PTM3C_ECOLI
ID PTM3C_ECOLI Reviewed; 637 AA.
AC P00550; Q2M7R2;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 215.
DE RecName: Full=PTS system mannitol-specific EIICBA component {ECO:0000303|PubMed:368051};
DE AltName: Full=EIICBA-Mtl {ECO:0000303|PubMed:368051};
DE Short=EII-Mtl {ECO:0000303|PubMed:368051};
DE Includes:
DE RecName: Full=Mannitol permease IIC component {ECO:0000303|PubMed:368051};
DE AltName: Full=PTS system mannitol-specific EIIC component {ECO:0000303|PubMed:368051};
DE Includes:
DE RecName: Full=Mannitol-specific phosphotransferase enzyme IIB component {ECO:0000303|PubMed:368051};
DE EC=2.7.1.197 {ECO:0000269|PubMed:2123863, ECO:0000305|PubMed:368051};
DE AltName: Full=PTS system mannitol-specific EIIB component {ECO:0000303|PubMed:368051};
DE Includes:
DE RecName: Full=Mannitol-specific phosphotransferase enzyme IIA component {ECO:0000303|PubMed:368051};
DE AltName: Full=PTS system mannitol-specific EIIA component {ECO:0000303|PubMed:368051};
GN Name=mtlA {ECO:0000303|PubMed:368051}; OrderedLocusNames=b3599, JW3573;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBCELLULAR LOCATION.
RX PubMed=6309813; DOI=10.1016/s0021-9258(17)44522-4;
RA Lee C.A., Saier M.H. Jr.;
RT "Mannitol-specific enzyme II of the bacterial phosphotransferase system.
RT III. The nucleotide sequence of the permease gene.";
RL J. Biol. Chem. 258:10761-10767(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8041620; DOI=10.1093/nar/22.13.2576;
RA Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.;
RT "Analysis of the Escherichia coli genome. V. DNA sequence of the region
RT from 76.0 to 81.5 minutes.";
RL Nucleic Acids Res. 22:2576-2586(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 619-637.
RC STRAIN=K12;
RX PubMed=3135464; DOI=10.1111/j.1365-2958.1988.tb00045.x;
RA Davis T., Yamada M., Elgort M., Saier M.H. Jr.;
RT "Nucleotide sequence of the mannitol (mtl) operon in Escherichia coli.";
RL Mol. Microbiol. 2:405-412(1988).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=368051; DOI=10.1016/s0021-9258(17)37905-x;
RA Jacobson G.R., Lee C.A., Saier M.H. Jr.;
RT "Purification of the mannitol-specific enzyme II of the Escherichia coli
RT phosphoenolpyruvate:sugar phosphotransferase system.";
RL J. Biol. Chem. 254:249-252(1979).
RN [7]
RP FUNCTION, AND SUBSTRATE SPECIFICITY.
RX PubMed=6427236; DOI=10.1002/jcb.240230120;
RA Jacobson G.R., Tanney L.E., Kelly D.M., Palman K.B., Corn S.B.;
RT "Substrate and phospholipid specificity of the purified mannitol permease
RT of Escherichia coli.";
RL J. Cell. Biochem. 23:231-240(1983).
RN [8]
RP SUBUNIT.
RX PubMed=3322385; DOI=10.1021/bi00395a019;
RA Pas H.H., Ellory J.C., Robillard G.T.;
RT "Bacterial phosphoenolpyruvate-dependent phosphotransferase system:
RT association state of membrane-bound mannitol-specific enzyme II
RT demonstrated by inactivation.";
RL Biochemistry 26:6689-6696(1987).
RN [9]
RP PHOSPHORYLATION AT CYS-384 AND HIS-554.
RX PubMed=3142516; DOI=10.1021/bi00416a002;
RA Pas H.H., Robillard G.T.;
RT "S-phosphocysteine and phosphohistidine are intermediates in the
RT phosphoenolpyruvate-dependent mannitol transport catalyzed by Escherichia
RT coli EIIMtl.";
RL Biochemistry 27:5835-5839(1988).
RN [10]
RP PHOSPHORYLATION AT CYS-384 AND HIS-554.
