PPSC_MYCTU
ID PPSC_MYCTU Reviewed; 2188 AA.
AC P96202; L0TBB0;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Phenolphthiocerol/phthiocerol polyketide synthase subunit C {ECO:0000305};
DE EC=2.3.1.292 {ECO:0000269|PubMed:15749014, ECO:0000305|PubMed:20553505};
DE AltName: Full=(Phenol)carboxyphthiodiolenone synthase subunit C;
DE AltName: Full=Beta-ketoacyl-acyl-carrier-protein synthase I;
DE AltName: Full=Phthiocerol synthesis polyketide synthase type I PpsC;
GN Name=ppsC; OrderedLocusNames=Rv2933;
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 FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND PATHWAY.
RX PubMed=15749014; DOI=10.1016/j.molcel.2005.02.009;
RA Trivedi O.A., Arora P., Vats A., Ansari M.Z., Tickoo R., Sridharan V.,
RA Mohanty D., Gokhale R.S.;
RT "Dissecting the mechanism and assembly of a complex virulence mycobacterial
RT lipid.";
RL Mol. Cell 17:631-643(2005).
RN [3]
RP IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
RX PubMed=19099550; DOI=10.1186/1752-0509-2-109;
RA Raman K., Yeturu K., Chandra N.;
RT "targetTB: a target identification pipeline for Mycobacterium tuberculosis
RT through an interactome, reactome and genome-scale structural analysis.";
RL BMC Syst. Biol. 2:109-109(2008).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=20553505; DOI=10.1111/j.1742-4658.2010.07688.x;
RA Simeone R., Leger M., Constant P., Malaga W., Marrakchi H., Daffe M.,
RA Guilhot C., Chalut C.;
RT "Delineation of the roles of FadD22, FadD26 and FadD29 in the biosynthesis
RT of phthiocerol dimycocerosates and related compounds in Mycobacterium
RT tuberculosis.";
RL FEBS J. 277:2715-2725(2010).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 PHOSPHOPANTETHEINYLATION AT SER-2105, AND MUTAGENESIS OF SER-2105.
RX PubMed=28203522; DOI=10.1002/2211-5463.12140;
RA Jung J., Bashiri G., Johnston J.M., Baker E.N.;
RT "Mass spectral determination of phosphopantetheinylation specificity for
RT carrier proteins in Mycobacterium tuberculosis.";
RL FEBS Open Bio 6:1220-1226(2016).
RN [7] {ECO:0007744|PDB:1PQW}
RP X-RAY CRYSTALLOGRAPHY (2.66 ANGSTROMS) OF 1559-1755, AND SUBUNIT.
RC STRAIN=ATCC 25618 / H37Rv;
RA Gogos A., Mu H., Shapiro L.;
RT "Putative enoyl reductase domain of polyketide synthase.";
RL Submitted (JUN-2003) to the PDB data bank.
RN [8] {ECO:0007744|PDB:4OKI, ECO:0007744|PDB:4OOC}
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 1558-1750.
RA Faille A., Slama N., Quemard A., Mourey L., Pedelacq J.D.;
RT "Insights into the catalytic mechanism of the DH domain of the
RT Mycobacterium tuberculosis polyketide synthase PpsC and architecture of the
RT beta-carbon processing domains.";
RL Submitted (JAN-2014) to the PDB data bank.
RN [9] {ECO:0007744|PDB:5I0K, ECO:0007744|PDB:5L84, ECO:0007744|PDB:5NJI}
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 921-1217 OF APOENZYME AND IN
RP COMPLEXES WITH TRANS-BUT-2-ENOYL-COA AND TRANS-DODEC-2-ENOYL-COA
RP DERIVATIVES, ACTIVE SITE, AND MUTAGENESIS OF HIS-959.
RX PubMed=28377293; DOI=10.1016/j.jmb.2017.03.026;
RA Faille A., Gavalda S., Slama N., Lherbet C., Maveyraud L., Guillet V.,
RA Laval F., Quemard A., Mourey L., Pedelacq J.D.;
RT "Insights into substrate modification by dehydratases from type I
RT polyketide synthases.";
RL J. Mol. Biol. 429:1554-1569(2017).
