ID   COAD_ECOLI              Reviewed;         159 AA.
AC   P0A6I6; P23875; Q2M7U8;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   29-MAR-2005, sequence version 1.
DT   27-MAR-2024, entry version 148.
DE   RecName: Full=Phosphopantetheine adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_00151, ECO:0000303|PubMed:10480925};
DE            EC=2.7.7.3 {ECO:0000255|HAMAP-Rule:MF_00151, ECO:0000269|PubMed:10480925, ECO:0000269|PubMed:17873050};
DE   AltName: Full=Dephospho-CoA pyrophosphorylase {ECO:0000255|HAMAP-Rule:MF_00151};
DE   AltName: Full=Pantetheine-phosphate adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_00151};
DE            Short=PPAT {ECO:0000255|HAMAP-Rule:MF_00151, ECO:0000303|PubMed:10480925};
GN   Name=coaD {ECO:0000255|HAMAP-Rule:MF_00151,
GN   ECO:0000303|PubMed:10480925};
GN   Synonyms=kdtB {ECO:0000303|PubMed:1577693}, yicA;
GN   OrderedLocusNames=b3634, JW3609;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RX   PubMed=2033061; DOI=10.1016/s0021-9258(18)92875-9;
RA   Clementz T., Raetz C.R.H.;
RT   "A gene coding for 3-deoxy-D-manno-octulosonic-acid transferase in
RT   Escherichia coli. Identification, mapping, cloning, and sequencing.";
RL   J. Biol. Chem. 266:9687-9696(1991).
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   PROTEIN SEQUENCE OF 1-10, FUNCTION, CATALYTIC ACTIVITY, POSSIBLE ACTIVITY
RP   REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND COA-BINDING.
RC   STRAIN=K12 / JM101 / ATCC 33876 / DSM 3948 / NCIMB 11926;
RX   PubMed=10480925; DOI=10.1074/jbc.274.38.27105;
RA   Geerlof A., Lewendon A., Shaw W.V.;
RT   "Purification and characterization of phosphopantetheine
RT   adenylyltransferase from Escherichia coli.";
RL   J. Biol. Chem. 274:27105-27111(1999).
RN   [6]
RP   GENETIC CHARACTERIZATION.
RC   STRAIN=K12;
RX   PubMed=1577693; DOI=10.1128/jb.174.10.3250-3260.1992;
RA   Roncero C., Casadaban M.J.;
RT   "Genetic analysis of the genes involved in synthesis of the
RT   lipopolysaccharide core in Escherichia coli K-12: three operons in the rfa
RT   locus.";
RL   J. Bacteriol. 174:3250-3260(1992).
RN   [7]
RP   ACTIVITY REGULATION.
RX   PubMed=12750020; DOI=10.1016/s0223-5234(03)00047-3;
RA   Zhao L., Allanson N.M., Thomson S.P., Maclean J.K., Barker J.J.,
RA   Primrose W.U., Tyler P.D., Lewendon A.;
RT   "Inhibitors of phosphopantetheine adenylyltransferase.";
RL   Eur. J. Med. Chem. 38:345-349(2003).
RN   [8]
RP   FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP   PROPERTIES, SUBUNIT, AND COA-BINDING.
RC   STRAIN=K12 / JL4;
RX   PubMed=17873050; DOI=10.1128/jb.00732-07;
RA   Miller J.R., Ohren J., Sarver R.W., Mueller W.T., de Dreu P., Case H.,
RA   Thanabal V.;
RT   "Phosphopantetheine adenylyltransferase from Escherichia coli:
RT   investigation of the kinetic mechanism and role in regulation of coenzyme A
RT   biosynthesis.";
RL   J. Bacteriol. 189:8196-8205(2007).
RN   [9]
RP   ACTIVITY REGULATION, AND INHIBITOR SCREENING.
RX   PubMed=20486930; DOI=10.1111/j.1747-0285.2010.00957.x;
RA   Miller J.R., Thanabal V., Melnick M.M., Lall M., Donovan C., Sarver R.W.,
RA   Lee D.Y., Ohren J., Emerson D.;
RT   "The use of biochemical and biophysical tools for triage of high-throughput
RT   screening hits - A case study with Escherichia coli phosphopantetheine
RT   adenylyltransferase.";
RL   Chem. Biol. Drug Des. 75:444-454(2010).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH 3'-DEPHOSPHO-COA, AND
RP   SUBUNIT.
