AMPN_ECOLI
ID AMPN_ECOLI Reviewed; 870 AA.
AC P04825;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 204.
DE RecName: Full=Aminopeptidase N;
DE EC=3.4.11.2 {ECO:0000269|PubMed:16885166, ECO:0000269|PubMed:18416562, ECO:0000269|PubMed:19622865};
DE AltName: Full=Alpha-aminoacylpeptide hydrolase;
GN Name=pepN; OrderedLocusNames=b0932, JW0915;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2436977; DOI=10.1016/0378-1119(86)90366-5;
RA Foglino M., Gharbi S., Lazdunski A.;
RT "Nucleotide sequence of the pepN gene encoding aminopeptidase N of
RT Escherichia coli.";
RL Gene 49:303-309(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=3549459; DOI=10.1016/0378-1119(86)90360-4;
RA McCaman M.T., Gabe J.D.;
RT "The nucleotide sequence of the pepN gene and its over-expression in
RT Escherichia coli.";
RL Gene 48:145-153(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-242.
RC STRAIN=K12;
RX PubMed=3018440; DOI=10.1007/bf00330202;
RA McCaman M.T., Gabe J.D.;
RT "Sequence of the promoter and 5' coding region of pepN, and the amino-
RT terminus of peptidase N from Escherichia coli K-12.";
RL Mol. Gen. Genet. 204:148-152(1986).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-177, AND PROTEIN SEQUENCE OF 2-22.
RX PubMed=2869947; DOI=10.1111/j.1432-1033.1986.tb09525.x;
RA Bally M., Foglino M., Bruschi M., Murgier M., Lazdunski A.;
RT "Nucleotide sequence of the promoter and amino-terminal encoding region of
RT the Escherichia coli pepN gene.";
RL Eur. J. Biochem. 155:565-569(1986).
RN [8]
RP FUNCTION IN PEPTIDE DEGRADATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / JM101 / ATCC 33876 / DSM 3948 / NCIMB 11926;
RX PubMed=20067529; DOI=10.1111/j.1574-6968.2009.01879.x;
RA Hayashi M., Tabata K., Yagasaki M., Yonetani Y.;
RT "Effect of multidrug-efflux transporter genes on dipeptide resistance and
RT overproduction in Escherichia coli.";
RL FEMS Microbiol. Lett. 304:12-19(2010).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH ZINC IONS AND
RP BESTATIN, FUNCTION, ACTIVE SITE, COFACTOR, AND CATALYTIC ACTIVITY.
RX PubMed=16885166; DOI=10.1074/jbc.m605203200;
RA Ito K., Nakajima Y., Onohara Y., Takeo M., Nakashima K., Matsubara F.,
RA Ito T., Yoshimoto T.;
RT "Crystal structure of aminopeptidase N (proteobacteria alanyl
RT aminopeptidase) from Escherichia coli and conformational change of
RT methionine 260 involved in substrate recognition.";
RL J. Biol. Chem. 281:33664-33676(2006).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) IN COMPLEXES WITH ZINC IONS AND
RP SUBSTRATE ANALOGS, FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, AND COFACTOR.
RX PubMed=18416562; DOI=10.1021/bi7022333;
RA Addlagatta A., Gay L., Matthews B.W.;
RT "Structural basis for the unusual specificity of Escherichia coli
RT aminopeptidase N.";
RL Biochemistry 47:5303-5311(2008).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) IN COMPLEX WITH ZINC IONS AND
RP TRANSITION-STATE ANALOG PL250, FUNCTION, ACTIVE SITE, COFACTOR, AND
RP CATALYTIC ACTIVITY.
RX PubMed=19622865; DOI=10.1107/s090744490901779x;
RA Fournie-Zaluski M.C., Poras H., Roques B.P., Nakajima Y., Ito K.,
RA Yoshimoto T.;
RT "Structure of aminopeptidase N from Escherichia coli complexed with the
RT transition-state analogue aminophosphinic inhibitor PL250.";
RL Acta Crystallogr. D 65:814-822(2009).