CC -!- FUNCTION: Part of the PpsABCDE complex involved in the biosynthesis of
CC the lipid core common to phthiocerols and phenolphthiocerols by
CC successive additions of malonyl-CoA or methylmalonyl-CoA extender units
CC (PubMed:15749014, PubMed:20553505). PpsA can accept as substrate the
CC activated forms of either icosanoyl (C20), docosanoyl (C22) or
CC lignoceroyl (C24) groups from FadD26, or a (4-hydroxyphenyl)-C17 or (4-
CC hydroxyphenyl)-C19 fatty acyl from FadD29 (PubMed:15749014,
CC PubMed:20553505). PpsA initiates the biosynthesis and extends its
CC substrate using a malonyl-CoA extender unit. The PpsB and PpsC proteins
CC add the second and third malonyl-CoA extender units. PpsD adds an (R)-
CC methylmalonyl unit and PpsE adds a second (R)-methylmalonyl unit. The
CC incorporation of the methylmalonyl units results in formation of two
CC branched methyl groups in the elongated product (PubMed:15749014).
CC {ECO:0000269|PubMed:15749014, ECO:0000269|PubMed:20553505}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 (S)-methylmalonyl-CoA + 10 H(+) + icosanoyl-
CC [(phenol)carboxyphthiodiolenone synthase] + 3 malonyl-CoA + 5 NADPH =
CC C32-carboxyphthiodiolenone-[(phenol)carboxyphthiodiolenone synthase]
CC + 5 CO2 + 5 CoA + 2 H2O + 5 NADP(+); Xref=Rhea:RHEA:57748, Rhea:RHEA-
CC COMP:14985, Rhea:RHEA-COMP:14986, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57327, ChEBI:CHEBI:57384, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:87848, ChEBI:CHEBI:142236;
CC EC=2.3.1.292; Evidence={ECO:0000269|PubMed:15749014,
CC ECO:0000305|PubMed:20553505};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 (S)-methylmalonyl-CoA + docosanoyl-
CC [(phenol)carboxyphthiodiolenone synthase] + 10 H(+) + 3 malonyl-CoA +
CC 5 NADPH = C34-carboxyphthiodiolenone-[(phenol)carboxyphthiodiolenone
CC synthase] + 5 CO2 + 5 CoA + 2 H2O + 5 NADP(+); Xref=Rhea:RHEA:57752,
CC Rhea:RHEA-COMP:14987, Rhea:RHEA-COMP:14988, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57327, ChEBI:CHEBI:57384, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:142237, ChEBI:CHEBI:142238;
CC EC=2.3.1.292; Evidence={ECO:0000269|PubMed:15749014,
CC ECO:0000305|PubMed:20553505};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 (S)-methylmalonyl-CoA + 17-(4-hydroxyphenyl)heptadecanoyl-
CC [(phenol)carboxyphthiodiolenone synthase] + 10 H(+) + 3 malonyl-CoA +
CC 5 NADPH = C35-(phenol)carboxyphthiodiolenone-
CC [(phenol)carboxyphthiodiolenone synthase] + 5 CO2 + 5 CoA + 2 H2O + 5
CC NADP(+); Xref=Rhea:RHEA:57756, Rhea:RHEA-COMP:14272, Rhea:RHEA-
CC COMP:14989, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57327, ChEBI:CHEBI:57384,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:133300,
CC ChEBI:CHEBI:142259; EC=2.3.1.292;
CC Evidence={ECO:0000269|PubMed:15749014, ECO:0000305|PubMed:20553505};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 (S)-methylmalonyl-CoA + 19-(4-hydroxyphenyl)nonadecanoyl-
CC [(phenol)carboxyphthiodiolenone synthase] + 10 H(+) + 3 malonyl-CoA +
CC 5 NADPH = C37-(phenol)carboxyphthiodiolenone-
CC [(phenol)carboxyphthiodiolenone synthase] + 5 CO2 + 5 CoA + 2 H2O + 5
CC NADP(+); Xref=Rhea:RHEA:57760, Rhea:RHEA-COMP:14273, Rhea:RHEA-
CC COMP:14990, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57327, ChEBI:CHEBI:57384,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:133301,
CC ChEBI:CHEBI:142260; EC=2.3.1.292;
CC Evidence={ECO:0000269|PubMed:15749014, ECO:0000305|PubMed:20553505};
CC -!- COFACTOR:
CC Name=NADP(+); Xref=ChEBI:CHEBI:58349;
CC Evidence={ECO:0000269|PubMed:15749014};
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000269|PubMed:28203522};
CC Note=Binds 1 phosphopantetheine covalently.
