CULP6_MYCTU
ID CULP6_MYCTU Reviewed; 336 AA.
AC O53581; I6Y4J8; Q7D4U8;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Carboxylesterase/lipase Culp6 {ECO:0000305};
DE EC=3.1.1.- {ECO:0000269|PubMed:19225166};
DE AltName: Full=Cell wall lipase {ECO:0000303|PubMed:21384024};
DE AltName: Full=Cutinase-like protein 6 {ECO:0000303|PubMed:19225166};
DE Short=Culp6 {ECO:0000303|PubMed:19225166};
GN Name=cut6; OrderedLocusNames=Rv3802c {ECO:0000312|EMBL:CCP46631.1};
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, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=19169353; DOI=10.1371/journal.pone.0004281;
RA Parker S.K., Barkley R.M., Rino J.G., Vasil M.L.;
RT "Mycobacterium tuberculosis Rv3802c encodes a phospholipase/thioesterase
RT and is inhibited by the antimycobacterial agent tetrahydrolipstatin.";
RL PLoS ONE 4:e4281-e4281(2009).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-175; ASP-268 AND
RP HIS-299, AND ACTIVE SITE.
RC STRAIN=H37Rv;
RX PubMed=19225166; DOI=10.1096/fj.08-114421;
RA West N.P., Chow F.M., Randall E.J., Wu J., Chen J., Ribeiro J.M.,
RA Britton W.J.;
RT "Cutinase-like proteins of Mycobacterium tuberculosis: characterization of
RT their variable enzymatic functions and active site identification.";
RL FASEB J. 23:1694-1704(2009).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY
RP REGULATION.
RC STRAIN=H37Rv;
RX PubMed=20656688; DOI=10.1074/jbc.m110.150094;
RA Crellin P.K., Vivian J.P., Scoble J., Chow F.M., West N.P., Brammananth R.,
RA Proellocks N.I., Shahine A., Le Nours J., Wilce M.C., Britton W.J.,
RA Coppel R.L., Rossjohn J., Beddoe T.;
RT "Tetrahydrolipstatin inhibition, functional analyses, and three-dimensional
RT structure of a lipase essential for mycobacterial viability.";
RL J. Biol. Chem. 285:30050-30060(2010).
RN [5]
RP ACTIVITY REGULATION, AND BIOTECHNOLOGY.
RX PubMed=21384024; DOI=10.1039/c0cc05635a;
RA West N.P., Cergol K.M., Xue M., Randall E.J., Britton W.J., Payne R.J.;
RT "Inhibitors of an essential mycobacterial cell wall lipase (Rv3802c) as
RT tuberculosis drug leads.";
RL Chem. Commun. (Camb.) 47:5166-5168(2011).
RN [6] {ECO:0007744|PubMed:21969609}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [7]
RP BIOTECHNOLOGY.
RX PubMed=23085165; DOI=10.1016/j.jmgm.2012.06.016;
RA Saravanan P., Avinash H., Dubey V.K., Patra S.;
RT "Targeting essential cell wall lipase Rv3802c for potential therapeutics
RT against tuberculosis.";
RL J. Mol. Graph. Model. 38:235-242(2012).
RN [8]
RP ACTIVITY REGULATION.
RX PubMed=31741730; DOI=10.1039/c9md00122k;
RA Vartak A., Goins C., de Moura V.C.N., Schreidah C.M., Landgraf A.D.,
RA Lin B., Du J., Jackson M., Ronning D.R., Sucheck S.J.;
RT "Biochemical and microbiological evaluation of N-aryl urea derivatives
RT against mycobacteria and mycobacterial hydrolases.";
RL Med. Chem. Commun. 10:1197-1204(2019).
RN [9] {ECO:0007744|PDB:5W95}
RP X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS) OF 70-336 IN COMPLEX WITH
RP PENTAETHYLENE GLYCOL, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVE SITE,
RP DISULFIDE BONDS, AND MUTAGENESIS OF ASN-132 AND ASN-288.
RX PubMed=29247008; DOI=10.1074/jbc.ra117.000240;
RA Goins C.M., Schreidah C.M., Dajnowicz S., Ronning D.R.;
RT "Structural basis for lipid binding and mechanism of the Mycobacterium
RT tuberculosis Rv3802 phospholipase.";
RL J. Biol. Chem. 293:1363-1372(2018).
CC -!- FUNCTION: Shows esterase and phospholipase A activities
CC (PubMed:19169353, PubMed:19225166, PubMed:20656688, PubMed:29247008).