CC -!- FUNCTION: Aminopeptidase N is involved in the degradation of
CC intracellular peptides generated by protein breakdown during normal
CC growth as well as in response to nutrient starvation.
CC {ECO:0000269|PubMed:16885166, ECO:0000269|PubMed:18416562,
CC ECO:0000269|PubMed:19622865, ECO:0000305|PubMed:20067529}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal amino acid, Xaa-|-Yaa- from a
CC peptide, amide or arylamide. Xaa is preferably Ala, but may be most
CC amino acids including Pro (slow action). When a terminal hydrophobic
CC residue is followed by a prolyl residue, the two may be released as
CC an intact Xaa-Pro dipeptide.; EC=3.4.11.2;
CC Evidence={ECO:0000269|PubMed:16885166, ECO:0000269|PubMed:18416562,
CC ECO:0000269|PubMed:19622865};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:16885166, ECO:0000269|PubMed:18416562,
CC ECO:0000269|PubMed:19622865};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:16885166,
CC ECO:0000269|PubMed:18416562, ECO:0000269|PubMed:19622865};
CC -!- INTERACTION:
CC P04825; P19318: narY; NbExp=3; IntAct=EBI-545385, EBI-555059;
CC P04825; P04825: pepN; NbExp=2; IntAct=EBI-545385, EBI-545385;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein;
CC Cytoplasmic side.
CC -!- DISRUPTION PHENOTYPE: A quadruple peptidase disruption (pepA, pepB,
CC pepD and pepN) does not grow in M9 minimal medium, does grow better
CC when supplemented with casamino acids (PubMed:20067529).
CC {ECO:0000269|PubMed:20067529}.
CC -!- SIMILARITY: Belongs to the peptidase M1 family. {ECO:0000305}.
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DR EMBL; X04020; CAA27647.1; -; Genomic_DNA.
DR EMBL; X03709; CAA27336.1; -; Genomic_DNA.
DR EMBL; M15676; AAA24318.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74018.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35684.1; -; Genomic_DNA.
DR EMBL; M15273; AAA24317.1; -; Genomic_DNA.
DR PIR; C64833; DPECN.
DR RefSeq; NP_415452.1; NC_000913.3.
DR RefSeq; WP_000193841.1; NZ_SSZK01000002.1.
DR PDB; 2DQ6; X-ray; 1.50 A; A=1-870.
DR PDB; 2DQM; X-ray; 1.60 A; A=1-870.
DR PDB; 2HPO; X-ray; 1.65 A; A=1-870.
DR PDB; 2HPT; X-ray; 2.30 A; A=1-870.
DR PDB; 2ZXG; X-ray; 1.55 A; A=1-870.
DR PDB; 3B2P; X-ray; 2.00 A; A=1-870.
DR PDB; 3B2X; X-ray; 1.50 A; A=1-870.
DR PDB; 3B34; X-ray; 1.30 A; A=1-870.
DR PDB; 3B37; X-ray; 1.70 A; A=1-870.
DR PDB; 3B3B; X-ray; 1.85 A; A=1-870.
DR PDB; 3KED; X-ray; 2.30 A; A=1-870.
DR PDB; 3PUU; X-ray; 2.15 A; A=1-870.
DR PDB; 3QJX; X-ray; 1.45 A; A=1-870.
DR PDB; 4Q4E; X-ray; 1.90 A; A=1-870.
DR PDB; 4Q4I; X-ray; 2.31 A; A=1-870.
DR PDB; 4XMT; X-ray; 2.00 A; A=4-870.
DR PDB; 4XMU; X-ray; 2.91 A; A=5-870.
DR PDB; 4XMV; X-ray; 2.92 A; A=5-870.
DR PDB; 4XMW; X-ray; 2.20 A; A=4-870.
DR PDB; 4XMX; X-ray; 2.30 A; A=5-870.
DR PDB; 4XMZ; X-ray; 2.15 A; A=4-870.