CC {ECO:0000305|PubMed:28203522};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000269|PubMed:15749014}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|Ref.7}.
CC -!- MISCELLANEOUS: Was identified as a high-confidence drug target.
CC {ECO:0000269|PubMed:19099550}.
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DR EMBL; AL123456; CCP45736.1; -; Genomic_DNA.
DR PIR; A70984; A70984.
DR RefSeq; NP_217449.1; NC_000962.3.
DR RefSeq; WP_003414837.1; NZ_KK339370.1.
DR PDB; 1PQW; X-ray; 2.66 A; A/B=1559-1755.
DR PDB; 4OKI; X-ray; 1.50 A; A/B=1558-1750.
DR PDB; 4OOC; X-ray; 2.70 A; A=921-1222.
DR PDB; 5I0K; X-ray; 3.20 A; A=921-1217.
DR PDB; 5L84; X-ray; 2.90 A; A=921-1222.
DR PDB; 5NJI; X-ray; 1.60 A; A=921-1222.
DR PDB; 6RCX; X-ray; 2.00 A; B=2057-2188.
DR PDB; 7AHB; X-ray; 1.90 A; A/B=546-876.
DR PDBsum; 1PQW; -.
DR PDBsum; 4OKI; -.
DR PDBsum; 4OOC; -.
DR PDBsum; 5I0K; -.
DR PDBsum; 5L84; -.
DR PDBsum; 5NJI; -.
DR PDBsum; 6RCX; -.
DR PDBsum; 7AHB; -.
DR AlphaFoldDB; P96202; -.
DR SMR; P96202; -.
DR STRING; 83332.Rv2933; -.
DR iPTMnet; P96202; -.
DR PaxDb; P96202; -.
DR GeneID; 887686; -.
DR KEGG; mtu:Rv2933; -.
DR PATRIC; fig|83332.111.peg.3263; -.
DR TubercuList; Rv2933; -.
DR eggNOG; COG0604; Bacteria.
DR eggNOG; COG1028; Bacteria.
DR eggNOG; COG3321; Bacteria.
DR InParanoid; P96202; -.
DR OMA; KMRGGEF; -.
DR PhylomeDB; P96202; -.
DR UniPathway; UPA00094; -.
DR EvolutionaryTrace; P96202; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0034081; C:polyketide synthase complex; ISS:UniProtKB.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0004312; F:fatty acid synthase activity; IBA:GO_Central.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0071766; P:Actinobacterium-type cell wall biogenesis; ISS:UniProtKB.
DR GO; GO:0071770; P:DIM/DIP cell wall layer assembly; IDA:MTBBASE.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IDA:MTBBASE.
DR GO; GO:0097041; P:phenolic phthiocerol biosynthetic process; ISS:UniProtKB.
DR GO; GO:0097040; P:phthiocerol biosynthetic process; ISS:UniProtKB.
DR Gene3D; 1.10.1200.10; -; 1.
DR Gene3D; 3.10.129.110; -; 1.