RX   PubMed=10205156; DOI=10.1093/emboj/18.8.2021;
RA   Izard T., Geerlof A.;
RT   "The crystal structure of a novel bacterial adenylyltransferase reveals
RT   half of sites reactivity.";
RL   EMBO J. 18:2021-2030(1999).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (1.63 ANGSTROMS) IN COMPLEXES WITH ATP OR
RP   4'-PHOSPHOPANTETHEINE, COFACTOR, REACTION MECHANISM, SITE, AND SUBUNIT.
RX   PubMed=11812124; DOI=10.1006/jmbi.2001.5272;
RA   Izard T.;
RT   "The crystal structures of phosphopantetheine adenylyltransferase with
RT   bound substrates reveal the enzyme's catalytic mechanism.";
RL   J. Mol. Biol. 315:487-495(2002).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (1.78 ANGSTROMS) IN COMPLEX WITH COENZYME A AND
RP   4'-PHOSPHOPANTETHEINE, ACTIVITY REGULATION, AND SUBUNIT.
RX   PubMed=12837781; DOI=10.1128/jb.185.14.4074-4080.2003;
RA   Izard T.;
RT   "A novel adenylate binding site confers phosphopantetheine
RT   adenylyltransferase interactions with coenzyme A.";
RL   J. Bacteriol. 185:4074-4080(2003).
RN   [13]
RP   X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS).
RX   PubMed=27130242; DOI=10.1007/s10858-016-0032-2;
RA   Proudfoot A., Frank A.O., Ruggiu F., Mamo M., Lingel A.;
RT   "Facilitating unambiguous NMR assignments and enabling higher probe density
RT   through selective labeling of all methyl containing amino acids.";
RL   J. Biomol. NMR 65:15-27(2016).
CC   -!- FUNCTION: Reversibly transfers an adenylyl group from ATP to 4'-
CC       phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate
CC       (PubMed:10480925, PubMed:17873050). CoA is not a substrate for the
CC       enzyme (PubMed:10480925). {ECO:0000255|HAMAP-Rule:MF_00151,
CC       ECO:0000269|PubMed:10480925, ECO:0000269|PubMed:17873050}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-4'-phosphopantetheine + ATP + H(+) = 3'-dephospho-CoA +
CC         diphosphate; Xref=Rhea:RHEA:19801, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57328,
CC         ChEBI:CHEBI:61723; EC=2.7.7.3; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00151, ECO:0000269|PubMed:10480925,
CC         ECO:0000269|PubMed:17873050};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:11812124};
CC       Note=Crystallized in the absence of Mg(2+), the catalytic metal is not
CC       bound by the protein but probably by non-esterified oxygen atoms from
CC       ATP and/or ordered H(2)O (PubMed:11812124).
CC       {ECO:0000305|PubMed:11812124};
CC   -!- ACTIVITY REGULATION: Feedback inhibited by CoA, which is competitive
CC       with ATP, 4'-phosphopantetheine and 3'-dephospho-CoA (PubMed:17873050,
CC       PubMed:10480925). Binds 0.5 CoA tightly per monomer in the same
CC       position as 3'-dephospho-CoA but in a different fashion
CC       (PubMed:12837781, PubMed:17873050). Is inhibited by the very potent and
CC       specific inhibitor PTX042695 dipeptide, with an IC(50) of 6 nM, a
CC       compound which has no activity against porcine PPAT (PubMed:12750020).
CC       A series of pyrazoloquinolones were also characterized as ATP-
CC       competitive inhibitors of PPAT (PubMed:20486930).
