PAC_ECOLX
ID PAC_ECOLX Reviewed; 846 AA.
AC P06875; Q47434; Q47435; Q47436; Q47437; Q60253;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Penicillin G acylase;
DE EC=3.5.1.11;
DE AltName: Full=Penicillin G amidase;
DE AltName: Full=Penicillin G amidohydrolase;
DE Contains:
DE RecName: Full=Penicillin G acylase subunit alpha;
DE Contains:
DE RecName: Full=Penicillin G acylase subunit beta;
DE Flags: Precursor;
GN Name=pac;
OS Escherichia coli.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3016663; DOI=10.1093/nar/14.14.5713;
RA Schumacher G., Sizmann D., Haug H., Buckel P., Boeck A.;
RT "Penicillin acylase from E. coli: unique gene-protein relation.";
RL Nucleic Acids Res. 14:5713-5727(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3315861; DOI=10.1016/0378-1119(87)90161-2;
RA Oh S.-J., Kim Y.-C., Park Y.-W., Min S.-Y., Kim I.-S., Kang H.-S.;
RT "Complete nucleotide sequence of the penicillin G acylase gene and the
RT flanking regions, and its expression in Escherichia coli.";
RL Gene 56:87-97(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-368.
RC STRAIN=W / ATCC 11105 / DSM 1900 / 113-3;
RX PubMed=3005131; DOI=10.1016/0378-1119(85)90018-6;
RA Oliver G., Valle F., Rosetti F., Gomez-Pedrozo M., Santamaria P.,
RA Gosset G., Bolivar F.;
RT "A common precursor for the two subunits of the penicillin acylase from
RT Escherichia coli ATCC11105.";
RL Gene 40:9-14(1985).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-368.
RX PubMed=3556321; DOI=10.1016/0378-1119(86)90316-1;
RA Valle F., Gosset G., Tenorio B., Oliver G., Bolivar F.;
RT "Characterization of the regulatory region of the Escherichia coli
RT penicillin acylase structural gene.";
RL Gene 50:119-122(1986).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-350 AND 741-846.
RX PubMed=2989404;
RA Bruns W., Hoppe J., Tsai H., Bruning H.J., Maywald F., Collins J.,
RA Mayer H.;
RT "Structure of the penicillin acylase gene from Escherichia coli: a
RT periplasmic enzyme that undergoes multiple proteolytic processing.";
RL J. Mol. Appl. Genet. 3:36-44(1985).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-95.
RC STRAIN=W / ATCC 11105 / DSM 1900 / 113-3;
RA Radoja S., Francetic O., Stojicevic N., Moric I., Glisin S.,
RA Konstantinovic M.;
RT "Transcriptional and gene fusion analyses of the Escherichia coli
RT penicillin amidase gene expression.";
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP PROTEIN SEQUENCE OF 27-36 AND 291-299.
RC STRAIN=W / ATCC 11105 / DSM 1900 / 113-3;
RX PubMed=1849824; DOI=10.1111/j.1432-1033.1991.tb15884.x;
RA Slade A., Horrocks A.J., Lindsay C.D., Dunbar B., Virden R.;
RT "Site-directed chemical conversion of serine to cysteine in penicillin
RT acylase from Escherichia coli ATCC 11105. Effect on conformation and
RT catalytic activity.";
RL Eur. J. Biochem. 197:75-80(1991).
RN [8]
RP PROTEOLYTIC PROCESSING.
RX PubMed=2205499; DOI=10.1111/j.1432-1033.1990.tb19207.x;
RA Sizmann D., Keilmann C., Boeck A.;
RT "Primary structure requirements for the maturation in vivo of penicillin
RT acylase from Escherichia coli ATCC 11105.";
RL Eur. J. Biochem. 192:143-151(1990).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), AND MUTAGENESIS OF SER-290.
RC STRAIN=W / ATCC 11105 / DSM 1900 / 113-3;
RX PubMed=7816145; DOI=10.1038/373264a0;
RA Duggleby H.J., Tolley S.P., Hill C.P., Dodson E.J., Dodson G.,
RA Moody P.C.E.;
RT "Penicillin acylase has a single-amino-acid catalytic centre.";
RL Nature 373:264-268(1995).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 27-235.
