LNT_ECOLI
ID LNT_ECOLI Reviewed; 512 AA.
AC P23930; P77703;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Apolipoprotein N-acyltransferase {ECO:0000255|HAMAP-Rule:MF_01148, ECO:0000303|PubMed:2032623};
DE Short=ALP N-acyltransferase {ECO:0000255|HAMAP-Rule:MF_01148, ECO:0000303|PubMed:2032623};
DE EC=2.3.1.269 {ECO:0000255|HAMAP-Rule:MF_01148, ECO:0000269|PubMed:21676878, ECO:0000269|PubMed:28675161, ECO:0000269|PubMed:28885614};
DE AltName: Full=Copper homeostasis protein CutE;
GN Name=lnt {ECO:0000255|HAMAP-Rule:MF_01148, ECO:0000303|PubMed:15513925};
GN Synonyms=cutE {ECO:0000303|PubMed:1938881};
GN OrderedLocusNames=b0657, JW0654;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DISRUPTION PHENOTYPE.
RC STRAIN=K12;
RX PubMed=1938881; DOI=10.1128/jb.173.21.6742-6748.1991;
RA Rogers S.D., Bhave M.R., Mercer J.F.B., Camakaris J., Lee B.T.O.;
RT "Cloning and characterization of cutE, a gene involved in copper transport
RT in Escherichia coli.";
RL J. Bacteriol. 173:6742-6748(1991).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
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], AND SEQUENCE REVISION TO
RP 186.
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 FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=2032623; DOI=10.1016/0378-1097(91)90251-5;
RA Gupta S.D., Wu H.C.;
RT "Identification and subcellular localization of apolipoprotein N-
RT acyltransferase in Escherichia coli.";
RL FEMS Microbiol. Lett. 62:37-41(1991).
RN [7]
RP PROBABLE FUNCTION.
RX PubMed=8344936; DOI=10.1016/s0021-9258(19)85454-6;
RA Gupta S.D., Gan K., Schmid M.B., Wu H.C.;
RT "Characterization of a temperature-sensitive mutant of Salmonella
RT typhimurium defective in apolipoprotein N-acyltransferase.";
RL J. Biol. Chem. 268:16551-16556(1993).
RN [8]
RP SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=15513925; DOI=10.1074/jbc.m411059200;
RA Robichon C., Vidal-Ingigliardi D., Pugsley A.P.;
RT "Depletion of apolipoprotein N-acyltransferase causes mislocalization of
RT outer membrane lipoproteins in Escherichia coli.";
RL J. Biol. Chem. 280:974-983(2005).
RN [9]
RP SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [10]
RP MUTAGENESIS OF TRP-148; TRP-237; GLU-267; LYS-335; GLU-343; CYS-387;
RP TYR-388 AND GLU-389.
RX PubMed=17416655; DOI=10.1128/jb.00099-07;
RA Vidal-Ingigliardi D., Lewenza S., Buddelmeijer N.;
RT "Identification of essential residues in apolipoprotein N-acyl transferase,
RT a member of the CN hydrolase family.";
RL J. Bacteriol. 189:4456-4464(2007).
RN [11]
RP FUNCTION, CATALYTIC ACTIVITY, AND REACTION MECHANISM.
RX PubMed=21676878; DOI=10.1074/jbc.m111.243519;
RA Hillmann F., Argentini M., Buddelmeijer N.;
RT "Kinetics and phospholipid specificity of apolipoprotein N-
RT acyltransferase.";
RL J. Biol. Chem. 286:27936-27946(2011).
RN [12] {ECO:0007744|PDB:5XHQ}
RP X-RAY CRYSTALLOGRAPHY (2.59 ANGSTROMS) OF 1-508, FUNCTION, CATALYTIC
RP ACTIVITY, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY, AND MUTAGENESIS OF
RP SER-78; GLY-145; GLU-267; LYS-335; VAL-339; GLY-342; GLU-343; ARG-352;
RP CYS-387; TYR-388; GLU-389 AND PHE-416.
RC STRAIN=K12;
RX PubMed=28885614; DOI=10.1038/ncomms15948;
RA Lu G., Xu Y., Zhang K., Xiong Y., Li H., Cui L., Wang X., Lou J., Zhai Y.,
RA Sun F., Zhang X.C.;
RT "Crystal structure of E. coli apolipoprotein N-acyl transferase.";
RL Nat. Commun. 8:15948-15948(2017).