CC       {ECO:0000269|PubMed:12750020, ECO:0000269|PubMed:12837781,
CC       ECO:0000269|PubMed:17873050, ECO:0000269|PubMed:20486930,
CC       ECO:0000305|PubMed:10480925}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=7 uM for 3'-dephospho-CoA {ECO:0000269|PubMed:10480925};
CC         KM=17 uM for 3'-dephospho-CoA {ECO:0000269|PubMed:17873050};
CC         KM=0.22 mM for diphosphate {ECO:0000269|PubMed:10480925};
CC         KM=0.23 mM for diphosphate {ECO:0000269|PubMed:17873050};
CC         KM=220 uM for ATP {ECO:0000269|PubMed:17873050};
CC         KM=4.7 uM for 4'-phosphopantetheine {ECO:0000269|PubMed:17873050};
CC         Note=kcat is 1.37 sec(-1) for the forward reaction, with ATP and
CC         pantetheine 4'-phosphate as substrates (PubMed:17873050). kcat is 3.3
CC         sec(-1) for the reverse reaction, with diphosphate and
CC         3'-dephospho-CoA as substrates (PubMed:10480925). kcat is 1.37
CC         sec(-1) for the reverse reaction, with diphosphate and
CC         3'-dephospho-CoA as substrates (PubMed:17873050).
CC         {ECO:0000269|PubMed:10480925, ECO:0000269|PubMed:17873050};
CC       pH dependence:
CC         Optimum pH is 6.9. {ECO:0000269|PubMed:10480925};
CC   -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-
CC       pantothenate: step 4/5. {ECO:0000255|HAMAP-Rule:MF_00151}.
CC   -!- SUBUNIT: Homohexamer, a dimerized trimer with a solvent channel through
CC       the middle (PubMed:10480925, PubMed:10205156, PubMed:11812124,
CC       PubMed:12837781, PubMed:17873050). In crystals only 1 trimer is seen to
CC       bind substrate/product at a time (PubMed:10205156, PubMed:11812124).
CC       {ECO:0000269|PubMed:10205156, ECO:0000269|PubMed:10480925,
CC       ECO:0000269|PubMed:11812124, ECO:0000269|PubMed:12837781,
CC       ECO:0000269|PubMed:17873050}.
CC   -!- INTERACTION:
CC       P0A6I6; P60723: rplD; NbExp=2; IntAct=EBI-553173, EBI-545597;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00151}.
CC   -!- MISCELLANEOUS: The crystal structures in complex with substrates
CC       suggest the enzyme stabilizes the transition state but the functional
CC       groups of the enzyme are not directly involved in reaction catalysis.
CC       {ECO:0000305|PubMed:11812124}.
CC   -!- SIMILARITY: Belongs to the bacterial CoaD family. {ECO:0000255|HAMAP-
CC       Rule:MF_00151}.
CC   -!- CAUTION: Was originally thought to have an essential function in
CC       lipopolysaccharide biosynthesis. {ECO:0000305|PubMed:1577693}.
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DR   EMBL; M60670; AAA24044.1; -; Genomic_DNA.
DR   EMBL; M86305; AAA03746.1; -; Genomic_DNA.
DR   EMBL; U00039; AAB18611.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC76658.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77658.1; -; Genomic_DNA.
DR   PIR; JU0468; JU0468.
DR   RefSeq; NP_418091.1; NC_000913.3.
DR   RefSeq; WP_001171866.1; NZ_STEB01000024.1.
DR   PDB; 1B6T; X-ray; 1.80 A; A/B=1-159.
DR   PDB; 1GN8; X-ray; 1.83 A; A/B=1-159.
DR   PDB; 1H1T; X-ray; 1.78 A; A/B=1-159.
DR   PDB; 1QJC; X-ray; 1.63 A; A/B=2-159.
DR   PDB; 5JBN; X-ray; 1.45 A; A/B=1-159.
DR   PDB; 6B7A; X-ray; 1.99 A; A/B=1-159.
DR   PDB; 6B7B; X-ray; 1.98 A; A/B=1-159.
DR   PDB; 6B7C; X-ray; 1.56 A; A/B=1-159.
DR   PDB; 6B7D; X-ray; 1.80 A; A/B=1-159.
DR   PDB; 6B7E; X-ray; 2.10 A; A/B=1-159.
DR   PDB; 6B7F; X-ray; 2.56 A; A/B=1-159.
DR   PDB; 6CCK; X-ray; 1.61 A; A/B=1-159.
DR   PDB; 6CCL; X-ray; 1.77 A; A/B=1-159.