RX PubMed=11601852; DOI=10.1006/jmbi.2001.5043;
RA McVey C.E., Walsh M.A., Dodson G.G., Wilson K.S., Brannigan J.A.;
RT "Crystal structures of penicillin acylase enzyme-substrate complexes:
RT structural insights into the catalytic mechanism.";
RL J. Mol. Biol. 313:139-150(2001).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + penicillin = 6-aminopenicillanate + a carboxylate;
CC Xref=Rhea:RHEA:18693, ChEBI:CHEBI:15377, ChEBI:CHEBI:29067,
CC ChEBI:CHEBI:51356, ChEBI:CHEBI:57869; EC=3.5.1.11;
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Note=Binds 1 Ca(2+) ion per dimer.;
CC -!- SUBUNIT: Heterodimer of an alpha subunit and a beta subunit processed
CC from the same precursor.
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- SIMILARITY: Belongs to the peptidase S45 family. {ECO:0000305}.
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DR EMBL; M15950; AAA24269.1; -; Genomic_DNA.
DR EMBL; X04114; CAA27728.1; -; Genomic_DNA.
DR EMBL; M17609; AAA24324.1; -; Genomic_DNA.
DR EMBL; M14424; AAA24270.1; -; Genomic_DNA.
DR EMBL; M11672; AAA24258.1; -; Genomic_DNA.
DR EMBL; M12373; AAA24259.1; -; Genomic_DNA.
DR EMBL; AF109125; AAD19653.1; -; Genomic_DNA.
DR PIR; A23593; PNECA.
DR RefSeq; WP_000797400.1; NZ_WVWF01000016.1.
DR PDB; 1AI4; X-ray; 2.35 A; A=27-235, B=290-846.
DR PDB; 1AI5; X-ray; 2.36 A; A=27-235, B=290-846.
DR PDB; 1AI6; X-ray; 2.55 A; A=27-235, B=290-846.
DR PDB; 1AI7; X-ray; 2.50 A; A=27-235, B=290-846.
DR PDB; 1AJN; X-ray; 2.36 A; A=27-235, B=290-846.
DR PDB; 1AJP; X-ray; 2.31 A; A=27-235, B=290-846.
DR PDB; 1AJQ; X-ray; 2.05 A; A=27-235, B=290-846.
DR PDB; 1E3A; X-ray; 1.80 A; A=27-286, B=287-846.
DR PDB; 1FXH; X-ray; 1.97 A; A=27-235, B=290-846.
DR PDB; 1FXV; X-ray; 2.25 A; A=27-235, B=290-846.
DR PDB; 1GK9; X-ray; 1.30 A; A=27-286, B=290-846.
DR PDB; 1GKF; X-ray; 1.41 A; A=27-286, B=290-846.
DR PDB; 1GM7; X-ray; 1.45 A; A=27-235, B=290-846.
DR PDB; 1GM8; X-ray; 2.00 A; A=27-235, B=290-846.
DR PDB; 1GM9; X-ray; 1.80 A; A=27-235, B=290-846.
DR PDB; 1H2G; X-ray; 2.00 A; A=27-235, B=290-846.
DR PDB; 1JX9; X-ray; 2.28 A; A=26-234, B=290-846.
DR PDB; 1K5Q; X-ray; 2.34 A; A=26-234, B=290-846.
DR PDB; 1K5S; X-ray; 2.43 A; A=26-234, B=290-846.
DR PDB; 1K7D; X-ray; 2.15 A; A=26-234, B=290-846.
DR PDB; 1KEC; X-ray; 2.30 A; A=26-234, B=290-846.
DR PDB; 1PNK; X-ray; 1.90 A; A=27-235, B=290-846.
DR PDB; 1PNL; X-ray; 2.50 A; A=27-235, B=290-846.
DR PDB; 1PNM; X-ray; 2.50 A; A=27-235, B=290-846.
DR PDBsum; 1AI4; -.
DR PDBsum; 1AI5; -.
DR PDBsum; 1AI6; -.
DR PDBsum; 1AI7; -.
DR PDBsum; 1AJN; -.
DR PDBsum; 1AJP; -.
DR PDBsum; 1AJQ; -.
DR PDBsum; 1E3A; -.
DR PDBsum; 1FXH; -.
DR PDBsum; 1FXV; -.
DR PDBsum; 1GK9; -.
DR PDBsum; 1GKF; -.
DR PDBsum; 1GM7; -.
DR PDBsum; 1GM8; -.
DR PDBsum; 1GM9; -.
DR PDBsum; 1H2G; -.
DR PDBsum; 1JX9; -.
DR PDBsum; 1K5Q; -.
DR PDBsum; 1K5S; -.
DR PDBsum; 1K7D; -.
DR PDBsum; 1KEC; -.
DR PDBsum; 1PNK; -.
DR PDBsum; 1PNL; -.
DR PDBsum; 1PNM; -.
