNA-BINDING, ACTIVITY REGULATION, SUBUNIT, AND DOMAIN.
RX PubMed=16533030; DOI=10.1021/bi0524215;
RA Kliegman J.I., Griner S.L., Helmann J.D., Brennan R.G., Glasfeld A.;
RT "Structural basis for the metal-selective activation of the manganese
RT transport regulator of Bacillus subtilis.";
RL Biochemistry 45:3493-3505(2006).
RN [10] {ECO:0007744|PDB:2HYF, ECO:0007744|PDB:2HYG}
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS), AND SUBUNIT.
RX PubMed=17118401; DOI=10.1016/j.jmb.2006.10.080;
RA DeWitt M.A., Kliegman J.I., Helmann J.D., Brennan R.G., Farrens D.L.,
RA Glasfeld A.;
RT "The conformations of the manganese transport regulator of Bacillus
RT subtilis in its metal-free state.";
RL J. Mol. Biol. 365:1257-1265(2007).
RN [11] {ECO:0007744|PDB:3R60, ECO:0007744|PDB:3R61, ECO:0007744|PDB:4HV5, ECO:0007744|PDB:4HV6, ECO:0007744|PDB:4HX4, ECO:0007744|PDB:4HX7, ECO:0007744|PDB:4HX8}
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 2-142 IN COMPLEXES WITH CADMIUM;
RP COBALT; IRON AND MANGANESE AND OF MUTANTS LYS-11 AND ALA-77, DNA-BINDING,
RP ACTIVITY REGULATION, SUBUNIT, DOMAIN, AND MUTAGENESIS OF GLU-11 AND HIS-77.
RX PubMed=23298157; DOI=10.1021/bi301550t;
RA McGuire A.M., Cuthbert B.J., Ma Z., Grauer-Gray K.D., Brunjes Brophy M.,
RA Spear K.A., Soonsanga S., Kliegman J.I., Griner S.L., Helmann J.D.,
RA Glasfeld A.;
RT "Roles of the A and C sites in the manganese-specific activation of MntR.";
RL Biochemistry 52:701-713(2013).
CC -!- FUNCTION: Central regulator of manganese homeostasis that regulates the
CC expression of both manganese uptake and efflux systems
CC (PubMed:27748968, PubMed:10760146, PubMed:12950915). In the presence of
CC high levels of manganese, it mediates repression of the manganese
CC uptake systems MntH and MntABCD and activation of the efflux systems
CC MneP and MneS. Binds with high affinity to the regulatory regions of
CC its target genes (PubMed:27748968, PubMed:12950915). The manganese
CC concentration required for activation of efflux is higher than that for
CC repression of uptake (PubMed:27748968). {ECO:0000269|PubMed:10760146,
CC ECO:0000269|PubMed:12950915, ECO:0000269|PubMed:27748968}.
CC -!- ACTIVITY REGULATION: DNA binding is strongly activated by Mn(2+) and
CC Cd(2+), but it is poorly activated by non-cognate metal cations,
CC including Co(2+), Fe(2+), Ni(2+), Ca(2+) and Zn(2+). In the strict
CC absence of divalent transition metal ions, MntR has a low affinity for
CC DNA. {ECO:0000269|PubMed:14580210, ECO:0000269|PubMed:16533030,
CC ECO:0000269|PubMed:23298157}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00732,
CC ECO:0000269|PubMed:12847518, ECO:0000269|PubMed:14580210,
CC ECO:0000269|PubMed:16533030, ECO:0000269|PubMed:17118401,
CC ECO:0000269|PubMed:23298157}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00732,
CC ECO:0000305}.
CC -!- DOMAIN: Contains an N-terminal DNA-binding domain and a C-terminal
CC dimerization domain (PubMed:12847518, PubMed:16533030,
CC PubMed:23298157). Contains two metal binding sites per subunit, site A
CC (corresponding to metal ion 2) and site C (corresponding to metal ion
CC 1), which both contribute to the metal selectivity of MntR. A large
CC metal cation is needed at the A site to correctly orient and position
CC the C site ligands. Smaller, non-cognate metal cations bind at the A
CC site, but disrupt the C site, blocking the full activation of MntR.
CC Binding at the C site also favors Mn(2+) and Cd(2+) over other metals
CC (PubMed:16533030, PubMed:23298157). {ECO:0000269|PubMed:12847518,
CC ECO:0000269|PubMed:16533030, ECO:0000269|PubMed:23298157}.