DR   PDB; 6CCM; X-ray; 1.79 A; A/B=1-159.
DR   PDB; 6CCN; X-ray; 1.87 A; A/B=1-159.
DR   PDB; 6CCO; X-ray; 1.82 A; A/B=1-159.
DR   PDB; 6CCQ; X-ray; 1.92 A; A/B=1-159.
DR   PDB; 6CCS; X-ray; 2.06 A; A/B=1-159.
DR   PDB; 6CHL; X-ray; 2.20 A; A/B=1-159.
DR   PDB; 6CHM; X-ray; 2.28 A; A/B=1-159.
DR   PDB; 6CHN; X-ray; 2.03 A; A/B=1-159.
DR   PDB; 6CHO; X-ray; 1.85 A; A/B=1-159.
DR   PDB; 6CHP; X-ray; 1.94 A; A/B=1-159.
DR   PDB; 6CHQ; X-ray; 1.79 A; A/B=1-159.
DR   PDB; 6CKW; X-ray; 2.06 A; A/B=1-159.
DR   PDBsum; 1B6T; -.
DR   PDBsum; 1GN8; -.
DR   PDBsum; 1H1T; -.
DR   PDBsum; 1QJC; -.
DR   PDBsum; 5JBN; -.
DR   PDBsum; 6B7A; -.
DR   PDBsum; 6B7B; -.
DR   PDBsum; 6B7C; -.
DR   PDBsum; 6B7D; -.
DR   PDBsum; 6B7E; -.
DR   PDBsum; 6B7F; -.
DR   PDBsum; 6CCK; -.
DR   PDBsum; 6CCL; -.
DR   PDBsum; 6CCM; -.
DR   PDBsum; 6CCN; -.
DR   PDBsum; 6CCO; -.
DR   PDBsum; 6CCQ; -.
DR   PDBsum; 6CCS; -.
DR   PDBsum; 6CHL; -.
DR   PDBsum; 6CHM; -.
DR   PDBsum; 6CHN; -.
DR   PDBsum; 6CHO; -.
DR   PDBsum; 6CHP; -.
DR   PDBsum; 6CHQ; -.
DR   PDBsum; 6CKW; -.
DR   AlphaFoldDB; P0A6I6; -.
DR   SMR; P0A6I6; -.
DR   BioGRID; 4263379; 238.
DR   DIP; DIP-35966N; -.
DR   IntAct; P0A6I6; 10.
DR   STRING; 511145.b3634; -.
DR   BindingDB; P0A6I6; -.
DR   ChEMBL; CHEMBL4523175; -.
DR   jPOST; P0A6I6; -.
DR   PaxDb; 511145-b3634; -.
DR   EnsemblBacteria; AAC76658; AAC76658; b3634.
DR   GeneID; 75202203; -.
DR   GeneID; 947386; -.
DR   KEGG; ecj:JW3609; -.
DR   KEGG; eco:b3634; -.
DR   PATRIC; fig|1411691.4.peg.3072; -.
DR   EchoBASE; EB1176; -.
DR   eggNOG; COG0669; Bacteria.
DR   HOGENOM; CLU_100149_0_1_6; -.
DR   InParanoid; P0A6I6; -.
DR   OMA; MALMNRK; -.
DR   OrthoDB; 9806661at2; -.
DR   PhylomeDB; P0A6I6; -.
DR   BioCyc; EcoCyc:PANTEPADENYLYLTRAN-MONOMER; -.
DR   BioCyc; MetaCyc:PANTEPADENYLYLTRAN-MONOMER; -.
DR   BRENDA; 2.7.7.3; 2026.
DR   SABIO-RK; P0A6I6; -.
DR   UniPathway; UPA00241; UER00355.
DR   EvolutionaryTrace; P0A6I6; -.
DR   PRO; PR:P0A6I6; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR   GO; GO:0004595; F:pantetheine-phosphate adenylyltransferase activity; IDA:EcoCyc.
DR   GO; GO:0015937; P:coenzyme A biosynthetic process; IDA:EcoCyc.
DR   CDD; cd02163; PPAT; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   HAMAP; MF_00151; PPAT_bact; 1.
DR   InterPro; IPR004821; Cyt_trans-like.
