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 02-SEP-2026, entry version 217. 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; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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_CP009789.1. 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 AlphaFoldDB; P04825; -. DR MDposit; P04825; -. DR MDRepo; P04825; -. DR SMR; P04825; -. DR BioGRID; 4261880; 52. DR BioGRID; 851583; 8. DR DIP; DIP-10458N; -. DR FunCoup; P04825; 501. 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; 511145-b0932; -. DR EnsemblBacteria; AAC74018; AAC74018; b0932. DR GeneID; 947253; -. DR KEGG; ecj:JW0915; -. DR KEGG; eco:b0932; -. DR KEGG; ecoc:C3026_05725; -. 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 OrthoDB; 100605at2; -. DR PhylomeDB; P04825; -. DR BioCyc; EcoCyc:EG10696-MONOMER; -. DR BioCyc; MetaCyc:EG10696-MONOMER; -. DR BRENDA; 3.4.11.2; 2026. DR SABIO-RK; P04825; -. DR EvolutionaryTrace; P04825; -. DR PRO; PR:P04825; -. DR Proteomes; UP000000625; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016285; F:alanyl aminopeptidase activity; EXP:UniProtKB. 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:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006508; P:proteolysis; IMP:EcoCyc. DR CDD; cd09600; M1_APN; 1. DR FunFam; 1.10.390.10:FF:000002; Aminopeptidase N; 1. DR FunFam; 1.25.50.10:FF:000001; Aminopeptidase N; 1. DR FunFam; 2.60.40.1730:FF:000005; Aminopeptidase N; 1. DR FunFam; 2.60.40.1840:FF:000001; Aminopeptidase N; 1. DR FunFam; 3.30.2010.30:FF:000002; Putative aminopeptidase N; 1. DR Gene3D; 2.60.40.1840; -; 1. DR Gene3D; 3.30.2010.30; -; 1. DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1. DR Gene3D; 1.25.50.10; Peptidase M1, alanyl aminopeptidase, C-terminal domain; 1. DR Gene3D; 2.60.40.1730; tricorn interacting facor f3 domain; 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 NCBIfam; TIGR02414; pepN_proteo; 1. DR PANTHER; PTHR46322; PUROMYCIN-SENSITIVE AMINOPEPTIDASE; 1. DR PANTHER; PTHR46322:SF1; PUROMYCIN-SENSITIVE AMINOPEPTIDASE; 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; Leukotriene A4 hydrolase N-terminal domain; 1. DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1. DR PROSITE; PS00142; ZINC_PROTEASE; 1. 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; -. 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 5..7 FT /evidence="ECO:0007829|PDB:5MFR" 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..236 FT /evidence="ECO:0007829|PDB:3B34" FT HELIX 237..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..346 FT /evidence="ECO:0007829|PDB:3B34" FT HELIX 347..352 FT /evidence="ECO:0007829|PDB:3B34" FT HELIX 353..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 379..383 FT /evidence="ECO:0007829|PDB:3B34" FT HELIX 384..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 HELIX 435..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 HELIX 469..471 FT /evidence="ECO:0007829|PDB:5YO1" FT STRAND 483..490 FT /evidence="ECO:0007829|PDB:3B34" FT HELIX 497..499 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 587..589 FT /evidence="ECO:0007829|PDB:5YQB" 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 619..621 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..782 FT /evidence="ECO:0007829|PDB:3B34" FT HELIX 783..787 FT /evidence="ECO:0007829|PDB:3B34" FT HELIX 788..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 833..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 //