CC May be involved in cell wall biosynthesis and/or maintenance
CC (PubMed:19169353, PubMed:19225166, PubMed:20656688). Can hydrolyze
CC various substrates, including the p-nitrophenol-linked aliphatic esters
CC pNP-laurate (C12), pNP-myristate (C14), pNP-palmitate (C16), pNP-
CC stearate (C18), pNP-butyrate (C4), phosphatidylcholine,
CC phosphatidylethanolamine, phosphatidylserine, 4-methylumbelliferyl
CC heptanoate and palmitic acid and arachidonic acid containing
CC phospholipids (PubMed:19169353, PubMed:19225166, PubMed:20656688). Does
CC not exhibit cutinase activity (PubMed:19225166).
CC {ECO:0000269|PubMed:19169353, ECO:0000269|PubMed:19225166,
CC ECO:0000269|PubMed:20656688, ECO:0000269|PubMed:29247008}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dodecanoate ester + H2O = an aliphatic alcohol + dodecanoate
CC + H(+); Xref=Rhea:RHEA:47364, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:18262, ChEBI:CHEBI:87659;
CC Evidence={ECO:0000269|PubMed:19225166};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47365;
CC Evidence={ECO:0000269|PubMed:19225166};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a tetradecanoate ester + H2O = an aliphatic alcohol + H(+) +
CC tetradecanoate; Xref=Rhea:RHEA:47388, ChEBI:CHEBI:2571,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30807,
CC ChEBI:CHEBI:87691; Evidence={ECO:0000269|PubMed:19225166};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47389;
CC Evidence={ECO:0000269|PubMed:19225166};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + hexadecanoate ester = an aliphatic alcohol + H(+) +
CC hexadecanoate; Xref=Rhea:RHEA:47392, ChEBI:CHEBI:2571,
CC ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:25835; Evidence={ECO:0000269|PubMed:19225166};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47393;
CC Evidence={ECO:0000269|PubMed:19225166};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + octadecanoate ester = an aliphatic alcohol + H(+) +
CC octadecanoate; Xref=Rhea:RHEA:47396, ChEBI:CHEBI:2571,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25629,
CC ChEBI:CHEBI:75925; Evidence={ECO:0000269|PubMed:19225166};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47397;
CC Evidence={ECO:0000269|PubMed:19225166};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a butanoate ester + H2O = an aliphatic alcohol + butanoate +
CC H(+); Xref=Rhea:RHEA:47348, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17968, ChEBI:CHEBI:50477;
CC Evidence={ECO:0000269|PubMed:19225166, ECO:0000269|PubMed:20656688};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47349;
CC Evidence={ECO:0000269|PubMed:19225166, ECO:0000269|PubMed:20656688};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z)-octadecenoyl-sn-glycero-3-phospho-L-serine + H2O =
CC (9Z)-octadecenoate + 1-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-
CC serine + H(+); Xref=Rhea:RHEA:47328, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:74617,
CC ChEBI:CHEBI:74905; Evidence={ECO:0000269|PubMed:19169353};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47329;
CC Evidence={ECO:0000269|PubMed:19169353};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1-
CC hexadecanoyl-sn-glycero-3-phosphocholine + H(+) + hexadecanoate;
CC Xref=Rhea:RHEA:41223, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:72998, ChEBI:CHEBI:72999;
CC Evidence={ECO:0000269|PubMed:19169353};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41224;
CC Evidence={ECO:0000269|PubMed:19169353};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-acyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-
CC phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + a 1-acyl-
CC sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:40651,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395,
CC ChEBI:CHEBI:58168, ChEBI:CHEBI:75063;
CC Evidence={ECO:0000269|PubMed:19169353};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40652;
CC Evidence={ECO:0000269|PubMed:19169353};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phosphoethanolamine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-
CC hexadecanoyl-sn-glycero-3-phosphoethanolamine + H(+);
CC Xref=Rhea:RHEA:40431, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:32395, ChEBI:CHEBI:73004, ChEBI:CHEBI:73009;
CC Evidence={ECO:0000269|PubMed:19169353};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40432;
