BACD_BACSU
ID BACD_BACSU Reviewed; 472 AA.
AC P39641;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Alanine--anticapsin ligase {ECO:0000303|PubMed:23317005};
DE EC=6.3.2.49 {ECO:0000269|PubMed:16030213, ECO:0000269|PubMed:22407814, ECO:0000269|PubMed:23317005, ECO:0000269|PubMed:24702628};
DE AltName: Full=ATP-dependent dipeptide ligase {ECO:0000303|PubMed:22407814};
DE AltName: Full=Bacilysin synthetase {ECO:0000303|PubMed:12372825};
DE AltName: Full=L-Ala-L-amino acid dipeptide ligase {ECO:0000303|PubMed:23317005};
DE AltName: Full=L-alanine--L-anticapsin ligase {ECO:0000303|PubMed:23317005};
DE AltName: Full=L-amino acid ligase {ECO:0000303|PubMed:16030213};
DE Short=Lal {ECO:0000303|PubMed:16030213};
GN Name=bacD {ECO:0000303|PubMed:15609023};
GN Synonyms=ywfE {ECO:0000303|PubMed:16030213}; OrderedLocusNames=BSU37710;
GN ORFNames=ipa-83d;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=7934828; DOI=10.1111/j.1365-2958.1993.tb01963.x;
RA Glaser P., Kunst F., Arnaud M., Coudart M.P., Gonzales W., Hullo M.-F.,
RA Ionescu M., Lubochinsky B., Marcelino L., Moszer I., Presecan E.,
RA Santana M., Schneider E., Schweizer J., Vertes A., Rapoport G., Danchin A.;
RT "Bacillus subtilis genome project: cloning and sequencing of the 97 kb
RT region from 325 degrees to 333 degrees.";
RL Mol. Microbiol. 10:371-384(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP INDUCTION.
RC STRAIN=168 / 61884;
RX PubMed=12372825; DOI=10.1074/jbc.m208722200;
RA Inaoka T., Takahashi K., Ohnishi-Kameyama M., Yoshida M., Ochi K.;
RT "Guanine nucleotides guanosine 5'-diphosphate 3'-diphosphate and GTP co-
RT operatively regulate the production of an antibiotic bacilysin in Bacillus
RT subtilis.";
RL J. Biol. Chem. 278:2169-2176(2003).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RC STRAIN=ATCC 15245 / 3349 / IAM 1-3;
RX PubMed=16030213; DOI=10.1128/jb.187.15.5195-5202.2005;
RA Tabata K., Ikeda H., Hashimoto S.;
RT "ywfE in Bacillus subtilis codes for a novel enzyme, L-amino acid ligase.";
RL J. Bacteriol. 187:5195-5202(2005).
RN [5]
RP FUNCTION IN BACILYSIN PRODUCTION, AND GENE NAME.
RX PubMed=15609023; DOI=10.1007/s00203-004-0743-8;
RA Steinborn G., Hajirezaei M.-R., Hofemeister J.;
RT "bac genes for recombinant bacilysin and anticapsin production in Bacillus
RT host strains.";
RL Arch. Microbiol. 183:71-79(2005).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND SUBSTRATE SPECIFICITY.
RX PubMed=23317005; DOI=10.1021/bi3016229;
RA Parker J.B., Walsh C.T.;
RT "Action and timing of BacC and BacD in the late stages of biosynthesis of
RT the dipeptide antibiotic bacilysin.";
RL Biochemistry 52:889-901(2013).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG;
RP ADP AND MAGNESIUM, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, MUTAGENESIS OF TYR-75 AND SER-184, COFACTOR, REACTION
RP MECHANISM, AND SUBUNIT.
RX PubMed=22407814; DOI=10.1002/pro.2058;
RA Shomura Y., Hinokuchi E., Ikeda H., Senoo A., Takahashi Y., Saito J.,
RA Komori H., Shibata N., Yonetani Y., Higuchi Y.;
RT "Structural and enzymatic characterization of BacD, an L-amino acid
RT dipeptide ligase from Bacillus subtilis.";
RL Protein Sci. 21:707-716(2012).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 4-468 OF WILD-TYPE AND MUTANT
RP ALA-332 IN COMPLEX WITH ADP; ALANINE AND PHOSPHATE, FUNCTION, CATALYTIC
RP ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF GLU-109; GLU-273;
RP HIS-309; GLU-311; ARG-328 AND TRP-332, COFACTOR, SUBUNIT, AND REACTION
RP MECHANISM.
