PAPA5_MYCTU
ID PAPA5_MYCTU Reviewed; 422 AA.
AC P9WIN5; L0TE04; P96208;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=Phthiocerol/phthiodiolone dimycocerosyl transferase;
DE EC=2.3.1.282 {ECO:0000269|PubMed:15070765, ECO:0000269|PubMed:22361940, ECO:0000269|PubMed:26271001};
DE AltName: Full=Acyltransferase PapA5;
DE AltName: Full=Phthiocerol/phthiodiolone O-acyltransferase;
DE AltName: Full=Polyketide synthase-associated protein A5;
GN Name=papA5; OrderedLocusNames=Rv2939; ORFNames=MTCY19H9.07;
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 AS AN ACYLTRANSFERASE, ROLE IN PDIM SYNTHESIS, CATALYTIC ACTIVITY,
RP SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF
RP HIS-123; HIS-124; ASP-128 AND TYR-143.
RC STRAIN=ATCC 35801 / TMC 107 / Erdman;
RX PubMed=15070765; DOI=10.1073/pnas.0306928101;
RA Onwueme K.C., Ferreras J.A., Buglino J., Lima C.D., Quadri L.E.N.;
RT "Mycobacterial polyketide-associated proteins are acyltransferases: proof
RT of principle with Mycobacterium tuberculosis PapA5.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:4608-4613(2004).
RN [3]
RP ERRATUM OF PUBMED:15070765.
RX DOI=10.1073/pnas.0402005101;
RA Onwueme K.C., Ferreras J.A., Buglino J., Lima C.D., Quadri L.E.N.;
RL Proc. Natl. Acad. Sci. U.S.A. 101:6834-6834(2004).
RN [4]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, INTERACTION WITH MAS PROTEIN, AND
RP MUTAGENESIS OF ARG-234 AND ARG-312.
RC STRAIN=ATCC 25618 / H37Rv;
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 [5]
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 [6]
RP INTERACTION WITH FHAB, PHOSPHORYLATION, AND DEPHOSPHORYLATION BY PSTP.
RX PubMed=19826007; DOI=10.1074/jbc.m109.058834;
RA Gupta M., Sajid A., Arora G., Tandon V., Singh Y.;
RT "Forkhead-associated domain-containing protein Rv0019c and polyketide-
RT associated protein PapA5, from substrates of serine/threonine protein
RT kinase PknB to interacting proteins of Mycobacterium tuberculosis.";
RL J. Biol. Chem. 284:34723-34734(2009).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP 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 [8]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=22361940; DOI=10.1099/mic.0.057869-0;
RA Chavadi S.S., Onwueme K.C., Edupuganti U.R., Jerome J., Chatterjee D.,
RA Soll C.E., Quadri L.E.;
RT "The mycobacterial acyltransferase PapA5 is required for biosynthesis of
RT cell wall-associated phenolic glycolipids.";
RL Microbiology 158:1379-1387(2012).
RN [9]
RP CATALYTIC ACTIVITY, AND PHOSPHORYLATION AT THR-198.
RX PubMed=26271001; DOI=10.1021/acs.biochem.5b00455;
RA Touchette M.H., Bommineni G.R., Delle Bovi R.J., Gadbery J.E., Nicora C.D.,
RA Shukla A.K., Kyle J.E., Metz T.O., Martin D.W., Sampson N.S., Miller W.T.,
RA Tonge P.J., Seeliger J.C.;
RT "Diacyltransferase activity and chain length specificity of Mycobacterium
RT tuberculosis PapA5 in the synthesis of alkyl beta-diol lipids.";
RL Biochemistry 54:5457-5468(2015).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS), SUBUNIT, DOMAIN, AND ACTIVE SITES.
RC STRAIN=ATCC 35801 / TMC 107 / Erdman;
RX PubMed=15123643; DOI=10.1074/jbc.m404011200;
RA Buglino J., Onwueme K.C., Ferreras J.A., Quadri L.E.N., Lima C.D.;
RT "Crystal structure of PapA5, a phthiocerol dimycocerosyl transferase from
RT Mycobacterium tuberculosis.";
RL J. Biol. Chem. 279:30634-30642(2004).