DR PDB; 4XN1; X-ray; 2.20 A; A=4-870.
DR PDB; 4XN2; X-ray; 2.11 A; A=5-870.
DR PDB; 4XN4; X-ray; 1.99 A; A=5-870.
DR PDB; 4XN5; X-ray; 2.66 A; A=5-870.
DR PDB; 4XN7; X-ray; 2.22 A; A=5-870.
DR PDB; 4XN8; X-ray; 1.89 A; A=5-870.
DR PDB; 4XN9; X-ray; 2.80 A; A=5-870.
DR PDB; 4XNA; X-ray; 2.40 A; A=5-870.
DR PDB; 4XNB; X-ray; 1.95 A; A=5-870.
DR PDB; 4XND; X-ray; 1.93 A; A=5-870.
DR PDB; 4XO3; X-ray; 2.00 A; A=5-870.
DR PDB; 4XO4; X-ray; 2.18 A; A=1-870.
DR PDB; 4XO5; X-ray; 1.98 A; A=5-870.
DR PDB; 5MFR; X-ray; 1.40 A; A=1-870.
DR PDB; 5MFS; X-ray; 1.57 A; A=1-870.
DR PDB; 5MFT; X-ray; 1.59 A; A=1-870.
DR PDB; 5YO1; X-ray; 2.50 A; A=1-870.
DR PDB; 5YQ1; X-ray; 1.58 A; A=1-870.
DR PDB; 5YQ2; X-ray; 1.60 A; A=1-870.
DR PDB; 5YQB; X-ray; 1.56 A; A=1-870.
DR PDB; 6G8B; X-ray; 2.37 A; A=1-870.
DR PDBsum; 2DQ6; -.
DR PDBsum; 2DQM; -.
DR PDBsum; 2HPO; -.
DR PDBsum; 2HPT; -.
DR PDBsum; 2ZXG; -.
DR PDBsum; 3B2P; -.
DR PDBsum; 3B2X; -.
DR PDBsum; 3B34; -.
DR PDBsum; 3B37; -.
DR PDBsum; 3B3B; -.
DR PDBsum; 3KED; -.
DR PDBsum; 3PUU; -.
DR PDBsum; 3QJX; -.
DR PDBsum; 4Q4E; -.
DR PDBsum; 4Q4I; -.
DR PDBsum; 4XMT; -.
DR PDBsum; 4XMU; -.
DR PDBsum; 4XMV; -.
DR PDBsum; 4XMW; -.
DR PDBsum; 4XMX; -.
DR PDBsum; 4XMZ; -.
DR PDBsum; 4XN1; -.
DR PDBsum; 4XN2; -.
DR PDBsum; 4XN4; -.
DR PDBsum; 4XN5; -.
DR PDBsum; 4XN7; -.
DR PDBsum; 4XN8; -.
DR PDBsum; 4XN9; -.
DR PDBsum; 4XNA; -.
DR PDBsum; 4XNB; -.
DR PDBsum; 4XND; -.
DR PDBsum; 4XO3; -.
DR PDBsum; 4XO4; -.
DR PDBsum; 4XO5; -.
DR PDBsum; 5MFR; -.
DR PDBsum; 5MFS; -.
DR PDBsum; 5MFT; -.
DR PDBsum; 5YO1; -.
DR PDBsum; 5YQ1; -.
DR PDBsum; 5YQ2; -.
DR PDBsum; 5YQB; -.
DR PDBsum; 6G8B; -.
DR AlphaFoldDB; P04825; -.
DR SMR; P04825; -.
DR BioGRID; 4261880; 49.
DR BioGRID; 851583; 8.
DR DIP; DIP-10458N; -.
DR IntAct; P04825; 13.
DR STRING; 511145.b0932; -.
DR BindingDB; P04825; -.
DR ChEMBL; CHEMBL4325; -.
DR DrugBank; DB08506; N-{(2S)-3-[(1R)-1-aminoethyl](hydroxy)phosphoryl-2-benzylpropanoyl}-L-phenylalanine.