CC -!- DISRUPTION PHENOTYPE: Null mutant is very sensitive to manganese
CC (PubMed:27748968, PubMed:10760146). Mutant also displays increased
CC sensitivity to cadmium (PubMed:10760146). {ECO:0000269|PubMed:10760146,
CC ECO:0000269|PubMed:27748968}.
CC -!- SIMILARITY: Belongs to the DtxR/MntR family. {ECO:0000255|HAMAP-
CC Rule:MF_00732, ECO:0000305}.
CC -!- CAUTION: Was originally thought to act as an activator for the mntABCD
CC operon. {ECO:0000305|PubMed:10760146, ECO:0000305|PubMed:12950915}.
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DR EMBL; D84432; BAA12551.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14383.2; -; Genomic_DNA.
DR PIR; E69959; E69959.
DR RefSeq; NP_390332.2; NC_000964.3.
DR RefSeq; WP_003236923.1; NZ_JNCM01000036.1.
DR PDB; 1ON1; X-ray; 1.75 A; A/B=1-142.
DR PDB; 1ON2; X-ray; 1.61 A; A/B=1-142.
DR PDB; 2EV0; X-ray; 1.65 A; A/B=1-142.
DR PDB; 2EV5; X-ray; 2.00 A; A/B=1-142.
DR PDB; 2EV6; X-ray; 1.70 A; A/B=1-142.
DR PDB; 2F5C; X-ray; 2.40 A; A=1-142.
DR PDB; 2F5D; X-ray; 1.90 A; A/B=1-142.
DR PDB; 2F5E; X-ray; 2.20 A; A/B=1-142.
DR PDB; 2F5F; X-ray; 2.40 A; A/B=1-142.
DR PDB; 2HYF; X-ray; 2.80 A; A/B/C/D=1-142.
DR PDB; 2HYG; X-ray; 2.80 A; D=1-142.
DR PDB; 3R60; X-ray; 1.80 A; A/B=2-142.
DR PDB; 3R61; X-ray; 1.90 A; A/B=2-142.
DR PDB; 4HV5; X-ray; 1.90 A; A/B=2-142.
DR PDB; 4HV6; X-ray; 2.30 A; A/B=2-142.
DR PDB; 4HX4; X-ray; 1.65 A; A/B=2-142.
DR PDB; 4HX7; X-ray; 1.90 A; A/B=2-142.
DR PDB; 4HX8; X-ray; 2.00 A; A/B=2-142.
DR PDBsum; 1ON1; -.
DR PDBsum; 1ON2; -.
DR PDBsum; 2EV0; -.
DR PDBsum; 2EV5; -.
DR PDBsum; 2EV6; -.
DR PDBsum; 2F5C; -.
DR PDBsum; 2F5D; -.
DR PDBsum; 2F5E; -.
DR PDBsum; 2F5F; -.
DR PDBsum; 2HYF; -.
DR PDBsum; 2HYG; -.
DR PDBsum; 3R60; -.
DR PDBsum; 3R61; -.
DR PDBsum; 4HV5; -.
DR PDBsum; 4HV6; -.
DR PDBsum; 4HX4; -.
DR PDBsum; 4HX7; -.
DR PDBsum; 4HX8; -.
DR AlphaFoldDB; P54512; -.
DR SMR; P54512; -.
DR STRING; 224308.BSU24520; -.
DR PaxDb; P54512; -.
DR PRIDE; P54512; -.
DR EnsemblBacteria; CAB14383; CAB14383; BSU_24520.
DR GeneID; 938554; -.
DR KEGG; bsu:BSU24520; -.
DR PATRIC; fig|224308.179.peg.2670; -.
DR eggNOG; COG1321; Bacteria.
DR InParanoid; P54512; -.
DR OMA; SWDAIDR; -.
DR PhylomeDB; P54512; -.
DR BioCyc; BSUB:BSU24520-MON; -.
DR EvolutionaryTrace; P54512; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0030026; P:cellular manganese ion homeostasis; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 1.10.60.10; -; 1.
DR HAMAP; MF_00732; HTH_MntR; 1.
DR InterPro; IPR001367; Fe_dep_repressor.
DR InterPro; IPR036421; Fe_dep_repressor_sf.
DR InterPro; IPR022687; HTH_DTXR.
DR InterPro; IPR022897; HTH_tscrpt_reg_MntR.
DR InterPro; IPR022689; Iron_dep_repressor.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF02742; Fe_dep_repr_C; 1.
DR Pfam; PF01325; Fe_dep_repress; 1.
DR SMART; SM00529; HTH_DTXR; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF47979; SSF47979; 1.