DR AlphaFoldDB; P06875; -.
DR SMR; P06875; -.
DR STRING; 585034.ECIAI1_4561; -.
DR DrugBank; DB01702; 2-(3,4-Dihydroxyphenyl)Acetic Acid.
DR DrugBank; DB08193; 2-(3-NITROPHENYL)ACETIC ACID.
DR DrugBank; DB08327; Homogentisic acid.
DR DrugBank; DB08559; N-[(2S,4S,6R)-2-(dihydroxymethyl)-4-hydroxy-3,3-dimethyl-7-oxo-4lambda~4~-thia-1-azabicyclo[3.2.0]hept-6-yl]-2-phenylacetamide.
DR DrugBank; DB07331; p-Nitrophenylacetic acid.
DR MEROPS; S45.001; -.
DR GeneID; 66671774; -.
DR OMA; NGEMNEH; -.
DR BioCyc; MetaCyc:MON-18775; -.
DR BRENDA; 3.5.1.11; 2026.
DR SABIO-RK; P06875; -.
DR EvolutionaryTrace; P06875; -.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008953; F:penicillin amidase activity; IEA:UniProtKB-EC.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:InterPro.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR CDD; cd03748; Ntn_PGA; 1.
DR Gene3D; 1.10.1400.10; -; 1.
DR Gene3D; 1.10.439.10; -; 1.
DR Gene3D; 2.30.120.10; -; 1.
DR Gene3D; 3.60.20.10; -; 1.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR014395; Pen/GL7ACA/AHL_acylase.
DR InterPro; IPR043147; Penicillin_amidase_A-knob.
DR InterPro; IPR023343; Penicillin_amidase_dom1.
DR InterPro; IPR043146; Penicillin_amidase_N_B-knob.
DR InterPro; IPR033813; PGA_C.
DR InterPro; IPR002692; S45.
DR PANTHER; PTHR34218; PTHR34218; 1.
DR Pfam; PF01804; Penicil_amidase; 1.
DR PIRSF; PIRSF001227; Pen_acylase; 1.
DR SUPFAM; SSF56235; SSF56235; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic resistance; Calcium; Direct protein sequencing;
KW Hydrolase; Metal-binding; Periplasm; Signal; Zymogen.
FT SIGNAL 1..26
FT /evidence="ECO:0000269|PubMed:1849824"
FT CHAIN 27..846
FT /note="Penicillin G acylase"
FT /id="PRO_0000027345"
FT CHAIN 27..235
FT /note="Penicillin G acylase subunit alpha"
FT /id="PRO_0000027346"
FT PROPEP 236..289
FT /note="Spacer peptide"
FT /id="PRO_0000027347"
FT CHAIN 290..846
FT /note="Penicillin G acylase subunit beta"
FT /id="PRO_0000027348"
FT ACT_SITE 290
FT /note="Nucleophile"
FT BINDING 178
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 362
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 364
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 365
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 494
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 541
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT MUTAGEN 290
FT /note="S->C: Loss of activity."
FT /evidence="ECO:0000269|PubMed:7816145"
FT CONFLICT 68
FT /note="Q -> R (in Ref. 5; AAA24258)"
FT /evidence="ECO:0000305"
FT CONFLICT 77
FT /note="Q -> R (in Ref. 5; AAA24258)"
FT /evidence="ECO:0000305"
FT CONFLICT 97
FT /note="R -> S (in Ref. 5; AAA24258)"
FT /evidence="ECO:0000305"
FT CONFLICT 103
FT /note="A -> R (in Ref. 3; AAA24270)"
FT /evidence="ECO:0000305"
FT CONFLICT 130
FT /note="I -> T (in Ref. 2 and 5)"
FT /evidence="ECO:0000305"
FT CONFLICT 217