CC Evidence={ECO:0000269|PubMed:19169353};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + hexadecanoyl-CoA = CoA + H(+) + hexadecanoate;
CC Xref=Rhea:RHEA:16645, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379;
CC Evidence={ECO:0000269|PubMed:19169353};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16646;
CC Evidence={ECO:0000269|PubMed:19169353};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=decanoyl-CoA + H2O = CoA + decanoate + H(+);
CC Xref=Rhea:RHEA:40059, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:27689, ChEBI:CHEBI:57287, ChEBI:CHEBI:61430;
CC Evidence={ECO:0000269|PubMed:19169353};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40060;
CC Evidence={ECO:0000269|PubMed:19169353};
CC -!- ACTIVITY REGULATION: Inhibited by tetrahydrolipstatin (THL), a specific
CC lipase inhibitor, and by derivatives of THL (PubMed:19169353,
CC PubMed:20656688, PubMed:21384024). Inhibited by high concentrations of
CC paraoxon (PubMed:19225166). Also inhibited by a Furan-based urea
CC derivative, 1-(3,5-difluorophenyl)-3-(furan-2-ylmethyl)urea
CC (PubMed:31741730). {ECO:0000269|PubMed:19169353,
CC ECO:0000269|PubMed:19225166, ECO:0000269|PubMed:20656688,
CC ECO:0000269|PubMed:21384024, ECO:0000269|PubMed:31741730}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=23.52 mM for nitrophenyl butyrate {ECO:0000269|PubMed:19169353};
CC KM=0.017 mM for palmitoyl-S-CoA {ECO:0000269|PubMed:19169353};
CC KM=2.28 mM for decanoyl-S-CoA {ECO:0000269|PubMed:19169353};
CC KM=4.52 mM for pNP-butyrate {ECO:0000269|PubMed:20656688};
CC KM=19.88 uM for 4-methylumbelliferyl heptanoate
CC {ECO:0000269|PubMed:29247008};
CC Vmax=1.62 mol/min/mg enzyme with nitrophenyl butyrate as substrate
CC {ECO:0000269|PubMed:19169353};
CC Vmax=1.35 mol/min/mg enzyme with palmitoyl-S-CoA as substrate
CC {ECO:0000269|PubMed:19169353};
CC Vmax=1.11 mol/min/mg enzyme with decanoyl-S-CoA as substrate
CC {ECO:0000269|PubMed:19169353};
CC Vmax=241 nmol/min/mg enzyme with pNP-butyrate as substrate
CC {ECO:0000269|PubMed:20656688};
CC Note=kcat is 0.00881 sec(-1) with nitrophenyl butyrate as substrate.
CC kcat is 0.0733 sec(-1) with palmitoyl-S-CoA as substrate. kcat is
CC 0.0845 sec(-1) with decanoyl-S-CoA as substrate (PubMed:19169353).
CC kcat is 0.143 sec(-1) with pNP-butyrate as substrate
CC (PubMed:20656688). kcat is 10.05 min(-1) with 4-methylumbelliferyl
CC heptanoate as substrate (PubMed:29247008).
CC {ECO:0000269|PubMed:19169353, ECO:0000269|PubMed:20656688,
CC ECO:0000269|PubMed:29247008};
CC pH dependence:
CC Optimum pH is above 7.0 for lipase activity.
CC {ECO:0000269|PubMed:19225166};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000255}. Secreted, cell wall
CC {ECO:0000269|PubMed:19225166}.
CC -!- BIOTECHNOLOGY: The essential nature of the cell wall protein Culp6
CC makes it a promising target for drug development.
CC {ECO:0000269|PubMed:21384024, ECO:0000269|PubMed:23085165}.
CC -!- SIMILARITY: Belongs to the cutinase family. {ECO:0000305}.
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DR EMBL; AL123456; CCP46631.1; -; Genomic_DNA.
DR RefSeq; NP_218319.1; NC_000962.3.
DR RefSeq; WP_003420779.1; NZ_NVQJ01000022.1.
DR PDB; 5W95; X-ray; 1.72 A; A/B=70-336.
DR PDBsum; 5W95; -.
DR AlphaFoldDB; O53581; -.
DR SMR; O53581; -.
DR STRING; 83332.Rv3802c; -.
DR ChEMBL; CHEMBL4523141; -.
DR SwissLipids; SLP:000001328; -.
DR ESTHER; myctu-Rv3802c; Cutinase.
DR PaxDb; O53581; -.
DR PRIDE; O53581; -.
DR DNASU; 886135; -.
DR GeneID; 45427803; -.
DR GeneID; 886135; -.
DR KEGG; mtu:Rv3802c; -.
DR PATRIC; fig|83332.111.peg.4227; -.
DR TubercuList; Rv3802c; -.
DR eggNOG; COG4223; Bacteria.
DR OMA; TLNWAQG; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005576; C:extracellular region; HDA:MTBBASE.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; IDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0047617; F:acyl-CoA hydrolase activity; IDA:MTBBASE.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IDA:MTBBASE.
DR GO; GO:0016298; F:lipase activity; IDA:MTBBASE.
DR GO; GO:0016290; F:palmitoyl-CoA hydrolase activity; IEA:RHEA.
DR GO; GO:0008970; F:phospholipase A1 activity; IDA:MTBBASE.
DR GO; GO:0016042; P:lipid catabolic process; IDA:MTBBASE.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000675; Cutinase/axe.
DR PANTHER; PTHR33630; PTHR33630; 1.
DR Pfam; PF01083; Cutinase; 1.