RX PubMed=24702628; DOI=10.1021/bi500292b;
RA Tsuda T., Asami M., Koguchi Y., Kojima S.;
RT "Single mutation alters the substrate specificity of L-amino acid ligase.";
RL Biochemistry 53:2650-2660(2014).
CC -!- FUNCTION: Part of the bacABCDEFG operon responsible for the
CC biosynthesis of bacilysin, an irreversible inactivator of the
CC glutaminase domain of glucosamine synthetase. Catalyzes the formation
CC of alpha-dipeptides from various L-amino acids in the presence of ATP.
CC In vivo catalyzes the ligation of L-alanine and L-anticapsin
CC (epoxycyclohexanonyl-Ala) to produce the final bacilysin antibiotic (L-
CC Ala-L-4S-cyclohexenonyl-Ala dipeptide). The substrate specificity is
CC restricted to small amino acids such as L-Ala, for the N-terminal end
CC of the dipeptide, whereas a wide range of hydrophobic amino acids such
CC as L-Phe, L-Tyr and L-Met are recognized for the C-terminal end.
CC {ECO:0000269|PubMed:15609023, ECO:0000269|PubMed:16030213,
CC ECO:0000269|PubMed:22407814, ECO:0000269|PubMed:23317005,
CC ECO:0000269|PubMed:24702628}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-alanine + L-anticapsin = ADP + bacilysin + H(+) +
CC phosphate; Xref=Rhea:RHEA:44332, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57972,
CC ChEBI:CHEBI:84310, ChEBI:CHEBI:84311, ChEBI:CHEBI:456216;
CC EC=6.3.2.49; Evidence={ECO:0000269|PubMed:16030213,
CC ECO:0000269|PubMed:22407814, ECO:0000269|PubMed:23317005,
CC ECO:0000269|PubMed:24702628};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:22407814, ECO:0000269|PubMed:24702628};
CC Note=Binds 2 Mg(2+) ions per monomer. {ECO:0000269|PubMed:22407814,
CC ECO:0000269|PubMed:24702628};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.07 mM for ATP {ECO:0000269|PubMed:16030213};
CC KM=0.42 mM for L-alanine {ECO:0000269|PubMed:16030213};
CC KM=1.64 mM for L-alanine {ECO:0000269|PubMed:24702628};
CC KM=1.7 mM for L-alanine {ECO:0000269|PubMed:22407814};
CC KM=5.23 mM for L-phenylalanine {ECO:0000269|PubMed:24702628};
CC KM=20 mM for L-phenylalanine {ECO:0000269|PubMed:22407814};
CC KM=105.0 mM for L-glutamine {ECO:0000269|PubMed:16030213};
CC Vmax=0.764 umol/min/mg enzyme for Ala-Gln synthesis
CC {ECO:0000269|PubMed:16030213};
CC Note=kcat is 9.32 sec(-1) for ligase activity with alanine as
CC substrate (PubMed:24702628). kcat is 10.4 sec(-1) for ligase activity
CC with phenylalanine as substrate (PubMed:24702628). kcat is 630 min(-
CC 1) for ligase activity with alanine and phenylalanine as substrate
CC (PubMed:22407814). {ECO:0000269|PubMed:22407814,
CC ECO:0000269|PubMed:24702628};
CC pH dependence:
CC Optimum pH is 9.5. {ECO:0000269|PubMed:16030213};
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius.
CC {ECO:0000269|PubMed:16030213};
CC -!- PATHWAY: Antibiotic biosynthesis; bacilysin biosynthesis.
CC {ECO:0000305|PubMed:23317005}.
CC -!- SUBUNIT: Monomer or homodimer. {ECO:0000269|PubMed:22407814,
CC ECO:0000269|PubMed:24702628}.
CC -!- INDUCTION: The compound guanosine 5'-diphosphate 3'-diphosphate (ppGpp)
CC is essential for the transcription of the bacABCDE operon and GTP
CC regulates the transcription of both this operon and ywfH via the CodY-
CC mediated regulation system. {ECO:0000269|PubMed:12372825}.
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DR EMBL; X73124; CAA51639.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15798.1; -; Genomic_DNA.
DR PIR; S39738; S39738.
DR RefSeq; NP_391651.1; NC_000964.3.
DR RefSeq; WP_003242921.1; NZ_JNCM01000034.1.
DR PDB; 3VMM; X-ray; 2.50 A; A=1-472.
DR PDB; 3WNZ; X-ray; 1.90 A; A=4-468.
DR PDB; 3WO0; X-ray; 2.00 A; A=4-468.