FT /note="A -> G (in Ref. 5; AAA24258)"
FT /evidence="ECO:0000305"
FT CONFLICT 250
FT /note="R -> P (in Ref. 3; AAA24270)"
FT /evidence="ECO:0000305"
FT CONFLICT 272
FT /note="A -> V (in Ref. 1 and 5)"
FT /evidence="ECO:0000305"
FT CONFLICT 305
FT /note="A -> R (in Ref. 3; AAA24270)"
FT /evidence="ECO:0000305"
FT CONFLICT 342..350
FT /note="PGLVFGHNG -> LGWFPGYMV (in Ref. 5; AAA24258)"
FT /evidence="ECO:0000305"
FT CONFLICT 632
FT /note="G -> P (in Ref. 2; AAA24324)"
FT /evidence="ECO:0000305"
FT CONFLICT 789
FT /note="W -> Q (in Ref. 5; AAA24259)"
FT /evidence="ECO:0000305"
FT STRAND 32..38
FT /evidence="ECO:0007829|PDB:1GK9"
FT STRAND 43..46
FT /evidence="ECO:0007829|PDB:1GK9"
FT HELIX 50..77
FT /evidence="ECO:0007829|PDB:1GK9"
FT HELIX 81..84
FT /evidence="ECO:0007829|PDB:1GK9"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:1GK9"
FT HELIX 89..97
FT /evidence="ECO:0007829|PDB:1GK9"
FT HELIX 101..109
FT /evidence="ECO:0007829|PDB:1GK9"
FT HELIX 113..135
FT /evidence="ECO:0007829|PDB:1GK9"
FT HELIX 137..140
FT /evidence="ECO:0007829|PDB:1GK9"
FT HELIX 143..148
FT /evidence="ECO:0007829|PDB:1GK9"
FT HELIX 157..167
FT /evidence="ECO:0007829|PDB:1GK9"
FT HELIX 169..172
FT /evidence="ECO:0007829|PDB:1GK9"
FT HELIX 178..192
FT /evidence="ECO:0007829|PDB:1GK9"
FT HELIX 194..204
FT /evidence="ECO:0007829|PDB:1GK9"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:1GK9"
FT TURN 218..220
FT /evidence="ECO:0007829|PDB:1GK9"
FT HELIX 229..231
FT /evidence="ECO:0007829|PDB:1E3A"
FT HELIX 232..234
FT /evidence="ECO:0007829|PDB:1GK9"
FT HELIX 235..237
FT /evidence="ECO:0007829|PDB:1E3A"
FT HELIX 246..249
FT /evidence="ECO:0007829|PDB:1E3A"
FT HELIX 264..278
FT /evidence="ECO:0007829|PDB:1E3A"
FT HELIX 279..281
FT /evidence="ECO:0007829|PDB:1E3A"
FT STRAND 291..295
FT /evidence="ECO:0007829|PDB:1GK9"
FT TURN 297..299
FT /evidence="ECO:0007829|PDB:1GK9"
FT STRAND 300..310
FT /evidence="ECO:0007829|PDB:1GK9"
FT STRAND 316..318
FT /evidence="ECO:0007829|PDB:1GK9"
FT STRAND 320..328
FT /evidence="ECO:0007829|PDB:1GK9"
FT STRAND 331..338
FT /evidence="ECO:0007829|PDB:1GK9"
FT STRAND 345..348
FT /evidence="ECO:0007829|PDB:1GK9"
FT STRAND 350..358
FT /evidence="ECO:0007829|PDB:1GK9"
FT STRAND 364..370
FT /evidence="ECO:0007829|PDB:1GK9"
FT STRAND 373..375
FT /evidence="ECO:0007829|PDB:1PNK"
FT STRAND 378..381
FT /evidence="ECO:0007829|PDB:1GK9"
FT STRAND 384..387
FT /evidence="ECO:0007829|PDB:1GK9"
FT STRAND 389..395
FT /evidence="ECO:0007829|PDB:1GK9"
FT STRAND 403..410
FT /evidence="ECO:0007829|PDB:1GK9"
FT STRAND 413..419
FT /evidence="ECO:0007829|PDB:1GK9"
FT TURN 420..423
FT /evidence="ECO:0007829|PDB:1GK9"
FT STRAND 424..430
FT /evidence="ECO:0007829|PDB:1GK9"
FT TURN 431..434
FT /evidence="ECO:0007829|PDB:1GK9"
FT HELIX 436..445
FT /evidence="ECO:0007829|PDB:1GK9"
FT HELIX 446..448
FT /evidence="ECO:0007829|PDB:1GK9"
FT HELIX 452..459