CC -!- FUNCTION: Catalyzes diesterification of phthiocerol, phthiodiolone, and
CC phenolphthiocerol with mycocerosic acids, the final step in the
CC phthiocerol, phthiodiolone and phenolphthiocerol dimycocerosate esters
CC (PDIM) synthesis. Can directly transfer the mycocerosate bound to the
CC mycocerosic acid synthase (mas) onto the substrate alcohols. Is also
CC able to catalyze acyl transfer using various nucleophiles as acceptors
CC and several acyl-CoA thioesters as donors in vitro; preference is
CC observed for saturated medium chain alcohols and long chain acyl-CoA
CC thioesters. {ECO:0000269|PubMed:15070765, ECO:0000269|PubMed:15749014,
CC ECO:0000269|PubMed:22361940}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 a mycocerosyl-[mycocerosic acid synthase] + a phthiocerol =
CC a dimycocerosyl phthiocerol + 2 holo-[mycocerosic acid synthase].;
CC EC=2.3.1.282; Evidence={ECO:0000269|PubMed:22361940,
CC ECO:0000269|PubMed:26271001};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 a mycocerosyl-[mycocerosic acid synthase] + a phthiodiolone
CC = a dimycocerosyl phthiodiolone + 2 holo-[mycocerosic acid
CC synthase].; EC=2.3.1.282; Evidence={ECO:0000269|PubMed:22361940,
CC ECO:0000269|PubMed:26271001};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 a mycocerosyl-[mycocerosic acid synthase] + a
CC phenolphthiocerol = a dimycocerosyl phenolphthiocerol + 2 holo-
CC [mycocerosic acid synthase].; EC=2.3.1.282;
CC Evidence={ECO:0000269|PubMed:22361940, ECO:0000269|PubMed:26271001};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexadecanoyl-CoA + octan-1-ol = CoA + octyl hexadecanoyl;
CC Xref=Rhea:RHEA:44064, ChEBI:CHEBI:16188, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57379, ChEBI:CHEBI:84059;
CC Evidence={ECO:0000269|PubMed:15070765};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44065;
CC Evidence={ECO:0000269|PubMed:15070765};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexadecanoyl-CoA + nonan-1-ol = CoA + nonyl hexadecanoate;
CC Xref=Rhea:RHEA:44112, ChEBI:CHEBI:35986, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57379, ChEBI:CHEBI:84062;
CC Evidence={ECO:0000269|PubMed:15070765};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44113;
CC Evidence={ECO:0000269|PubMed:15070765};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=decan-1-ol + hexadecanoyl-CoA = CoA + decanyl hexadecanoate;
CC Xref=Rhea:RHEA:44096, ChEBI:CHEBI:28903, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57379, ChEBI:CHEBI:84063;
CC Evidence={ECO:0000269|PubMed:15070765};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44097;
CC Evidence={ECO:0000269|PubMed:15070765};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexadecanoyl-CoA + tetradecan-1-ol = CoA + tetradecanyl
CC hexadecanoate; Xref=Rhea:RHEA:44124, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57379, ChEBI:CHEBI:77417, ChEBI:CHEBI:84064;
CC Evidence={ECO:0000269|PubMed:15070765};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44125;
CC Evidence={ECO:0000269|PubMed:15070765};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexadecan-1-ol + hexadecanoyl-CoA = CoA + hexadecanyl
CC hexadecanoate; Xref=Rhea:RHEA:38167, ChEBI:CHEBI:16125,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:75584;
CC Evidence={ECO:0000269|PubMed:15070765};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38168;
CC Evidence={ECO:0000269|PubMed:15070765};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexadecanoyl-CoA + octadecan-1-ol = CoA + octadecanyl
CC hexadecanoate; Xref=Rhea:RHEA:44120, ChEBI:CHEBI:32154,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:84066;
CC Evidence={ECO:0000269|PubMed:15070765};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44121;
CC Evidence={ECO:0000269|PubMed:15070765};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=eicosan-1-ol + hexadecanoyl-CoA = CoA + eicosanyl
CC hexadecanoate; Xref=Rhea:RHEA:44116, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57379, ChEBI:CHEBI:75627, ChEBI:CHEBI:84065;
CC Evidence={ECO:0000269|PubMed:15070765};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44117;
CC Evidence={ECO:0000269|PubMed:15070765};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9E)-octadecenoyl-CoA + hexadecan-1-ol = CoA + hexadecanyl
CC (9E)-octadecenoate; Xref=Rhea:RHEA:44128, ChEBI:CHEBI:16125,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:77537, ChEBI:CHEBI:84072;
CC Evidence={ECO:0000269|PubMed:15070765};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44129;
CC Evidence={ECO:0000269|PubMed:15070765};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + hexadecan-1-ol = CoA + hexadecanyl
CC (9Z)-octadecenoate; Xref=Rhea:RHEA:38227, ChEBI:CHEBI:16125,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:75622;
CC Evidence={ECO:0000269|PubMed:15070765};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38228;
CC Evidence={ECO:0000269|PubMed:15070765};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dodecanoyl-CoA + hexadecan-1-ol = CoA + hexadecanyl
CC dodecanoate; Xref=Rhea:RHEA:44136, ChEBI:CHEBI:16125,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57375, ChEBI:CHEBI:84080;
CC Evidence={ECO:0000269|PubMed:15070765};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44137;
CC Evidence={ECO:0000269|PubMed:15070765};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexadecan-1-ol + octadecanoyl-CoA = CoA + hexadecanyl
CC octadecanoate; Xref=Rhea:RHEA:38251, ChEBI:CHEBI:16125,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57394, ChEBI:CHEBI:75631;
CC Evidence={ECO:0000269|PubMed:15070765};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38252;
CC Evidence={ECO:0000269|PubMed:15070765};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=500 uM for 1-octanol {ECO:0000269|PubMed:15070765};
CC KM=24 uM for 2-dodecanol {ECO:0000269|PubMed:15749014};
CC KM=4 uM for palmitoyl-CoA {ECO:0000269|PubMed:15070765};
CC KM=118 uM for lauroyl-CoA {ECO:0000269|PubMed:15749014};
CC KM=0.39 uM for mycoserosate acylated to mas protein
CC {ECO:0000269|PubMed:15749014};
CC pH dependence:
CC Optimum pH is 6.5. {ECO:0000269|PubMed:15070765};
CC -!- SUBUNIT: Monomer. Interacts directly with the acyl carrier protein
CC (ACP) domain of the mycocerosic acid synthase (mas) protein. Interacts
CC with FhaB. {ECO:0000269|PubMed:15123643, ECO:0000269|PubMed:15749014,
CC ECO:0000269|PubMed:19826007}.