DR   InterPro; IPR001980; PPAT.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   NCBIfam; TIGR01510; coaD_prev_kdtB; 1.
DR   NCBIfam; TIGR00125; cyt_tran_rel; 1.
DR   PANTHER; PTHR21342; PHOSPHOPANTETHEINE ADENYLYLTRANSFERASE; 1.
DR   PANTHER; PTHR21342:SF1; PHOSPHOPANTETHEINE ADENYLYLTRANSFERASE; 1.
DR   Pfam; PF01467; CTP_transf_like; 1.
DR   PRINTS; PR01020; LPSBIOSNTHSS.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Coenzyme A biosynthesis; Cytoplasm;
KW   Direct protein sequencing; Magnesium; Nucleotide-binding;
KW   Nucleotidyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..159
FT                   /note="Phosphopantetheine adenylyltransferase"
FT                   /id="PRO_0000156204"
FT   BINDING         7..11
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000269|PubMed:11812124,
FT                   ECO:0007744|PDB:1GN8"
FT   BINDING         10
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:11812124,
FT                   ECO:0000269|PubMed:12837781, ECO:0007744|PDB:1H1T,
FT                   ECO:0007744|PDB:1QJC"
FT   BINDING         18
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000269|PubMed:11812124,
FT                   ECO:0007744|PDB:1GN8"
FT   BINDING         42
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:11812124,
FT                   ECO:0000269|PubMed:12837781, ECO:0007744|PDB:1H1T,
FT                   ECO:0007744|PDB:1QJC"
FT   BINDING         74
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:11812124,
FT                   ECO:0000269|PubMed:12837781, ECO:0007744|PDB:1H1T,
FT                   ECO:0007744|PDB:1QJC"
FT   BINDING         88
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:11812124,
FT                   ECO:0007744|PDB:1QJC"
FT   BINDING         89..91
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000269|PubMed:11812124,
FT                   ECO:0007744|PDB:1GN8"
FT   BINDING         99
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000269|PubMed:11812124,
FT                   ECO:0007744|PDB:1GN8"
FT   BINDING         124..130
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000269|PubMed:11812124,
FT                   ECO:0007744|PDB:1GN8"
FT   SITE            18
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000305|PubMed:11812124"
FT   STRAND          4..9
FT                   /evidence="ECO:0007829|PDB:5JBN"
FT   HELIX           16..28
FT                   /evidence="ECO:0007829|PDB:5JBN"
FT   STRAND          29..37
FT                   /evidence="ECO:0007829|PDB:5JBN"
FT   HELIX           40..42
FT                   /evidence="ECO:0007829|PDB:5JBN"
FT   HELIX           48..58
FT                   /evidence="ECO:0007829|PDB:5JBN"
FT   TURN            59..61
FT                   /evidence="ECO:0007829|PDB:5JBN"
FT   STRAND          65..70
FT                   /evidence="ECO:0007829|PDB:5JBN"
FT   HELIX           74..80
FT                   /evidence="ECO:0007829|PDB:5JBN"
FT   STRAND          85..89
FT                   /evidence="ECO:0007829|PDB:5JBN"
FT   HELIX           96..109
FT                   /evidence="ECO:0007829|PDB:5JBN"
FT   STRAND          113..118
FT                   /evidence="ECO:0007829|PDB:5JBN"
FT   HELIX           122..124
FT                   /evidence="ECO:0007829|PDB:5JBN"
FT   HELIX           129..137
FT                   /evidence="ECO:0007829|PDB:5JBN"
FT   HELIX           143..145
FT                   /evidence="ECO:0007829|PDB:5JBN"
FT   HELIX           148..159
FT                   /evidence="ECO:0007829|PDB:5JBN"
SQ   SEQUENCE   159 AA;  17837 MW;  C4D7B8715A061B91 CRC64;
     MQKRAIYPGT FDPITNGHID IVTRATQMFD HVILAIAASP SKKPMFTLEE RVALAQQATA
     HLGNVEVVGF SDLMANFARN QHATVLIRGL RAVADFEYEM QLAHMNRHLM PELESVFLMP
     SKEWSFISSS LVKEVARHQG DVTHFLPENV HQALMAKLA
//