RX PubMed=2407724; DOI=10.1128/jb.172.3.1509-1515.1990;
RA White D.W., Jacobson G.R.;
RT "Molecular cloning of the C-terminal domain of Escherichia coli D-mannitol
RT permease: expression, phosphorylation, and complementation with C-terminal
RT permease deletion proteins.";
RL J. Bacteriol. 172:1509-1515(1990).
RN [11]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=2123863; DOI=10.1128/jb.172.12.7119-7125.1990;
RA Elferink M.G., Driessen A.J., Robillard G.T.;
RT "Functional reconstitution of the purified phosphoenolpyruvate-dependent
RT mannitol-specific transport system of Escherichia coli in phospholipid
RT vesicles: coupling between transport and phosphorylation.";
RL J. Bacteriol. 172:7119-7125(1990).
RN [12]
RP TOPOLOGY.
RX PubMed=1946374; DOI=10.1073/pnas.88.21.9603;
RA Sugiyama J.E., Mahmoodian S., Jacobson G.R.;
RT "Membrane topology analysis of Escherichia coli mannitol permease by using
RT a nested-deletion method to create mtlA-phoA fusions.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:9603-9607(1991).
RN [13]
RP INDUCTION.
RX PubMed=8300537; DOI=10.1128/jb.176.3.840-847.1994;
RA Figge R.M., Ramseier T.M., Saier M.H. Jr.;
RT "The mannitol repressor (MtlR) of Escherichia coli.";
RL J. Bacteriol. 176:840-847(1994).
RN [14]
RP SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 490-637 IN COMPLEX WITH THE
RP HISTIDINE PHOSPHOCARRIER PROTEIN HPR, AND ACTIVE SITE.
RX PubMed=9551558; DOI=10.1016/s0969-2126(98)00039-2;
RA van Montfort R.L.M., Pijning T., Kalk K.H., Hangyi I., Kouwijzer M.L.C.E.,
RA Robillard G.T., Dijkstra B.W.;
RT "The structure of the Escherichia coli phosphotransferase IIAmannitol
RT reveals a novel fold with two conformations of the active site.";
RL Structure 6:377-388(1998).
RN [16]
RP STRUCTURE BY NMR OF 491-637 IN COMPLEX WITH THE HISTIDINE PHOSPHOCARRIER
RP PROTEIN HPR, AND ACTIVE SITE.
RX PubMed=12202490; DOI=10.1074/jbc.m207314200;
RA Cornilescu G., Lee B.R., Cornilescu C.C., Wang G., Peterkofsky A.,
RA Clore G.M.;
RT "Solution structure of the phosphoryl transfer complex between the
RT cytoplasmic A domain of the mannitol transporter IIMannitol and HPr of the
RT Escherichia coli phosphotransferase system.";
RL J. Biol. Chem. 277:42289-42298(2002).
RN [17]
RP STRUCTURE BY NMR OF 367-489, AND ACTIVE SITE.
RX PubMed=15258141; DOI=10.1074/jbc.m406764200;
RA Legler P.M., Cai M., Peterkofsky A., Clore G.M.;
RT "Three-dimensional solution structure of the cytoplasmic B domain of the
RT mannitol transporter IImannitol of the Escherichia coli phosphotransferase
RT system.";
RL J. Biol. Chem. 279:39115-39121(2004).
RN [18]
RP STRUCTURE BY NMR OF 491-637 OF MUTANT GLN-554 AND 375-475 OF MUTANT
RP SER-384, ACTIVE SITE, AND REACTION MECHANISM.
RX PubMed=16443929; DOI=10.1074/jbc.m513466200;
RA Suh J.Y., Cai M., Williams D.C. Jr., Clore G.M.;
RT "Solution structure of a post-transition state analog of the
RT phosphotransfer reaction between the A and B cytoplasmic domains of the
RT mannitol transporter IIMannitol of the Escherichia coli phosphotransferase
RT system.";
RL J. Biol. Chem. 281:8939-8949(2006).