DR MEROPS; M01.005; -.
DR jPOST; P04825; -.
DR PaxDb; P04825; -.
DR PRIDE; P04825; -.
DR EnsemblBacteria; AAC74018; AAC74018; b0932.
DR EnsemblBacteria; BAA35684; BAA35684; BAA35684.
DR GeneID; 947253; -.
DR KEGG; ecj:JW0915; -.
DR KEGG; eco:b0932; -.
DR PATRIC; fig|1411691.4.peg.1342; -.
DR EchoBASE; EB0690; -.
DR eggNOG; COG0308; Bacteria.
DR HOGENOM; CLU_007993_2_0_6; -.
DR InParanoid; P04825; -.
DR OMA; FKRWYSQ; -.
DR PhylomeDB; P04825; -.
DR BioCyc; EcoCyc:EG10696-MON; -.
DR BioCyc; MetaCyc:EG10696-MON; -.
DR BRENDA; 3.4.11.2; 2026.
DR SABIO-RK; P04825; -.
DR EvolutionaryTrace; P04825; -.
DR PRO; PR:P04825; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004177; F:aminopeptidase activity; IDA:EcoliWiki.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IMP:EcoCyc.
DR Gene3D; 1.10.390.10; -; 1.
DR Gene3D; 1.25.50.10; -; 1.
DR Gene3D; 2.60.40.1730; -; 1.
DR Gene3D; 2.60.40.1840; -; 1.
DR InterPro; IPR045357; Aminopeptidase_N-like_N.
DR InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR InterPro; IPR038438; PepN_Ig-like_sf.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR012779; Peptidase_M1_pepN.
DR InterPro; IPR024601; Peptidase_M1_pepN_C.
DR InterPro; IPR037144; Peptidase_M1_pepN_C_sf.
DR InterPro; IPR035414; Peptidase_M1_pepN_Ig-like.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR PANTHER; PTHR46322; PTHR46322; 1.
DR Pfam; PF11940; DUF3458; 1.
DR Pfam; PF17432; DUF3458_C; 1.
DR Pfam; PF01433; Peptidase_M1; 1.
DR Pfam; PF17900; Peptidase_M1_N; 1.
DR PRINTS; PR00756; ALADIPTASE.
DR SUPFAM; SSF63737; SSF63737; 1.
DR TIGRFAMs; TIGR02414; pepN_proteo; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminopeptidase; Cell inner membrane; Cell membrane;
KW Direct protein sequencing; Hydrolase; Membrane; Metal-binding;
KW Metalloprotease; Protease; Reference proteome; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2869947"
FT CHAIN 2..870
FT /note="Aminopeptidase N"
FT /id="PRO_0000095069"
FT ACT_SITE 298
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:16885166,
FT ECO:0000305|PubMed:18416562, ECO:0000305|PubMed:19622865"
FT BINDING 121
FT /ligand="substrate"
FT BINDING 261..265
FT /ligand="substrate"
FT BINDING 297
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT BINDING 301
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT BINDING 320
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT SITE 381
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000305"
FT CONFLICT 76
FT /note="E -> D (in Ref. 7; CAA27647)"
FT /evidence="ECO:0000305"
FT HELIX 10..12
