MTDRP_MYCTU
ID MTDRP_MYCTU Reviewed; 653 AA.
AC P9WLZ7; L0T6M8; Q11034;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 48.
DE RecName: Full=Multidomain regulatory protein Rv1364c {ECO:0000303|PubMed:21220116};
DE AltName: Full=Anti-sigma-F factor Rv1364c {ECO:0000305};
DE Short=Anti-SigF factor {ECO:0000303|PubMed:30642988};
DE AltName: Full=Protein-serine/threonine phosphatase {ECO:0000305};
DE EC=3.1.3.16 {ECO:0000269|PubMed:19700407, ECO:0000269|PubMed:30642988};
DE AltName: Full=Putative multidomain regulator of SigF {ECO:0000303|PubMed:19016841};
DE Short=MursiF {ECO:0000303|PubMed:19016841};
DE AltName: Full=Serine/threonine-protein kinase {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000269|PubMed:19700407, ECO:0000269|PubMed:30642988};
GN OrderedLocusNames=Rv1364c; ORFNames=MTCY02B10.28c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP INDUCTION.
RX PubMed=17485404; DOI=10.2741/2417;
RA Dhandayuthapani S.;
RT "Stress response of genes encoding putative stress signaling molecules of
RT Mycobacterium tuberculosis.";
RL Front. Biosci. 12:4676-4681(2007).
RN [3]
RP COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, DOMAIN, AND MUTAGENESIS OF ASP-211
RP AND ASP-328.
RX PubMed=19016841; DOI=10.1111/j.1742-4658.2008.06753.x;
RA Sachdeva P., Narayan A., Misra R., Brahmachari V., Singh Y.;
RT "Loss of kinase activity in Mycobacterium tuberculosis multidomain protein
RT Rv1364c.";
RL FEBS J. 275:6295-6308(2008).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, DOMAIN, PHOSPHORYLATION AT SER-600,
RP AND MUTAGENESIS OF ASP-328; GLU-444; ASN-448; HIS-452 AND SER-600.
RX PubMed=19700407; DOI=10.1074/jbc.m109.056168;
RA Greenstein A.E., Hammel M., Cavazos A., Alber T.;
RT "Interdomain communication in the Mycobacterium tuberculosis environmental
RT phosphatase Rv1364c.";
RL J. Biol. Chem. 284:29828-29835(2009).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, OVEREXPRESSION, INTERACTION WITH SIGF,
RP PHOSPHORYLATION AT THR-54; THR-81; THR-299; THR-390; SER-506; THR-520;
RP THR-568 AND SER-600, AND MUTAGENESIS OF ASP-211; ASP-328; GLU-444; ASN-448
RP AND SER-600.
RX PubMed=30642988; DOI=10.1128/jb.00725-18;
RA Misra R., Menon D., Arora G., Virmani R., Gaur M., Naz S., Jaisinghani N.,
RA Bhaduri A., Bothra A., Maji A., Singhal A., Karwal P., Hentschker C.,
RA Becher D., Rao V., Nandicoori V.K., Gandotra S., Singh Y.;
RT "Tuning the Mycobacterium tuberculosis alternative sigma factor SigF
RT through the multidomain regulator Rv1364c and osmosensory kinase protein
RT kinase D.";
RL J. Bacteriol. 201:0-0(2019).
RN [7] {ECO:0007744|PDB:3KX0}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 1-163.
RX PubMed=20541534; DOI=10.1016/j.bbrc.2010.06.027;
RA Jaiswal R.K., Manjeera G., Gopal B.;
RT "Role of a PAS sensor domain in the Mycobacterium tuberculosis
RT transcription regulator Rv1364c.";
RL Biochem. Biophys. Res. Commun. 398:342-349(2010).
RN [8] {ECO:0007744|PDB:3K3C, ECO:0007744|PDB:3K3D, ECO:0007744|PDB:3KE6}
RP X-RAY CRYSTALLOGRAPHY (1.62 ANGSTROMS) OF 1-147; 1-156 AND 169-539 IN
RP COMPLEX WITH MANGANESE, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBUNIT.