DR SMART; SM01110; Cutinase; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Cell wall; Disulfide bond; Hydrolase;
KW Membrane; Reference proteome; Secreted; Serine esterase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..336
FT /note="Carboxylesterase/lipase Culp6"
FT /id="PRO_0000450109"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 44..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..62
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 175
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:19225166,
FT ECO:0000305|PubMed:29247008"
FT ACT_SITE 268
FT /evidence="ECO:0000305|PubMed:19225166,
FT ECO:0000305|PubMed:29247008"
FT ACT_SITE 299
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000305|PubMed:19225166,
FT ECO:0000305|PubMed:29247008"
FT SITE 176
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P00590"
FT DISULFID 72..164
FT /evidence="ECO:0000269|PubMed:29247008,
FT ECO:0007744|PDB:5W95"
FT DISULFID 264..271
FT /evidence="ECO:0000269|PubMed:29247008,
FT ECO:0007744|PDB:5W95"
FT MUTAGEN 132
FT /note="N->C: 2-fold decrease in kcat for 4-
FT methylumbelliferyl heptanoate and loss of phopholipase A
FT activity; when associated with C-288."
FT /evidence="ECO:0000269|PubMed:29247008"
FT MUTAGEN 175
FT /note="S->A: Loss of activity for both short- and long-
FT chain substrates."
FT /evidence="ECO:0000269|PubMed:19225166"
FT MUTAGEN 268
FT /note="D->A: Loss of activity for both short- and long-
FT chain substrates."
FT /evidence="ECO:0000269|PubMed:19225166"
FT MUTAGEN 288
FT /note="N->C: 2-fold decrease in kcat for 4-
FT methylumbelliferyl heptanoate and loss of phopholipase A
FT activity; when associated with C-132."
FT /evidence="ECO:0000269|PubMed:29247008"
FT MUTAGEN 299
FT /note="H->A: Loss of activity for both short- and long-
FT chain substrates."
FT /evidence="ECO:0000269|PubMed:19225166"
FT STRAND 74..80
FT /evidence="ECO:0007829|PDB:5W95"
FT HELIX 104..113
FT /evidence="ECO:0007829|PDB:5W95"
FT TURN 116..118
FT /evidence="ECO:0007829|PDB:5W95"
FT STRAND 119..123
FT /evidence="ECO:0007829|PDB:5W95"
FT HELIX 142..163
FT /evidence="ECO:0007829|PDB:5W95"
FT STRAND 168..174
FT /evidence="ECO:0007829|PDB:5W95"
FT HELIX 176..189
FT /evidence="ECO:0007829|PDB:5W95"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:5W95"
FT HELIX 197..199
FT /evidence="ECO:0007829|PDB:5W95"
FT STRAND 200..207
FT /evidence="ECO:0007829|PDB:5W95"
FT STRAND 215..218
FT /evidence="ECO:0007829|PDB:5W95"
FT HELIX 228..231
FT /evidence="ECO:0007829|PDB:5W95"
FT TURN 232..234
FT /evidence="ECO:0007829|PDB:5W95"
FT TURN 238..242
FT /evidence="ECO:0007829|PDB:5W95"
FT TURN 250..253
FT /evidence="ECO:0007829|PDB:5W95"
FT HELIX 254..259
FT /evidence="ECO:0007829|PDB:5W95"
FT STRAND 260..263
FT /evidence="ECO:0007829|PDB:5W95"
FT TURN 269..271
FT /evidence="ECO:0007829|PDB:5W95"
FT HELIX 275..278
FT /evidence="ECO:0007829|PDB:5W95"
FT TURN 280..282
FT /evidence="ECO:0007829|PDB:5W95"
FT HELIX 283..291
FT /evidence="ECO:0007829|PDB:5W95"
FT HELIX 298..300
FT /evidence="ECO:0007829|PDB:5W95"
FT STRAND 304..307
FT /evidence="ECO:0007829|PDB:5W95"
FT HELIX 315..328
FT /evidence="ECO:0007829|PDB:5W95"
SQ SEQUENCE 336 AA; 35448 MW; F374D163449C6547 CRC64;
MAKNSRRKRH RILAWIAAGA MASVVALVIV AVVIMLRGAE SPPSAVPPGV LPPGPTPAHP
HKPRPAFQDA SCPDVQMISV PGTWESSPQQ NPLNPVQFPK ALLLKVTGPI AQQFAPARVQ
TYTVAYTAQF HNPLTTDNQM SYNDSRAEGT RAMVAAMTDM NNRCPLTSYV LIGFSQGAVI
AGDVASDIGN GRGPVDEDLV LGVTLIADGR RQQGVGNQVP PSPRGEGAEI TLHEVPVLSG
LGLTMTGPRP GGFGALDGRT NEICAQGDLI CAAPAQAFSP ANLPTTLNTL AGGAGQPVHA
MYATPEFWNS DGEPATEWTL NWAHQLIENA PHPKHR