DR PROSITE; PS50944; HTH_DTXR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Cadmium; Cytoplasm; DNA-binding; Manganese;
KW Metal-binding; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..142
FT /note="HTH-type transcriptional regulator MntR"
FT /id="PRO_0000201118"
FT DOMAIN 1..63
FT /note="HTH dtxR-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00732"
FT BINDING 8
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:16533030,
FT ECO:0000269|PubMed:23298157"
FT BINDING 8
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:12847518,
FT ECO:0000269|PubMed:16533030, ECO:0000269|PubMed:23298157"
FT BINDING 11
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:16533030,
FT ECO:0000269|PubMed:23298157"
FT BINDING 11
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:12847518,
FT ECO:0000269|PubMed:16533030, ECO:0000269|PubMed:23298157"
FT BINDING 77
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:16533030,
FT ECO:0000269|PubMed:23298157"
FT BINDING 77
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:12847518,
FT ECO:0000269|PubMed:16533030, ECO:0000269|PubMed:23298157"
FT BINDING 99
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:16533030,
FT ECO:0000269|PubMed:23298157"
FT BINDING 99
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:16533030,
FT ECO:0000269|PubMed:23298157"
FT BINDING 99
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:16533030,
FT ECO:0000269|PubMed:23298157"
FT BINDING 99
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:12847518,
FT ECO:0000269|PubMed:16533030, ECO:0000269|PubMed:23298157"
FT BINDING 102
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:16533030,
FT ECO:0000269|PubMed:23298157"
FT BINDING 102
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:16533030,
FT ECO:0000269|PubMed:23298157"
FT BINDING 102
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:12847518,
FT ECO:0000269|PubMed:16533030, ECO:0000269|PubMed:23298157"
FT BINDING 102
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:12847518,
FT ECO:0000269|PubMed:16533030, ECO:0000269|PubMed:23298157"
FT BINDING 103
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:16533030,
FT ECO:0000269|PubMed:23298157"
FT BINDING 103
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:12847518,
FT ECO:0000269|PubMed:16533030, ECO:0000269|PubMed:23298157"
FT MUTAGEN 8
FT /note="D->M: Binds only one manganese ion, in a pseudo-
FT hexacoordinate geometry."
FT /evidence="ECO:0000269|PubMed:12847518"
FT MUTAGEN 11
FT /note="E->K: Retains selectivity for activation by Mn(2+)
FT and Cd(2+) over Co(2+) and Fe(2+). Can bind Mn(2+) in the C
FT site, despite alteration to the A site, and adopt active
FT DNA-binding conformations. Non-cognate ions fail to
FT generate fully active complexes."
FT /evidence="ECO:0000269|PubMed:23298157"
FT MUTAGEN 77
FT /note="H->A: Retains selectivity for activation by Mn(2+)
FT and Cd(2+) over Co(2+) and Fe(2+). Can bind Mn(2+) in the C
FT site, despite alteration to the A site, and adopt active
FT DNA-binding conformations. Non-cognate ions fail to
FT generate fully active complexes."
FT /evidence="ECO:0000269|PubMed:23298157"
FT CONFLICT 81
FT /note="E -> D (in Ref. 1; BAA12551)"
FT /evidence="ECO:0000305"
FT HELIX 4..20
FT /evidence="ECO:0007829|PDB:1ON2"
FT HELIX 25..32
FT /evidence="ECO:0007829|PDB:1ON2"
FT HELIX 36..48
FT /evidence="ECO:0007829|PDB:1ON2"
FT STRAND 51..55
FT /evidence="ECO:0007829|PDB:1ON2"
FT TURN 56..58
FT /evidence="ECO:0007829|PDB:1ON2"
FT STRAND 59..62
FT /evidence="ECO:0007829|PDB:1ON2"
FT HELIX 64..86
FT /evidence="ECO:0007829|PDB:1ON2"
FT HELIX 91..101
FT /evidence="ECO:0007829|PDB:1ON2"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:1ON2"
FT HELIX 107..121
FT /evidence="ECO:0007829|PDB:1ON2"
FT HELIX 124..134
FT /evidence="ECO:0007829|PDB:1ON2"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:2F5C"
SQ SEQUENCE 142 AA; 16759 MW; 653BD8E0F4AB9F2C CRC64;
MTTPSMEDYI EQIYMLIEEK GYARVSDIAE ALAVHPSSVT KMVQKLDKDE YLIYEKYRGL
VLTSKGKKIG KRLVYRHELL EQFLRIIGVD EEKIYNDVEG IEHHLSWNSI DRIGDLVQYF
EEDDARKKDL KSIQKKTEHH NQ