RX PubMed=21220116; DOI=10.1016/j.str.2010.11.010;
RA King-Scott J., Konarev P.V., Panjikar S., Jordanova R., Svergun D.I.,
RA Tucker P.A.;
RT "Structural characterization of the multidomain regulatory protein Rv1364c
RT from Mycobacterium tuberculosis.";
RL Structure 19:56-69(2011).
CC -!- FUNCTION: Primarily acts as an independent SigF regulator that is
CC sensitive to the osmosensory signal, mediating the cross talk of PknD
CC with the SigF regulon (PubMed:30642988). Possesses both phosphatase and
CC kinase activities (PubMed:30642988, PubMed:19700407). The kinase domain
CC functions as a classic anti-sigma factor-like kinase to phosphorylate
CC the anti-anti-sigma factor domain at the canonical regulatory site, and
CC the phosphatase domain antagonizes this activity (PubMed:19700407).
CC {ECO:0000269|PubMed:19700407, ECO:0000269|PubMed:30642988}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.16; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU01082, ECO:0000269|PubMed:19700407,
CC ECO:0000269|PubMed:30642988};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:61977; EC=3.1.3.16; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU01082};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000269|PubMed:19700407, ECO:0000269|PubMed:30642988};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000305};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU01082,
CC ECO:0000269|PubMed:19016841, ECO:0000269|PubMed:19700407,
CC ECO:0000269|PubMed:21220116};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU01082,
CC ECO:0000269|PubMed:19700407};
CC Note=Binds 2 manganese or magnesium ions per subunit.
CC {ECO:0000255|PROSITE-ProRule:PRU01082, ECO:0000269|PubMed:21220116};
CC -!- ACTIVITY REGULATION: The phosphatase domain is activated by the anti-
CC sigma factor kinase domain. {ECO:0000269|PubMed:19700407}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=19.1 mM for pNPP {ECO:0000269|PubMed:19700407};
CC KM=31.2 mM for pNPP {ECO:0000269|PubMed:21220116};
CC Vmax=0.02 umol/min/mg enzyme with pNPP as substrate
CC {ECO:0000269|PubMed:21220116};
CC Note=kcat is 14.2 min(-1) for pNPP hydrolysis.
CC {ECO:0000269|PubMed:19700407};
CC pH dependence:
CC Optimum pH is 8.5 for pNPP hydrolysis (PubMed:19016841). Optimum pH
CC is 8.0 for pNPP hydrolysis (PubMed:19700407).
CC {ECO:0000269|PubMed:19016841, ECO:0000269|PubMed:19700407};
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius for phosphatase activity.
CC {ECO:0000269|PubMed:19016841};
CC -!- SUBUNIT: Exists in solution as both monomer and dimer
CC (PubMed:21220116). Both the phosphorylated and unphosphorylated
CC proteins form extended dimers (PubMed:19700407). Interacts with SigF
CC (PubMed:30642988). Can efficiently bind to SigF independently of its
CC autophosphorylation (PubMed:30642988). Interaction between SigF and
CC Rv1364c is reduced significantly upon the phosphorylation of both
CC proteins by PknD (PubMed:30642988). {ECO:0000269|PubMed:19700407,
CC ECO:0000269|PubMed:21220116, ECO:0000269|PubMed:30642988}.
CC -!- INTERACTION:
CC P9WLZ7; P9WLZ7: Rv1364c; NbExp=5; IntAct=EBI-2602906, EBI-2602906;
CC -!- INDUCTION: Induced by heat stress. {ECO:0000269|PubMed:17485404}.
CC -!- DOMAIN: Multidomain protein in which the components of the entire
CC signal transduction cascade for SigF regulation appear to be encoded in
CC a single polypeptide. Contains an N-terminal PAS sensor domain,
CC followed by an adjacent PAC (PAS domain-associated C-terminus) region,
CC a phosphatase domain, an anti-sigma factor kinase domain, and a C-
CC terminal anti-anti-sigma factor domain (or substrate domain)
CC (Probable). Phosphorylation at Ser-600 leads to a change in the overall
CC shape of the dimer (PubMed:19700407). {ECO:0000269|PubMed:19700407,
CC ECO:0000305|PubMed:19016841, ECO:0000305|PubMed:19700407}.