DR Gene3D; 3.40.366.10; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR InterPro; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR013154; ADH_N.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR018201; Ketoacyl_synth_AS.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR020807; PKS_dehydratase.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR020843; PKS_ER.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR016039; Thiolase-like.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF16197; KAsynt_C_assoc; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF08659; KR; 1.
DR Pfam; PF00550; PP-binding; 1.
DR Pfam; PF14765; PS-DH; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00826; PKS_DH; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF47336; SSF47336; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 3.
DR SUPFAM; SSF52151; SSF52151; 1.
DR SUPFAM; SSF53901; SSF53901; 1.
DR SUPFAM; SSF55048; SSF55048; 1.
DR PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Fatty acid metabolism; Lipid metabolism;
KW Multifunctional enzyme; NADP; Oxidoreductase; Phosphopantetheine;
KW Phosphoprotein; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:21969609"
FT CHAIN 2..2188
FT /note="Phenolphthiocerol/phthiocerol polyketide synthase
FT subunit C"
FT /id="PRO_0000406948"
FT DOMAIN 2069..2145
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 37..465
FT /note="Beta-ketoacyl synthase"
FT /evidence="ECO:0000250"
FT REGION 572..890
FT /note="Acyltransferase"
FT /evidence="ECO:0000250"
FT REGION 928..1093
FT /note="Dehydratase"
FT /evidence="ECO:0000250"
FT REGION 1467..1778
FT /note="Enoylreductase"
FT /evidence="ECO:0000250"
FT REGION 1802..1981
FT /note="Beta-ketoacyl reductase"
FT /evidence="ECO:0000250"
FT ACT_SITE 210
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 660
FT /note="For malonyltransferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 959
FT /note="For dehydratase activity"
FT /evidence="ECO:0000305|PubMed:28377293"
FT BINDING 1803..1848
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0007744|PubMed:21969609"
FT MOD_RES 2105
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000269|PubMed:28203522"
FT MUTAGEN 959
FT /note="H->F: Lack of dehydration reaction."
FT /evidence="ECO:0000269|PubMed:28377293"
FT MUTAGEN 2105
FT /note="S->A: Lack of phosphopantetheinylation."
FT /evidence="ECO:0000269|PubMed:28203522"
FT HELIX 546..551
FT /evidence="ECO:0007829|PDB:7AHB"