FT /evidence="ECO:0007829|PDB:3B34"
FT STRAND 17..28
FT /evidence="ECO:0007829|PDB:3B34"
FT STRAND 34..44
FT /evidence="ECO:0007829|PDB:3B34"
FT STRAND 52..55
FT /evidence="ECO:0007829|PDB:3B34"
FT STRAND 60..66
FT /evidence="ECO:0007829|PDB:3B34"
FT STRAND 73..77
FT /evidence="ECO:0007829|PDB:3B34"
FT STRAND 80..83
FT /evidence="ECO:0007829|PDB:3B34"
FT STRAND 88..98
FT /evidence="ECO:0007829|PDB:3B34"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:3B34"
FT STRAND 108..112
FT /evidence="ECO:0007829|PDB:3B34"
FT STRAND 115..119
FT /evidence="ECO:0007829|PDB:3B34"
FT TURN 121..124
FT /evidence="ECO:0007829|PDB:3B34"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:3B34"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:3B34"
FT STRAND 139..148
FT /evidence="ECO:0007829|PDB:3B34"
FT TURN 149..151
FT /evidence="ECO:0007829|PDB:3B34"
FT STRAND 154..166
FT /evidence="ECO:0007829|PDB:3B34"
FT HELIX 168..170
FT /evidence="ECO:0007829|PDB:5MFR"
FT STRAND 171..182
FT /evidence="ECO:0007829|PDB:3B34"
FT HELIX 184..186
FT /evidence="ECO:0007829|PDB:3B34"
FT STRAND 189..192
FT /evidence="ECO:0007829|PDB:3B34"
FT STRAND 195..202
FT /evidence="ECO:0007829|PDB:3B34"
FT STRAND 208..215
FT /evidence="ECO:0007829|PDB:3B34"
FT HELIX 220..222
FT /evidence="ECO:0007829|PDB:3B34"
FT HELIX 224..241
FT /evidence="ECO:0007829|PDB:3B34"
FT STRAND 247..256
FT /evidence="ECO:0007829|PDB:3B34"
FT STRAND 259..263
FT /evidence="ECO:0007829|PDB:3B34"
FT STRAND 268..272
FT /evidence="ECO:0007829|PDB:3B34"
FT HELIX 273..275
FT /evidence="ECO:0007829|PDB:3B34"
FT TURN 280..282
FT /evidence="ECO:0007829|PDB:3B34"
FT HELIX 285..300
FT /evidence="ECO:0007829|PDB:3B34"
FT TURN 301..303
FT /evidence="ECO:0007829|PDB:3B34"
FT TURN 305..307
FT /evidence="ECO:0007829|PDB:3B34"
FT STRAND 308..312
FT /evidence="ECO:0007829|PDB:3B34"
FT HELIX 313..315
FT /evidence="ECO:0007829|PDB:3B34"
FT HELIX 316..334
FT /evidence="ECO:0007829|PDB:3B34"
FT HELIX 337..350
FT /evidence="ECO:0007829|PDB:3B34"
FT HELIX 352..356
FT /evidence="ECO:0007829|PDB:3B34"
FT STRAND 367..370
FT /evidence="ECO:0007829|PDB:3B34"
FT HELIX 372..375
FT /evidence="ECO:0007829|PDB:3B34"
FT HELIX 378..411
FT /evidence="ECO:0007829|PDB:3B34"
FT STRAND 414..416
FT /evidence="ECO:0007829|PDB:3B34"
FT HELIX 418..429
FT /evidence="ECO:0007829|PDB:3B34"
FT TURN 434..437
FT /evidence="ECO:0007829|PDB:3B34"
FT HELIX 438..441
FT /evidence="ECO:0007829|PDB:3B34"
FT STRAND 447..455
FT /evidence="ECO:0007829|PDB:3B34"
FT TURN 456..459
FT /evidence="ECO:0007829|PDB:3B34"
FT STRAND 460..468