CC -!- PTM: Autophosphorylated (PubMed:30642988, PubMed:19700407).
CC Phosphorylated by PknD on multiple threonine and serine residues
CC (PubMed:30642988). Phosphorylation is antagonized by the phosphatase
CC activity (PubMed:19700407). {ECO:0000269|PubMed:19700407,
CC ECO:0000269|PubMed:30642988}.
CC -!- MISCELLANEOUS: Overexpression switch off espA induction under osmotic
CC stress. {ECO:0000269|PubMed:30642988}.
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DR EMBL; AL123456; CCP44122.1; -; Genomic_DNA.
DR PIR; C70742; C70742.
DR RefSeq; WP_003916806.1; NZ_NVQJ01000031.1.
DR RefSeq; YP_177802.1; NC_000962.3.
DR PDB; 3K3C; X-ray; 1.62 A; A/B/C/D=1-156.
DR PDB; 3K3D; X-ray; 2.30 A; A=1-147.
DR PDB; 3KE6; X-ray; 2.60 A; A/B=170-539.
DR PDB; 3KX0; X-ray; 2.30 A; X=1-163.
DR PDBsum; 3K3C; -.
DR PDBsum; 3K3D; -.
DR PDBsum; 3KE6; -.
DR PDBsum; 3KX0; -.
DR AlphaFoldDB; P9WLZ7; -.
DR SASBDB; P9WLZ7; -.
DR SMR; P9WLZ7; -.
DR IntAct; P9WLZ7; 5.
DR STRING; 83332.Rv1364c; -.
DR PaxDb; P9WLZ7; -.
DR DNASU; 886802; -.
DR GeneID; 886802; -.
DR KEGG; mtu:Rv1364c; -.
DR TubercuList; Rv1364c; -.
DR eggNOG; COG1366; Bacteria.
DR eggNOG; COG2172; Bacteria.
DR eggNOG; COG2208; Bacteria.
DR OMA; MNFTRWS; -.
DR PhylomeDB; P9WLZ7; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0004035; F:alkaline phosphatase activity; IDA:MTBBASE.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0000287; F:magnesium ion binding; IDA:MTBBASE.
DR GO; GO:0030145; F:manganese ion binding; IDA:MTBBASE.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0016791; F:phosphatase activity; IDA:MTBBASE.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MTBBASE.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR Gene3D; 3.30.750.24; -; 1.
DR Gene3D; 3.60.40.10; -; 1.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR036457; PPM-type_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase_dom.
DR InterPro; IPR002645; STAS_dom.
DR InterPro; IPR036513; STAS_dom_sf.
DR Pfam; PF13581; HATPase_c_2; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF07228; SpoIIE; 1.
DR Pfam; PF13466; STAS_2; 1.
DR SMART; SM00331; PP2C_SIG; 1.
DR SUPFAM; SSF52091; SSF52091; 1.
DR SUPFAM; SSF55785; SSF55785; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR TIGRFAMs; TIGR00229; sensory_box; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS51746; PPM_2; 1.