FT STRAND 571..575
FT /evidence="ECO:0007829|PDB:7AHB"
FT TURN 583..586
FT /evidence="ECO:0007829|PDB:7AHB"
FT HELIX 587..592
FT /evidence="ECO:0007829|PDB:7AHB"
FT HELIX 594..611
FT /evidence="ECO:0007829|PDB:7AHB"
FT HELIX 615..620
FT /evidence="ECO:0007829|PDB:7AHB"
FT HELIX 628..648
FT /evidence="ECO:0007829|PDB:7AHB"
FT STRAND 654..658
FT /evidence="ECO:0007829|PDB:7AHB"
FT HELIX 660..662
FT /evidence="ECO:0007829|PDB:7AHB"
FT HELIX 663..669
FT /evidence="ECO:0007829|PDB:7AHB"
FT HELIX 675..689
FT /evidence="ECO:0007829|PDB:7AHB"
FT HELIX 690..692
FT /evidence="ECO:0007829|PDB:7AHB"
FT STRAND 697..703
FT /evidence="ECO:0007829|PDB:7AHB"
FT HELIX 705..711
FT /evidence="ECO:0007829|PDB:7AHB"
FT TURN 712..714
FT /evidence="ECO:0007829|PDB:7AHB"
FT STRAND 719..723
FT /evidence="ECO:0007829|PDB:7AHB"
FT STRAND 725..727
FT /evidence="ECO:0007829|PDB:7AHB"
FT STRAND 729..733
FT /evidence="ECO:0007829|PDB:7AHB"
FT HELIX 735..747
FT /evidence="ECO:0007829|PDB:7AHB"
FT STRAND 752..754
FT /evidence="ECO:0007829|PDB:7AHB"
FT HELIX 764..769
FT /evidence="ECO:0007829|PDB:7AHB"
FT HELIX 770..776
FT /evidence="ECO:0007829|PDB:7AHB"
FT TURN 777..779
FT /evidence="ECO:0007829|PDB:7AHB"
FT STRAND 789..794
FT /evidence="ECO:0007829|PDB:7AHB"
FT TURN 795..798
FT /evidence="ECO:0007829|PDB:7AHB"
FT STRAND 801..803
FT /evidence="ECO:0007829|PDB:7AHB"
FT HELIX 809..817
FT /evidence="ECO:0007829|PDB:7AHB"
FT HELIX 822..830
FT /evidence="ECO:0007829|PDB:7AHB"
FT STRAND 835..838
FT /evidence="ECO:0007829|PDB:7AHB"
FT STRAND 840..842
FT /evidence="ECO:0007829|PDB:7AHB"
FT HELIX 846..856
FT /evidence="ECO:0007829|PDB:7AHB"
FT HELIX 859..861
FT /evidence="ECO:0007829|PDB:7AHB"
FT STRAND 863..865
FT /evidence="ECO:0007829|PDB:7AHB"
FT TURN 929..931
FT /evidence="ECO:0007829|PDB:5NJI"
FT STRAND 933..936
FT /evidence="ECO:0007829|PDB:5NJI"
FT TURN 938..940
FT /evidence="ECO:0007829|PDB:5NJI"
FT STRAND 943..949
FT /evidence="ECO:0007829|PDB:5NJI"
FT HELIX 956..958
FT /evidence="ECO:0007829|PDB:5NJI"
FT STRAND 959..961
FT /evidence="ECO:0007829|PDB:5NJI"
FT STRAND 964..966
FT /evidence="ECO:0007829|PDB:5NJI"
FT HELIX 969..983
FT /evidence="ECO:0007829|PDB:5NJI"
FT STRAND 987..990
FT /evidence="ECO:0007829|PDB:5NJI"
FT STRAND 992..999
FT /evidence="ECO:0007829|PDB:5NJI"
FT STRAND 1009..1017
FT /evidence="ECO:0007829|PDB:5NJI"
FT STRAND 1019..1029
FT /evidence="ECO:0007829|PDB:5NJI"
FT STRAND 1031..1033
FT /evidence="ECO:0007829|PDB:4OOC"
FT STRAND 1035..1045