CC -!- FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase
CC system (sugar PTS), a major carbohydrate active transport system,
CC catalyzes the phosphorylation of incoming sugar substrates
CC concomitantly with their translocation across the cell membrane. This
CC system is involved in D-mannitol transport (PubMed:368051,
CC PubMed:6427236, PubMed:2123863). Also able to use D-mannonic acid
CC (PubMed:6427236). {ECO:0000269|PubMed:2123863,
CC ECO:0000269|PubMed:368051, ECO:0000269|PubMed:6427236}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-mannitol(out) + N(pros)-phospho-L-histidyl-[protein] = D-
CC mannitol 1-phosphate(in) + L-histidyl-[protein];
CC Xref=Rhea:RHEA:33363, Rhea:RHEA-COMP:9745, Rhea:RHEA-COMP:9746,
CC ChEBI:CHEBI:16899, ChEBI:CHEBI:29979, ChEBI:CHEBI:61381,
CC ChEBI:CHEBI:64837; EC=2.7.1.197;
CC Evidence={ECO:0000269|PubMed:2123863, ECO:0000305|PubMed:368051};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=66 uM for mannitol phosphorylation {ECO:0000269|PubMed:2123863};
CC Vmax=21.7 nmol/min/mg enzyme toward mannitol
CC {ECO:0000269|PubMed:2123863};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:3322385}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00427, ECO:0000269|PubMed:15919996,
CC ECO:0000305|PubMed:6309813}; Multi-pass membrane protein
CC {ECO:0000255|PROSITE-ProRule:PRU00427, ECO:0000269|PubMed:15919996,
CC ECO:0000305|PubMed:368051}.
CC -!- INDUCTION: Induced by mannitol. Repressed by MltR.
CC {ECO:0000269|PubMed:8300537}.
CC -!- DOMAIN: The EIIC type-2 domain forms the PTS system translocation
CC channel and contains the specific substrate-binding site.
CC {ECO:0000255|PROSITE-ProRule:PRU00427}.
CC -!- DOMAIN: The PTS EIIB type-2 domain is phosphorylated by phospho-EIIA on
CC a cysteinyl residue. Then, it transfers the phosphoryl group to the
CC sugar substrate concomitantly with the sugar uptake processed by the
CC PTS EIIC type-2 domain. {ECO:0000255|PROSITE-ProRule:PRU00422}.
CC -!- DOMAIN: The PTS EIIA type-2 domain is phosphorylated by phospho-HPr on
CC a histidyl residue. Then, it transfers the phosphoryl group to the PTS
CC EIIB type-2 domain. {ECO:0000255|PROSITE-ProRule:PRU00417}.
CC -!- PTM: An intramolecular phosphotransfer takes places between His-554 and
CC Cys-384. {ECO:0000305|PubMed:16443929}.
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DR EMBL; V01503; CAA24748.1; -; Genomic_DNA.
DR EMBL; U00039; AAB18576.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76623.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77694.1; -; Genomic_DNA.
DR EMBL; X06794; CAA29953.1; -; Genomic_DNA.
DR PIR; A00661; WQEC2M.
DR RefSeq; NP_418056.1; NC_000913.3.
DR RefSeq; WP_000093247.1; NZ_SSZK01000022.1.
DR PDB; 1A3A; X-ray; 1.80 A; A/B/C/D=491-637.
DR PDB; 1J6T; NMR; -; A=491-637.
DR PDB; 1VKR; NMR; -; A=367-489.
DR PDB; 1VRV; NMR; -; A=375-475.
DR PDB; 2FEW; NMR; -; A=491-637, B=375-475.
DR PDBsum; 1A3A; -.
DR PDBsum; 1J6T; -.
DR PDBsum; 1VKR; -.
DR PDBsum; 1VRV; -.
DR PDBsum; 2FEW; -.
DR AlphaFoldDB; P00550; -.
DR BMRB; P00550; -.
DR SMR; P00550; -.
DR BioGRID; 4260741; 18.
DR DIP; DIP-10267N; -.
DR IntAct; P00550; 3.
DR MINT; P00550; -.
DR STRING; 511145.b3599; -.
DR TCDB; 4.A.2.1.2; the pts fructose-mannitol (fru) family.
DR iPTMnet; P00550; -.
DR jPOST; P00550; -.
DR PaxDb; P00550; -.
DR PRIDE; P00550; -.
DR EnsemblBacteria; AAC76623; AAC76623; b3599.
DR EnsemblBacteria; BAE77694; BAE77694; BAE77694.
DR GeneID; 66672506; -.
DR GeneID; 948118; -.
DR KEGG; ecj:JW3573; -.
DR KEGG; eco:b3599; -.
DR PATRIC; fig|1411691.4.peg.3108; -.
DR EchoBASE; EB0610; -.