FT /evidence="ECO:0007829|PDB:3B34"
FT STRAND 483..490
FT /evidence="ECO:0007829|PDB:3B34"
FT STRAND 500..505
FT /evidence="ECO:0007829|PDB:4XMU"
FT STRAND 508..512
FT /evidence="ECO:0007829|PDB:3B34"
FT STRAND 514..521
FT /evidence="ECO:0007829|PDB:3B34"
FT STRAND 529..533
FT /evidence="ECO:0007829|PDB:3B34"
FT HELIX 534..536
FT /evidence="ECO:0007829|PDB:2DQ6"
FT STRAND 541..543
FT /evidence="ECO:0007829|PDB:3B34"
FT HELIX 548..557
FT /evidence="ECO:0007829|PDB:3B34"
FT HELIX 561..584
FT /evidence="ECO:0007829|PDB:3B34"
FT HELIX 593..604
FT /evidence="ECO:0007829|PDB:3B34"
FT STRAND 606..608
FT /evidence="ECO:0007829|PDB:3B34"
FT HELIX 610..616
FT /evidence="ECO:0007829|PDB:3B34"
FT HELIX 622..626
FT /evidence="ECO:0007829|PDB:3B34"
FT HELIX 634..651
FT /evidence="ECO:0007829|PDB:3B34"
FT HELIX 653..662
FT /evidence="ECO:0007829|PDB:3B34"
FT HELIX 672..689
FT /evidence="ECO:0007829|PDB:3B34"
FT HELIX 693..706
FT /evidence="ECO:0007829|PDB:3B34"
FT HELIX 710..722
FT /evidence="ECO:0007829|PDB:3B34"
FT HELIX 728..739
FT /evidence="ECO:0007829|PDB:3B34"
FT HELIX 743..754
FT /evidence="ECO:0007829|PDB:3B34"
FT HELIX 761..768
FT /evidence="ECO:0007829|PDB:3B34"
FT HELIX 779..792
FT /evidence="ECO:0007829|PDB:3B34"
FT HELIX 794..797
FT /evidence="ECO:0007829|PDB:3B34"
FT HELIX 803..818
FT /evidence="ECO:0007829|PDB:3B34"
FT HELIX 820..831
FT /evidence="ECO:0007829|PDB:3B34"
FT HELIX 832..835
FT /evidence="ECO:0007829|PDB:3B34"
FT HELIX 838..852
FT /evidence="ECO:0007829|PDB:3B34"
FT HELIX 859..869
FT /evidence="ECO:0007829|PDB:3B34"
SQ SEQUENCE 870 AA; 98919 MW; 7C18C6BD8F2E5131 CRC64;
MTQQPQAKYR HDYRAPDYQI TDIDLTFDLD AQKTVVTAVS QAVRHGASDA PLRLNGEDLK
LVSVHINDEP WTAWKEEEGA LVISNLPERF TLKIINEISP AANTALEGLY QSGDALCTQC
EAEGFRHITY YLDRPDVLAR FTTKIIADKI KYPFLLSNGN RVAQGELENG RHWVQWQDPF
PKPCYLFALV AGDFDVLRDT FTTRSGREVA LELYVDRGNL DRAPWAMTSL KNSMKWDEER
FGLEYDLDIY MIVAVDFFNM GAMENKGLNI FNSKYVLART DTATDKDYLD IERVIGHEYF
HNWTGNRVTC RDWFQLSLKE GLTVFRDQEF SSDLGSRAVN RINNVRTMRG LQFAEDASPM
AHPIRPDMVI EMNNFYTLTV YEKGAEVIRM IHTLLGEENF QKGMQLYFER HDGSAATCDD
FVQAMEDASN VDLSHFRRWY SQSGTPIVTV KDDYNPETEQ YTLTISQRTP ATPDQAEKQP
LHIPFAIELY DNEGKVIPLQ KGGHPVNSVL NVTQAEQTFV FDNVYFQPVP ALLCEFSAPV
KLEYKWSDQQ LTFLMRHARN DFSRWDAAQS LLATYIKLNV ARHQQGQPLS LPVHVADAFR
AVLLDEKIDP ALAAEILTLP SVNEMAELFD IIDPIAIAEV REALTRTLAT ELADELLAIY
NANYQSEYRV EHEDIAKRTL RNACLRFLAF GETHLADVLV SKQFHEANNM TDALAALSAA
VAAQLPCRDA LMQEYDDKWH QNGLVMDKWF ILQATSPAAN VLETVRGLLQ HRSFTMSNPN
RIRSLIGAFA GSNPAAFHAE DGSGYLFLVE MLTDLNSRNP QVASRLIEPL IRLKRYDAKR
QEKMRAALEQ LKGLENLSGD LYEKITKALA