FT /evidence="ECO:0007829|PDB:5NJI"
FT STRAND 1067..1070
FT /evidence="ECO:0007829|PDB:5NJI"
FT HELIX 1072..1081
FT /evidence="ECO:0007829|PDB:5NJI"
FT STRAND 1084..1086
FT /evidence="ECO:0007829|PDB:5NJI"
FT HELIX 1088..1090
FT /evidence="ECO:0007829|PDB:5NJI"
FT STRAND 1093..1099
FT /evidence="ECO:0007829|PDB:5NJI"
FT STRAND 1100..1102
FT /evidence="ECO:0007829|PDB:5L84"
FT STRAND 1104..1108
FT /evidence="ECO:0007829|PDB:5NJI"
FT HELIX 1112..1114
FT /evidence="ECO:0007829|PDB:5NJI"
FT TURN 1115..1117
FT /evidence="ECO:0007829|PDB:5NJI"
FT HELIX 1118..1120
FT /evidence="ECO:0007829|PDB:4OOC"
FT HELIX 1125..1133
FT /evidence="ECO:0007829|PDB:5NJI"
FT HELIX 1134..1137
FT /evidence="ECO:0007829|PDB:5NJI"
FT HELIX 1139..1145
FT /evidence="ECO:0007829|PDB:5NJI"
FT STRAND 1161..1171
FT /evidence="ECO:0007829|PDB:5NJI"
FT HELIX 1175..1177
FT /evidence="ECO:0007829|PDB:5NJI"
FT STRAND 1180..1188
FT /evidence="ECO:0007829|PDB:5NJI"
FT STRAND 1191..1199
FT /evidence="ECO:0007829|PDB:5NJI"
FT STRAND 1205..1216
FT /evidence="ECO:0007829|PDB:5NJI"
FT HELIX 1572..1587
FT /evidence="ECO:0007829|PDB:4OKI"
FT TURN 1588..1591
FT /evidence="ECO:0007829|PDB:4OKI"
FT STRAND 1598..1601
FT /evidence="ECO:0007829|PDB:4OKI"
FT TURN 1602..1605
FT /evidence="ECO:0007829|PDB:4OKI"
FT HELIX 1607..1619
FT /evidence="ECO:0007829|PDB:4OKI"
FT STRAND 1622..1629
FT /evidence="ECO:0007829|PDB:4OKI"
FT HELIX 1630..1638
FT /evidence="ECO:0007829|PDB:4OKI"
FT STRAND 1642..1646
FT /evidence="ECO:0007829|PDB:4OKI"
FT HELIX 1652..1659
FT /evidence="ECO:0007829|PDB:4OKI"
FT TURN 1660..1662
FT /evidence="ECO:0007829|PDB:4OKI"
FT STRAND 1665..1670
FT /evidence="ECO:0007829|PDB:4OKI"
FT HELIX 1675..1682
FT /evidence="ECO:0007829|PDB:4OKI"
FT STRAND 1684..1692
FT /evidence="ECO:0007829|PDB:4OKI"
FT HELIX 1696..1699
FT /evidence="ECO:0007829|PDB:4OKI"
FT STRAND 1703..1705
FT /evidence="ECO:0007829|PDB:4OKI"
FT HELIX 1706..1709
FT /evidence="ECO:0007829|PDB:4OKI"
FT TURN 1710..1712
FT /evidence="ECO:0007829|PDB:4OKI"
FT STRAND 1714..1717
FT /evidence="ECO:0007829|PDB:4OKI"
FT HELIX 1720..1726
FT /evidence="ECO:0007829|PDB:4OKI"
FT HELIX 1728..1743
FT /evidence="ECO:0007829|PDB:4OKI"
FT HELIX 2073..2086
FT /evidence="ECO:0007829|PDB:6RCX"
FT HELIX 2098..2101
FT /evidence="ECO:0007829|PDB:6RCX"
FT HELIX 2105..2119
FT /evidence="ECO:0007829|PDB:6RCX"
FT HELIX 2127..2130
FT /evidence="ECO:0007829|PDB:6RCX"
FT HELIX 2134..2144
FT /evidence="ECO:0007829|PDB:6RCX"