CC -!- DOMAIN: Consists of two structural domains that are related to each
CC other. {ECO:0000269|PubMed:15123643}.
CC -!- PTM: Phosphorylated by PknB at Thr-198 (PubMed:19826007,
CC PubMed:26271001). Dephosphorylated by PstP (PubMed:19826007).
CC {ECO:0000269|PubMed:19826007, ECO:0000269|PubMed:26271001}.
CC -!- MISCELLANEOUS: Was identified as a high-confidence drug target.
CC -!- SIMILARITY: Belongs to the acyltransferase PapA5 family. {ECO:0000305}.
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DR EMBL; AL123456; CCP45742.1; -; Genomic_DNA.
DR PIR; G70984; G70984.
DR RefSeq; NP_217455.1; NC_000962.3.
DR RefSeq; WP_003414853.1; NZ_NVQJ01000015.1.
DR PDB; 1Q9J; X-ray; 2.75 A; A/B=1-422.
DR PDBsum; 1Q9J; -.
DR AlphaFoldDB; P9WIN5; -.
DR SMR; P9WIN5; -.
DR STRING; 83332.Rv2939; -.
DR SwissLipids; SLP:000001034; -.
DR iPTMnet; P9WIN5; -.
DR PaxDb; P9WIN5; -.
DR DNASU; 887327; -.
DR GeneID; 45426927; -.
DR GeneID; 887327; -.
DR KEGG; mtu:Rv2939; -.
DR TubercuList; Rv2939; -.
DR eggNOG; COG1020; Bacteria.
DR OMA; EMFAETH; -.
DR BioCyc; MetaCyc:G185E-7192-MON; -.
DR BRENDA; 2.3.1.282; 3445.
DR Reactome; R-MTU-9635470; Dimycocersyl phthiocerol biosynthesis.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IDA:MTBBASE.
DR GO; GO:0008374; F:O-acyltransferase activity; IDA:MTBBASE.
DR GO; GO:0016740; F:transferase activity; TAS:Reactome.
DR GO; GO:0071770; P:DIM/DIP cell wall layer assembly; IDA:MTBBASE.
DR GO; GO:0008610; P:lipid biosynthetic process; IDA:MTBBASE.
DR Gene3D; 3.30.559.10; -; 1.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR031641; PapA_C.
DR Pfam; PF16911; PapA_C; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Acyltransferase; Lipid biosynthesis;
KW Lipid metabolism; Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..422
FT /note="Phthiocerol/phthiodiolone dimycocerosyl transferase"
FT /id="PRO_0000058229"
FT ACT_SITE 124
FT /note="Proton acceptor"
FT /evidence="ECO:0000269|PubMed:15123643"
FT SITE 128
FT /note="Structural role in the organization of the active
FT site"
FT SITE 312
FT /note="Important for mas ACP domain recognition"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:21969609"
FT MOD_RES 198
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:26271001"
FT MUTAGEN 123
FT /note="H->A: About 2-fold decrease in activity."
FT /evidence="ECO:0000269|PubMed:15070765"
FT MUTAGEN 124
FT /note="H->A: 76-fold decrease in activity."
FT /evidence="ECO:0000269|PubMed:15070765"
FT MUTAGEN 128
FT /note="D->A: 65-fold decrease in activity."
FT /evidence="ECO:0000269|PubMed:15070765"
FT MUTAGEN 143
FT /note="Y->F: Less than 1.9-fold decrease in activity."