DR PROSITE; PS50801; STAS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Hydrolase; Kinase; Magnesium; Manganese;
KW Metal-binding; Nucleotide-binding; Phosphoprotein; Protein phosphatase;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..653
FT /note="Multidomain regulatory protein Rv1364c"
FT /id="PRO_0000103833"
FT DOMAIN 86..142
FT /note="PAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00141"
FT DOMAIN 177..396
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT DOMAIN 546..653
FT /note="STAS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00198"
FT REGION 397..544
FT /note="Anti-sigma factor kinase region"
FT /evidence="ECO:0000305|PubMed:19700407"
FT BINDING 211
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:21220116"
FT BINDING 211
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:21220116"
FT BINDING 212
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:21220116"
FT BINDING 328
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:21220116"
FT BINDING 387
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:21220116"
FT MOD_RES 54
FT /note="Phosphothreonine; by PknD"
FT /evidence="ECO:0000269|PubMed:30642988"
FT MOD_RES 81
FT /note="Phosphothreonine; by PknD"
FT /evidence="ECO:0000269|PubMed:30642988"
FT MOD_RES 299
FT /note="Phosphothreonine; by PknD"
FT /evidence="ECO:0000269|PubMed:30642988"
FT MOD_RES 390
FT /note="Phosphothreonine; by PknD"
FT /evidence="ECO:0000269|PubMed:30642988"
FT MOD_RES 506
FT /note="Phosphoserine; by PknD"
FT /evidence="ECO:0000269|PubMed:30642988"
FT MOD_RES 520
FT /note="Phosphothreonine; by PknD"
FT /evidence="ECO:0000269|PubMed:30642988"
FT MOD_RES 568
FT /note="Phosphothreonine; by PknD"
FT /evidence="ECO:0000269|PubMed:30642988"
FT MOD_RES 600
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:30642988"
FT MUTAGEN 211
FT /note="D->A: Does not affect autophosphorylation. 10-fold
FT decrease in phosphatase activity."
FT /evidence="ECO:0000269|PubMed:19016841,
FT ECO:0000269|PubMed:30642988"
FT MUTAGEN 328
FT /note="D->A: Leads to the accumulation of the
FT autophosphorylated protein. 10-fold decrease in phosphatase
FT activity."
FT /evidence="ECO:0000269|PubMed:19016841,
FT ECO:0000269|PubMed:19700407, ECO:0000269|PubMed:30642988"
FT MUTAGEN 444
FT /note="E->A: Strong decrease in ATPase activity. Abolishes
FT autophosphorylation."
FT /evidence="ECO:0000269|PubMed:30642988"
FT MUTAGEN 444
FT /note="E->K: Abolishes autophosphorylation."
FT /evidence="ECO:0000269|PubMed:19700407"
FT MUTAGEN 448
FT /note="N->A: Strong decrease in ATPase activity. Abolishes
FT autophosphorylation."
FT /evidence="ECO:0000269|PubMed:30642988"
FT MUTAGEN 448
FT /note="N->K: Abolishes autophosphorylation."
FT /evidence="ECO:0000269|PubMed:19700407"
FT MUTAGEN 452
FT /note="H->A: Abolishes autophosphorylation."
FT /evidence="ECO:0000269|PubMed:19700407"
FT MUTAGEN 600
FT /note="S->A: Decreases ATPase activity. Abolishes
FT autophosphorylation. Can still be phosphorylated by PknD."
FT /evidence="ECO:0000269|PubMed:19700407,
FT ECO:0000269|PubMed:30642988"
FT MUTAGEN 600