DR eggNOG; COG2213; Bacteria.
DR eggNOG; COG4668; Bacteria.
DR HOGENOM; CLU_028721_1_0_6; -.
DR InParanoid; P00550; -.
DR OMA; GWAIKRF; -.
DR PhylomeDB; P00550; -.
DR BioCyc; EcoCyc:MTLA-MON; -.
DR BioCyc; MetaCyc:MTLA-MON; -.
DR BRENDA; 2.7.1.197; 2026.
DR SABIO-RK; P00550; -.
DR EvolutionaryTrace; P00550; -.
DR PRO; PR:P00550; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0022872; F:protein-N(PI)-phosphohistidine-mannitol phosphotransferase system transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0090565; F:protein-phosphocysteine-mannitol phosphotransferase system transporter activity; IDA:EcoCyc.
DR GO; GO:0090563; F:protein-phosphocysteine-sugar phosphotransferase activity; IBA:GO_Central.
DR GO; GO:0015797; P:mannitol transmembrane transport; IDA:EcoCyc.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IDA:EcoCyc.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00211; PTS_IIA_fru; 1.
DR CDD; cd05567; PTS_IIB_mannitol; 1.
DR Gene3D; 3.40.930.10; -; 1.
DR InterPro; IPR016152; PTrfase/Anion_transptr.
DR InterPro; IPR002178; PTS_EIIA_type-2_dom.
DR InterPro; IPR036095; PTS_EIIB-like_sf.
DR InterPro; IPR013011; PTS_EIIB_2.
DR InterPro; IPR003501; PTS_EIIB_2/3.
DR InterPro; IPR029503; PTS_EIIB_mannitol.
DR InterPro; IPR003352; PTS_EIIC.
DR InterPro; IPR013014; PTS_EIIC_2.
DR InterPro; IPR004718; PTS_IIC_mtl.
DR Pfam; PF00359; PTS_EIIA_2; 1.
DR Pfam; PF02378; PTS_EIIC; 1.
DR Pfam; PF02302; PTS_IIB; 1.
DR SUPFAM; SSF52794; SSF52794; 1.
DR SUPFAM; SSF55804; SSF55804; 1.
DR TIGRFAMs; TIGR00851; mtlA; 1.
DR PROSITE; PS51094; PTS_EIIA_TYPE_2; 1.
DR PROSITE; PS00372; PTS_EIIA_TYPE_2_HIS; 1.
DR PROSITE; PS51099; PTS_EIIB_TYPE_2; 1.
DR PROSITE; PS51104; PTS_EIIC_TYPE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Kinase; Membrane;
KW Phosphoprotein; Phosphotransferase system; Reference proteome;
KW Sugar transport; Transferase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..637
FT /note="PTS system mannitol-specific EIICBA component"
FT /id="PRO_0000186614"
FT TOPO_DOM 1..23
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:1946374"
FT TRANSMEM 24..45
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:1946374"
FT TOPO_DOM 46..49
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:1946374"
FT TRANSMEM 50..70
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:1946374"
FT TOPO_DOM 71..133
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:1946374"
FT TRANSMEM 134..155
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:1946374"
FT TOPO_DOM 156..164
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:1946374"
FT TRANSMEM 165..185
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:1946374"
FT TOPO_DOM 186..272
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:1946374"
FT TRANSMEM 273..292
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:1946374"
FT TOPO_DOM 293..312
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:1946374"
FT TRANSMEM 313..334
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:1946374"
FT TOPO_DOM 335..637
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:1946374"
FT DOMAIN 12..341