DR PDB; 3WO1; X-ray; 2.30 A; A=4-468.
DR PDBsum; 3VMM; -.
DR PDBsum; 3WNZ; -.
DR PDBsum; 3WO0; -.
DR PDBsum; 3WO1; -.
DR AlphaFoldDB; P39641; -.
DR SMR; P39641; -.
DR STRING; 224308.BSU37710; -.
DR PaxDb; P39641; -.
DR PRIDE; P39641; -.
DR DNASU; 937214; -.
DR EnsemblBacteria; CAB15798; CAB15798; BSU_37710.
DR GeneID; 937214; -.
DR KEGG; bsu:BSU37710; -.
DR PATRIC; fig|224308.179.peg.4083; -.
DR eggNOG; COG0151; Bacteria.
DR InParanoid; P39641; -.
DR OMA; FIAPMAK; -.
DR PhylomeDB; P39641; -.
DR BioCyc; BSUB:BSU37710-MON; -.
DR BioCyc; MetaCyc:MON-19123; -.
DR BRENDA; 6.3.2.49; 658.
DR SABIO-RK; P39641; -.
DR UniPathway; UPA00100; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0034026; F:L-amino-acid alpha-ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.30.1490.20; -; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic biosynthesis; ATP-binding; Ligase; Magnesium;
KW Metal-binding; Nucleotide-binding; Reference proteome.
FT CHAIN 1..472
FT /note="Alanine--anticapsin ligase"
FT /id="PRO_0000064804"
FT DOMAIN 142..355
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 109
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:22407814"
FT BINDING 138
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:22407814,
FT ECO:0000269|PubMed:24702628"
FT BINDING 178
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:22407814,
FT ECO:0000269|PubMed:24702628"
FT BINDING 182
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:22407814"
FT BINDING 184..185
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:22407814,
FT ECO:0000269|PubMed:24702628"
FT BINDING 226..229
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:22407814,
FT ECO:0000269|PubMed:24702628"
FT BINDING 268
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:22407814,
FT ECO:0000269|PubMed:24702628"
FT BINDING 273
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:24702628"
FT BINDING 309..311
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:22407814,
FT ECO:0000269|PubMed:24702628"
FT BINDING 311
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:22407814,
FT ECO:0000269|PubMed:24702628"
FT BINDING 324
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:22407814,
FT ECO:0000269|PubMed:24702628"
FT BINDING 324
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:22407814,
FT ECO:0000269|PubMed:24702628"
FT BINDING 328..331
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:22407814,
FT ECO:0000269|PubMed:24702628"
FT SITE 332
FT /note="Plays a key role in restricting the N-terminal
FT substrate specificity to small amino acids such as L-Ala"
FT /evidence="ECO:0000269|PubMed:24702628"
FT MUTAGEN 75
FT /note="Y->F: Almost no effect on catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:22407814"
FT MUTAGEN 109
FT /note="E->A: Loss of ligase activity."
FT /evidence="ECO:0000269|PubMed:24702628"
FT MUTAGEN 184
FT /note="S->A: Almost no effect on catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:22407814"
FT MUTAGEN 273
FT /note="E->A: Loss of ligase activity."
FT /evidence="ECO:0000269|PubMed:24702628"
FT MUTAGEN 309
FT /note="H->R: Loss of ligase activity."
FT /evidence="ECO:0000269|PubMed:24702628"
FT MUTAGEN 311
FT /note="E->D: Loss of ligase activity."
FT /evidence="ECO:0000269|PubMed:24702628"
FT MUTAGEN 328
FT /note="R->K: Loss of ligase activity."
FT /evidence="ECO:0000269|PubMed:24702628"
FT MUTAGEN 332
FT /note="W->A: Hydrolyzes ATP, even in the absence of L-Ala,
FT and the structure appears to show a cavity in the N-
FT terminal substrate-binding pocket. Also alters the
FT substrate specificity and activity depending on the size
FT and shape of substituted amino acids."