FT /evidence="ECO:0007829|PDB:1GK9"
FT STRAND 464..472
FT /evidence="ECO:0007829|PDB:1GK9"
FT STRAND 477..483
FT /evidence="ECO:0007829|PDB:1GK9"
FT STRAND 498..502
FT /evidence="ECO:0007829|PDB:1GK9"
FT HELIX 512..514
FT /evidence="ECO:0007829|PDB:1GK9"
FT STRAND 517..520
FT /evidence="ECO:0007829|PDB:1GK9"
FT STRAND 524..530
FT /evidence="ECO:0007829|PDB:1GK9"
FT STRAND 532..534
FT /evidence="ECO:0007829|PDB:1GK9"
FT HELIX 553..561
FT /evidence="ECO:0007829|PDB:1GK9"
FT STRAND 562..564
FT /evidence="ECO:0007829|PDB:1GK9"
FT HELIX 568..580
FT /evidence="ECO:0007829|PDB:1GK9"
FT HELIX 585..596
FT /evidence="ECO:0007829|PDB:1GK9"
FT HELIX 604..613
FT /evidence="ECO:0007829|PDB:1GK9"
FT STRAND 625..630
FT /evidence="ECO:0007829|PDB:1GK9"
FT HELIX 632..646
FT /evidence="ECO:0007829|PDB:1GK9"
FT HELIX 648..651
FT /evidence="ECO:0007829|PDB:1GK9"
FT HELIX 656..660
FT /evidence="ECO:0007829|PDB:1GK9"
FT HELIX 680..689
FT /evidence="ECO:0007829|PDB:1GK9"
FT HELIX 690..693
FT /evidence="ECO:0007829|PDB:1GK9"
FT STRAND 694..696
FT /evidence="ECO:0007829|PDB:1E3A"
FT TURN 702..705
FT /evidence="ECO:0007829|PDB:1GK9"
FT HELIX 708..727
FT /evidence="ECO:0007829|PDB:1GK9"
FT HELIX 731..733
FT /evidence="ECO:0007829|PDB:1GK9"
FT STRAND 741..746
FT /evidence="ECO:0007829|PDB:1GK9"
FT STRAND 752..754
FT /evidence="ECO:0007829|PDB:1GK9"
FT HELIX 756..758
FT /evidence="ECO:0007829|PDB:1GK9"
FT STRAND 760..764
FT /evidence="ECO:0007829|PDB:1GK9"
FT STRAND 770..778
FT /evidence="ECO:0007829|PDB:1GK9"
FT STRAND 780..783
FT /evidence="ECO:0007829|PDB:1GM8"
FT STRAND 785..791
FT /evidence="ECO:0007829|PDB:1GK9"
FT STRAND 810..813
FT /evidence="ECO:0007829|PDB:1AI4"
FT HELIX 814..818
FT /evidence="ECO:0007829|PDB:1GK9"
FT STRAND 823..825
FT /evidence="ECO:0007829|PDB:1K7D"
FT HELIX 829..834
FT /evidence="ECO:0007829|PDB:1GK9"
FT STRAND 836..843
FT /evidence="ECO:0007829|PDB:1GK9"
SQ SEQUENCE 846 AA; 94643 MW; 48570EDCB53BA227 CRC64;
MKNRNRMIVN CVTASLMYYW SLPALAEQSS SEIKIVRDEY GMPHIYANDT WHLFYGYGYV
VAQDRLFQME MARRSTQGTV AEVLGKDFVK FDKDIRRNYW PDAIRAQIAA LSPEDMSILQ
GYADGMNAWI DKVNTNPETL LPKQFNTFGF TPKRWEPFDV AMIFVGTMAN RFSDSTSEID
NLALLTALKD KYGVSQGMAV FNQLKWLVNP SAPTTIAVQE SNYPLKFNQQ NSQTAALLPR
YDLPAPMLDR PAKGADGALL ALTAGKNRET IAAQFAQGGA NGLAGYPTTS NMWVIGKSKA
QDAKAIMVNG PQFGWYAPAY TYGIGLHGAG YDVTGNTPFA YPGLVFGHNG VISWGSTAGF
GDDVDIFAER LSAEKPGYYL HNGKWVKMLS REETITVKNG QAETFTVWRT VHGNILQTDQ
TTQTAYAKSR AWDGKEVASL LAWTHQMKAK NWQEWTQQAA KQALTINWYY ADVNGNIGYV
HTGAYPDRQS GHDPRLPVPG TGKWDWKGLL PFEMNPKVYN PQSGYIANWN NSPQKDYPAS
DLFAFLWGGA DRVTEIDRLL EQKPRLTADQ AWDVIRQTSR QDLNLRLFLP TLQAATSGLT
QSDPRRQLVE TLTRWDGINL LNDDGKTWQQ PGSAILNVWL TSMLKRTVVA AVPMPFDKWY
SASGYETTQD GPTGSLNISV GAKILYEAVQ GDKSPIPQAV DLFAGKPQQE VVLAALEDTW
ETLSKRYGNN VSNWKTPAMA LTFRANNFFG VPQAAAEETR HQAEYQNRGT ENDMIVFSPT
TSDRPVLAWD VVAPGQSGFI APDGTVDKHY EDQLKMYENF GRKSLWLTKQ DVEAHKESQE
VLHVQR