SQ SEQUENCE 2188 AA; 230622 MW; 3C431C011F01F1A2 CRC64;
MTAATPDRRA IITEALHKID DLTARLEIAE KSSSEPIAVI GMGCRFPGGV NNPEQFWDLL
CAGRSGIVRV PAQRWDADAY YCDDHTVPGT ICSTEGGFLT SWQPDEFDAE FFSISPREAA
AMDPQQRLLI EVAWEALEDA GVPQHTIRGT QTSVFVGVTA YDYMLTLAGR LRPVDLDAYI
PTGNSANFAA GRLAYILGAR GPAVVIDTAC SSSLVAVHLA CQSLRGRESD MALVGGTNLL
LSPGPSIACS RWGMLSPEGR CKTFDASADG YVRGEGAAVV VLKRLDDAVR DGNRILAVVR
GSAVNQDGAS SGVTVPNGPA QQALLAKALT SSKLTAADID YVEAHGTGTP LGDPIELDSL
SKVFSDRAGS DQLVIGSVKT NLGHLEAAAG VAGLMKAVLA VHNGYIPRHL NFHQLTPHAS
EAASRLRIAA DGIDWPTTGR PRRAGVSSFG VSGTNAHVVI EQAPDPMAAA GTEPQRGPVP
AVSTLVVFGK TAPRVAATAS VLADWLDGPG AAVPLADVAH TLNHHRARQT RFGTVAAVDR
RQAVIGLRAL AAGQSAPGVV APREGSIGGG TVFVYSGRGS QWAGMGRQLL ADEPAFAAAI
AELEPEFVAQ GGFSLRDVIA GGKELVGIEQ IQLGLIGMQL ALTALWRSYG VTPDAVIGHS
MGEVAAAVVA GALTPAQGLR VTAVRSRLMA PLSGQGTMAL LELDAEATEA LIADYPEVSL
GIYASPRQTV ISGPPLLIDE LIDKVRQQNG FATRVNIEVA PHNPAMDALQ PAMRSELADL
TPQPPTIPII STTYADLGIS LGSGPRFDAE HWATNMRNPV RFHQAIAHAG ADHHTFIEIS
AHPLLTHSIS DTLRASYDVD NYLSIGTLQR DAHDTLEFHT NLNTTHTTHP PQTPHPPEPH
PVLPTTPWQH TQHWITATSA AYHRPDTHPL LGVGVTDPTN GTRVWESELD PDLLWLADHV
IDDLVVLPGA AYAEIALAAA TDTFAVEQDQ PWMISELDLR QMLHVTPGTV LVTTLTGDEQ
RCQVEIRTRS GSSGWTTHAT ATVARAEPLA PLDHEGQRRE VTTADLEDQL DPDDLYQRLR
GAGQQHGPAF QGIVGLAVTQ AGVARAQVRL PASARTGSRE FMLHPVMMDI ALQTLGATRT
ATDLAGGQDA RQGPSSNSAL VVPVRFAGVH VYGDITRGVR AVGSLAAAGD RLVGEVVLTD
ANGQPLLVVD EVEMAVLGSG SGATELTNRL FMLEWEPAPL EKTAEATGAL LLIGDPAAGD
PLLPALQSSL RDRITDLELA SAADEATLRA AISRTSWDGI VVVCPPRAND ESMPDEAQLE
LARTRTLLVA SVVETVTRMG ARKSPRLWIV TRGAAQFDAG ESVTLAQTGL RGIARVLTFE
HSELNTTLVD IEPDGTGSLA ALAEELLAGS EADEVALRDG QRYVNRLVPA PTTTSGDLAA
EARHQVVNLD SSGASRAAVR LQIDQPGRLD ALNVHEVKRG RPQGDQVEVR VVAAGLNFSD
VLKAMGVYPG LDGAAPVIGG ECVGYVTAIG DEVDGVEVGQ RVIAFGPGTF GTHLGTIADL
VVPIPDTLAD NEAATFGVAY LTAWHSLCEV GRLSPGERVL IHSATGGVGM AAVSIAKMIG
ARIYTTAGSD AKREMLSRLG VEYVGDSRSV DFADEILELT DGYGVDVVLN SLAGEAIQRG
VQILAPGGRF IELGKKDVYA DASLGLAALA KSASFSVVDL DLNLKLQPAR YRQLLQHILQ
HVADGKLEVL PVTAFSLHDA ADAFRLMASG KHTGKIVISI PQHGSIEAIA APPPLPLVSR
DGGYLIVGGM GGLGFVVARW LAEQGAGLIV LNGRSAPSDE VAAAIAELNA SGSRIEVITG
DITEPDTAER LVRAVEDAGF RLAGVVHSAM VLADEIVLNM TDSAARRVFA PKVTGSWRLH
VATAARDVDW WLTFSSAAAL LGTPGQGAYA AANSWVDGLV AHRRSAGLPA VGINWGPWAD
VGRAQFFKDL GVEMINAEQG LAAMQAVLTA DRGRTGVFSL DARQWFQSFP AVAGSSLFAK
LHDSAARKSG QRRGGGAIRA QLDALDAAER PGHLASAIAD EIRAVLRSGD PIDHHRPLET
LGLDSLMGLE LRNRLEASLG ITLPVALVWA YPTISDLATA LCERMDYATP AAAQEISDTE
PELSDEEMDL LADLVDASEL EAATRGES