FT /evidence="ECO:0000269|PubMed:24702628"
FT STRAND 5..9
FT /evidence="ECO:0007829|PDB:3WNZ"
FT STRAND 12..15
FT /evidence="ECO:0007829|PDB:3WNZ"
FT HELIX 17..27
FT /evidence="ECO:0007829|PDB:3WNZ"
FT STRAND 28..35
FT /evidence="ECO:0007829|PDB:3WNZ"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:3WNZ"
FT HELIX 42..51
FT /evidence="ECO:0007829|PDB:3WNZ"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:3WNZ"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:3WNZ"
FT HELIX 65..68
FT /evidence="ECO:0007829|PDB:3WNZ"
FT HELIX 85..99
FT /evidence="ECO:0007829|PDB:3WNZ"
FT STRAND 102..107
FT /evidence="ECO:0007829|PDB:3WNZ"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:3WNZ"
FT HELIX 112..122
FT /evidence="ECO:0007829|PDB:3WNZ"
FT HELIX 129..134
FT /evidence="ECO:0007829|PDB:3WNZ"
FT HELIX 138..147
FT /evidence="ECO:0007829|PDB:3WNZ"
FT STRAND 155..158
FT /evidence="ECO:0007829|PDB:3WNZ"
FT HELIX 161..171
FT /evidence="ECO:0007829|PDB:3WNZ"
FT STRAND 173..181
FT /evidence="ECO:0007829|PDB:3WNZ"
FT TURN 184..187
FT /evidence="ECO:0007829|PDB:3WNZ"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:3WNZ"
FT TURN 194..196
FT /evidence="ECO:0007829|PDB:3WNZ"
FT HELIX 197..208
FT /evidence="ECO:0007829|PDB:3WNZ"
FT STRAND 220..227
FT /evidence="ECO:0007829|PDB:3WNZ"
FT HELIX 233..236
FT /evidence="ECO:0007829|PDB:3WNZ"
FT STRAND 238..242
FT /evidence="ECO:0007829|PDB:3WNZ"
FT STRAND 244..253
FT /evidence="ECO:0007829|PDB:3WNZ"
FT STRAND 256..265
FT /evidence="ECO:0007829|PDB:3WNZ"
FT STRAND 275..279
FT /evidence="ECO:0007829|PDB:3WNZ"
FT HELIX 284..301
FT /evidence="ECO:0007829|PDB:3WNZ"
FT STRAND 305..315
FT /evidence="ECO:0007829|PDB:3WNZ"
FT HELIX 316..318
FT /evidence="ECO:0007829|PDB:3WNZ"
FT STRAND 319..328
FT /evidence="ECO:0007829|PDB:3WNZ"
FT HELIX 334..342
FT /evidence="ECO:0007829|PDB:3WNZ"
FT HELIX 346..356
FT /evidence="ECO:0007829|PDB:3WNZ"
FT HELIX 357..359
FT /evidence="ECO:0007829|PDB:3WNZ"
FT STRAND 364..366
FT /evidence="ECO:0007829|PDB:3WNZ"
FT STRAND 371..379
FT /evidence="ECO:0007829|PDB:3WNZ"
FT HELIX 381..386
FT /evidence="ECO:0007829|PDB:3WNZ"
FT STRAND 395..403
FT /evidence="ECO:0007829|PDB:3WNZ"
FT STRAND 414..420
FT /evidence="ECO:0007829|PDB:3WNZ"
FT STRAND 426..431
FT /evidence="ECO:0007829|PDB:3WNZ"
FT HELIX 433..435
FT /evidence="ECO:0007829|PDB:3WNZ"
FT STRAND 439..446
FT /evidence="ECO:0007829|PDB:3WNZ"
FT HELIX 448..461
FT /evidence="ECO:0007829|PDB:3WNZ"
FT STRAND 463..467
FT /evidence="ECO:0007829|PDB:3WNZ"
SQ SEQUENCE 472 AA; 52267 MW; 0300F4FA6327976A CRC64;
MERKTVLVIA DLGGCPPHMF YKSAAEKYNL VSFIPRPFAI TASHAALIEK YSVAVIKDKD
YFKSLADFEH PDSIYWAHED HNKPEEEVVE QIVKVAEMFG ADAITTNNEL FIAPMAKACE
RLGLRGAGVQ AAENARDKNK MRDAFNKAGV KSIKNKRVTT LEDFRAALEE IGTPLILKPT
YLASSIGVTL ITDTETAEDE FNRVNDYLKS INVPKAVTFE APFIAEEFLQ GEYGDWYQTE
GYSDYISIEG IMADGEYFPI AIHDKTPQIG FTETSHITPS ILDEEAKKKI VEAAKKANEG
LGLQNCATHT EIKLMKNREP GLIESAARFA GWNMIPNIKK VFGLDMAQLL LDVLCFGKDA
DLPDGLLDQE PYYVADCHLY PQHFKQNGQI PETAEDLVIE AIDIPDGLLK GDTEIVSFSA
AAPGTSVDLT LFEAFNSIAA FELKGSNSQD VAESIRQIQQ HAKLTAKYVL PV