FT /note="S->E: Does not affect ATPase activity. Abolishes
FT autophosphorylation."
FT /evidence="ECO:0000269|PubMed:30642988"
FT HELIX 7..10
FT /evidence="ECO:0007829|PDB:3K3C"
FT HELIX 14..23
FT /evidence="ECO:0007829|PDB:3K3C"
FT STRAND 25..32
FT /evidence="ECO:0007829|PDB:3K3C"
FT TURN 33..36
FT /evidence="ECO:0007829|PDB:3K3C"
FT STRAND 37..41
FT /evidence="ECO:0007829|PDB:3K3C"
FT HELIX 43..48
FT /evidence="ECO:0007829|PDB:3K3C"
FT HELIX 59..62
FT /evidence="ECO:0007829|PDB:3K3C"
FT HELIX 64..68
FT /evidence="ECO:0007829|PDB:3K3C"
FT HELIX 71..81
FT /evidence="ECO:0007829|PDB:3K3C"
FT STRAND 85..99
FT /evidence="ECO:0007829|PDB:3K3C"
FT STRAND 101..114
FT /evidence="ECO:0007829|PDB:3K3C"
FT STRAND 120..129
FT /evidence="ECO:0007829|PDB:3K3C"
FT HELIX 131..149
FT /evidence="ECO:0007829|PDB:3K3C"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:3KE6"
FT STRAND 176..183
FT /evidence="ECO:0007829|PDB:3KE6"
FT STRAND 185..188
FT /evidence="ECO:0007829|PDB:3KE6"
FT STRAND 193..200
FT /evidence="ECO:0007829|PDB:3KE6"
FT STRAND 202..211
FT /evidence="ECO:0007829|PDB:3KE6"
FT HELIX 217..235
FT /evidence="ECO:0007829|PDB:3KE6"
FT HELIX 240..250
FT /evidence="ECO:0007829|PDB:3KE6"
FT HELIX 251..253
FT /evidence="ECO:0007829|PDB:3KE6"
FT STRAND 261..268
FT /evidence="ECO:0007829|PDB:3KE6"
FT TURN 269..271
FT /evidence="ECO:0007829|PDB:3KE6"
FT STRAND 273..281
FT /evidence="ECO:0007829|PDB:3KE6"
FT STRAND 285..287
FT /evidence="ECO:0007829|PDB:3KE6"
FT STRAND 293..295
FT /evidence="ECO:0007829|PDB:3KE6"
FT STRAND 313..316
FT /evidence="ECO:0007829|PDB:3KE6"
FT STRAND 322..326
FT /evidence="ECO:0007829|PDB:3KE6"
FT TURN 328..331
FT /evidence="ECO:0007829|PDB:3KE6"
FT HELIX 338..352
FT /evidence="ECO:0007829|PDB:3KE6"
FT HELIX 367..381
FT /evidence="ECO:0007829|PDB:3KE6"
FT STRAND 389..396
FT /evidence="ECO:0007829|PDB:3KE6"
FT STRAND 403..407
FT /evidence="ECO:0007829|PDB:3KE6"
FT HELIX 413..428
FT /evidence="ECO:0007829|PDB:3KE6"
FT HELIX 432..452
FT /evidence="ECO:0007829|PDB:3KE6"
FT STRAND 462..468
FT /evidence="ECO:0007829|PDB:3KE6"
FT STRAND 472..481
FT /evidence="ECO:0007829|PDB:3KE6"
FT HELIX 498..502
FT /evidence="ECO:0007829|PDB:3KE6"
FT STRAND 505..513
FT /evidence="ECO:0007829|PDB:3KE6"
FT STRAND 516..524
FT /evidence="ECO:0007829|PDB:3KE6"
FT STRAND 526..528
FT /evidence="ECO:0007829|PDB:3KE6"
SQ SEQUENCE 653 AA; 69524 MW; 51F29AA39D9C8B9F CRC64;
MAAEMDWDKT VGAAEDVRRI FEHIPAILVG LEGPDHRFVA VNAAYRGFSP LLDTVGQPAR
EVYPELEGQQ IYEMLDRVYQ TGEPQSGSEW RLQTDYDGSG VEERYFDFVV TPRRRADGSI
EGVQLIVDDV TSRVRARQAA EARVEELSER YRNVRDSATV MQQALLAASV PVVPGADIAA
EYLVAAEDTA AGGDWFDALA LGDRLVLVVG DVVGHGVEAA AVMSQLRTAL RMQISAGYTV
VEALEAVDRF HKQVPGSKSA TMCVGSLDFT SGEFQYCTAG HPPPLLVTAD ASARYVEPTG
AGPLGSGTGF PVRSEVLNIG DAILFYTDGL IERPGRPLEA STAEFADLAA SIASGSGGFV
LDAPARPIDR LCSDTLELLL RSTGYNDDVT LLAMQRRAPT PPLHITLDAT INAARTVRAQ
LREWLAEIGA DHSDIADIVH AISEFVENAV EHGYATDVSK GIVVAAALAG DGNVRASVID
RGQWKDHRDG ARGRGRGLAM AEALVSEARI MHGAGGTTAT LTHRLSRPAR FVTDTMVRRA
AFQQTIDSEF VSLVESGRIV VRGDVDSTTA ATLDRQIAVE SRSGIAPVTI DLSAVTHLGS
AGVGALAAAC DRARKQGTEC VLVAPPGSPA HHVLSLVQLP VVGADTEDIF AQE