FT /evidence="ECO:0000269|PubMed:15070765"
FT MUTAGEN 234
FT /note="R->E: 4-fold decrease in affinity for acylated mas
FT protein. No change in catalytic activity."
FT /evidence="ECO:0000269|PubMed:15749014"
FT MUTAGEN 312
FT /note="R->E: 40-fold decrease in affinity for acylated mas
FT protein. No change in catalytic activity."
FT /evidence="ECO:0000269|PubMed:15749014"
FT STRAND 5..9
FT /evidence="ECO:0007829|PDB:1Q9J"
FT HELIX 12..19
FT /evidence="ECO:0007829|PDB:1Q9J"
FT STRAND 23..32
FT /evidence="ECO:0007829|PDB:1Q9J"
FT HELIX 36..49
FT /evidence="ECO:0007829|PDB:1Q9J"
FT HELIX 51..53
FT /evidence="ECO:0007829|PDB:1Q9J"
FT STRAND 54..59
FT /evidence="ECO:0007829|PDB:1Q9J"
FT STRAND 63..69
FT /evidence="ECO:0007829|PDB:1Q9J"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:1Q9J"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:1Q9J"
FT TURN 100..102
FT /evidence="ECO:0007829|PDB:1Q9J"
FT STRAND 104..110
FT /evidence="ECO:0007829|PDB:1Q9J"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:1Q9J"
FT STRAND 117..123
FT /evidence="ECO:0007829|PDB:1Q9J"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:1Q9J"
FT HELIX 129..148
FT /evidence="ECO:0007829|PDB:1Q9J"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:1Q9J"
FT HELIX 164..170
FT /evidence="ECO:0007829|PDB:1Q9J"
FT TURN 186..189
FT /evidence="ECO:0007829|PDB:1Q9J"
FT STRAND 213..216
FT /evidence="ECO:0007829|PDB:1Q9J"
FT HELIX 220..230
FT /evidence="ECO:0007829|PDB:1Q9J"
FT TURN 231..234
FT /evidence="ECO:0007829|PDB:1Q9J"
FT HELIX 237..253
FT /evidence="ECO:0007829|PDB:1Q9J"
FT STRAND 260..267
FT /evidence="ECO:0007829|PDB:1Q9J"
FT TURN 268..271
FT /evidence="ECO:0007829|PDB:1Q9J"
FT STRAND 272..274
FT /evidence="ECO:0007829|PDB:1Q9J"
FT TURN 278..280
FT /evidence="ECO:0007829|PDB:1Q9J"
FT STRAND 285..292
FT /evidence="ECO:0007829|PDB:1Q9J"
FT HELIX 300..317
FT /evidence="ECO:0007829|PDB:1Q9J"
FT HELIX 319..322
FT /evidence="ECO:0007829|PDB:1Q9J"
FT HELIX 327..332
FT /evidence="ECO:0007829|PDB:1Q9J"
FT STRAND 336..338
FT /evidence="ECO:0007829|PDB:1Q9J"
FT STRAND 342..345
FT /evidence="ECO:0007829|PDB:1Q9J"
FT STRAND 360..368
FT /evidence="ECO:0007829|PDB:1Q9J"
FT STRAND 371..373
FT /evidence="ECO:0007829|PDB:1Q9J"
FT STRAND 378..384
FT /evidence="ECO:0007829|PDB:1Q9J"
FT STRAND 387..395
FT /evidence="ECO:0007829|PDB:1Q9J"
FT HELIX 399..412
FT /evidence="ECO:0007829|PDB:1Q9J"
FT TURN 413..415
FT /evidence="ECO:0007829|PDB:1Q9J"
SQ SEQUENCE 422 AA; 45429 MW; 19156C6B9FCC3AA7 CRC64;
MFPGSVIRKL SHSEEVFAQY EVFTSMTIQL RGVIDVDALS DAFDALLETH PVLASHLEQS
SDGGWNLVAD DLLHSGICVI DGTAATNGSP SGNAELRLDQ SVSLLHLQLI LREGGAELTL
YLHHCMADGH HGAVLVDELF SRYTDAVTTG DPGPITPQPT PLSMEAVLAQ RGIRKQGLSG
AERFMSVMYA YEIPATETPA VLAHPGLPQA VPVTRLWLSK QQTSDLMAFG REHRLSLNAV
VAAAILLTEW QLRNTPHVPI PYVYPVDLRF VLAPPVAPTE ATNLLGAASY LAEIGPNTDI
VDLASDIVAT LRADLANGVI QQSGLHFGTA FEGTPPGLPP LVFCTDATSF PTMRTPPGLE
IEDIKGQFYC SISVPLDLYS CAVYAGQLII EHHGHIAEPG KSLEAIRSLL CTVPSEYGWI
ME