FT /note="PTS EIIC type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT DOMAIN 378..473
FT /note="PTS EIIB type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00422"
FT DOMAIN 494..636
FT /note="PTS EIIA type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00417"
FT ACT_SITE 384
FT /note="Phosphocysteine intermediate; for EIIB activity"
FT /evidence="ECO:0000305|PubMed:15258141,
FT ECO:0000305|PubMed:16443929"
FT ACT_SITE 554
FT /note="Tele-phosphohistidine intermediate; for EIIA
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00417,
FT ECO:0000305|PubMed:12202490, ECO:0000305|PubMed:16443929,
FT ECO:0000305|PubMed:9551558"
FT SITE 538
FT /note="Stabilizes the transition state in the phosphoryl
FT transfer from HPr to EIIA"
FT /evidence="ECO:0000269|PubMed:9551558"
FT MOD_RES 384
FT /note="Phosphocysteine; by EIIA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00422,
FT ECO:0000269|PubMed:3142516, ECO:0000305|PubMed:15258141,
FT ECO:0000305|PubMed:16443929, ECO:0000305|PubMed:2407724"
FT MOD_RES 554
FT /note="Phosphohistidine; by HPr"
FT /evidence="ECO:0000269|PubMed:3142516,
FT ECO:0000305|PubMed:12202490, ECO:0000305|PubMed:16443929,
FT ECO:0000305|PubMed:2407724, ECO:0000305|PubMed:9551558"
FT STRAND 379..382
FT /evidence="ECO:0007829|PDB:1VKR"
FT STRAND 385..388
FT /evidence="ECO:0007829|PDB:1VKR"
FT HELIX 389..404
FT /evidence="ECO:0007829|PDB:1VKR"
FT STRAND 410..414
FT /evidence="ECO:0007829|PDB:1VKR"
FT STRAND 425..430
FT /evidence="ECO:0007829|PDB:1VKR"
FT HELIX 431..440
FT /evidence="ECO:0007829|PDB:1VKR"
FT STRAND 444..450
FT /evidence="ECO:0007829|PDB:1VKR"
FT HELIX 455..470
FT /evidence="ECO:0007829|PDB:1VKR"
FT HELIX 498..500
FT /evidence="ECO:0007829|PDB:1A3A"
FT HELIX 510..523
FT /evidence="ECO:0007829|PDB:1A3A"
FT HELIX 530..541
FT /evidence="ECO:0007829|PDB:1A3A"
FT STRAND 545..547
FT /evidence="ECO:0007829|PDB:1A3A"
FT HELIX 557..562
FT /evidence="ECO:0007829|PDB:1A3A"
FT STRAND 563..565
FT /evidence="ECO:0007829|PDB:1A3A"
FT STRAND 567..578
FT /evidence="ECO:0007829|PDB:1A3A"
FT STRAND 580..582
FT /evidence="ECO:0007829|PDB:1A3A"
FT STRAND 586..594
FT /evidence="ECO:0007829|PDB:1A3A"
FT TURN 597..599
FT /evidence="ECO:0007829|PDB:1A3A"
FT HELIX 600..610
FT /evidence="ECO:0007829|PDB:1A3A"
FT HELIX 614..622
FT /evidence="ECO:0007829|PDB:1A3A"
FT HELIX 626..632
FT /evidence="ECO:0007829|PDB:1A3A"
FT TURN 633..635
FT /evidence="ECO:0007829|PDB:1A3A"
SQ SEQUENCE 637 AA; 67972 MW; A992992D534BF98D CRC64;
MSSDIKIKVQ SFGRFLSNMV MPNIGAFIAW GIITALFIPT GWLPNETLAK LVGPMITYLL
PLLIGYTGGK LVGGERGGVV GAITTMGVIV GADMPMFLGS MIAGPLGGWC IKHFDRWVDG
KIKSGFEMLV NNFSAGIIGM ILAILAFLGI GPIVEALSKM LAAGVNFMVV HDMLPLASIF
VEPAKILFLN NAINHGIFSP LGIQQSHELG KSIFFLIEAN PGPGMGVLLA YMFFGRGSAK
QSAGGAAIIH FLGGIHEIYF PYVLMNPRLI LAVILGGMTG VFTLTILGGG LVSPASPGSI
LAVLAMTPKG AYFANIAGVC AAMAVSFVVS AILLKTSKVK EEDDIEAATR RMQDMKAESK
GASPLSAGDV TNDLSHVRKI IVACDAGMGS SAMGAGVLRK KIQDAGLSQI SVTNSAINNL
PPDVDLVITH RDLTERAMRQ VPQAQHISLT NFLDSGLYTS LTERLVAAQR HTANEEKVKD
SLKDSFDDSS ANLFKLGAEN IFLGRKAATK EEAIRFAGEQ LVKGGYVEPE YVQAMLDREK
LTPTYLGESI AVPHGTVEAK DRVLKTGVVF CQYPEGVRFG EEEDDIARLV IGIAARNNEH
IQVITSLTNA LDDESVIERL AHTTSVDEVL ELLAGRK