RN [13] {ECO:0007744|PDB:5N6H, ECO:0007744|PDB:5N6L}
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF WILD-TYPE AND MUTANT ALA-387,
RP FUNCTION, CATALYTIC ACTIVITY, REACTION MECHANISM, SUBCELLULAR LOCATION,
RP TOPOLOGY, ACTIVE SITE, AND MUTAGENESIS OF GLU-267; LYS-335 AND CYS-387.
RX PubMed=28675161; DOI=10.1038/ncomms15952;
RA Wiktor M., Weichert D., Howe N., Huang C.Y., Olieric V., Boland C.,
RA Bailey J., Vogeley L., Stansfeld P.J., Buddelmeijer N., Wang M.,
RA Caffrey M.;
RT "Structural insights into the mechanism of the membrane integral N-
RT acyltransferase step in bacterial lipoprotein synthesis.";
RL Nat. Commun. 8:15952-15952(2017).
CC -!- FUNCTION: Catalyzes the phospholipid dependent N-acylation of the N-
CC terminal cysteine of apolipoprotein, the last step in lipoprotein
CC maturation (PubMed:2032623, PubMed:21676878, PubMed:28885614,
CC PubMed:28675161). Utilizes a two-step reaction via a ping-pong
CC mechanism (PubMed:21676878, PubMed:28675161). Lnt undergoes covalent
CC modification in the presence of phospholipids, resulting in a thioester
CC acyl-enzyme intermediate. It then transfers the acyl chain to the amine
CC group of the N-terminal diacylglyceryl-modified cysteine of
CC apolipoprotein, leading to the formation of mature triacylated
CC lipoprotein (PubMed:21676878, PubMed:28675161). In vitro, can utilize
CC the phospholipids phosphatidylethanolamine (PE), phosphatidylglycerol
CC (PG), phosphatidic acid (PA) or cardiolipin (CL) (PubMed:2032623,
CC PubMed:21676878). PE is the most efficient acyl donor
CC (PubMed:21676878). {ECO:0000269|PubMed:2032623,
CC ECO:0000269|PubMed:21676878, ECO:0000269|PubMed:28675161,
CC ECO:0000269|PubMed:28885614, ECO:0000305|PubMed:8344936}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a glycerophospholipid + N-terminal S-1,2-diacyl-sn-glyceryl-L-
CC cysteinyl-[lipoprotein] = a 2-acyl-sn-glycero-3-phospholipid + H(+) +
CC N-acyl-S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipoprotein];
CC Xref=Rhea:RHEA:48228, Rhea:RHEA-COMP:14681, Rhea:RHEA-COMP:14684,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:136912, ChEBI:CHEBI:140656,
CC ChEBI:CHEBI:140657, ChEBI:CHEBI:140660; EC=2.3.1.269;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01148,
CC ECO:0000269|PubMed:21676878, ECO:0000269|PubMed:28675161,
CC ECO:0000269|PubMed:28885614};
CC -!- PATHWAY: Protein modification; lipoprotein biosynthesis (N-acyl
CC transfer). {ECO:0000255|HAMAP-Rule:MF_01148}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:28885614}.
CC -!- INTERACTION:
CC P23930; P21599: pykA; NbExp=3; IntAct=EBI-556569, EBI-368956;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01148, ECO:0000269|PubMed:15513925,
CC ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:2032623,
CC ECO:0000269|PubMed:28675161, ECO:0000269|PubMed:28885614}; Multi-pass
CC membrane protein {ECO:0000255|HAMAP-Rule:MF_01148,
CC ECO:0000269|PubMed:15513925, ECO:0000269|PubMed:28675161,
CC ECO:0000269|PubMed:28885614}.
CC -!- DISRUPTION PHENOTYPE: Essential. Depletion induces juxtapositioning of
CC inner and outer membranes and alters the architecture of the cell
CC envelope. It causes mislocalization of outer membrane lipoproteins
CC (PubMed:15513925). The mutant has a copper-sensitive, temperature
CC sensitive phenotype (PubMed:1938881). {ECO:0000269|PubMed:15513925,
CC ECO:0000269|PubMed:1938881}.
CC -!- SIMILARITY: Belongs to the CN hydrolase family. Apolipoprotein N-
CC acyltransferase subfamily. {ECO:0000255|HAMAP-Rule:MF_01148,
CC ECO:0000305}.
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DR EMBL; X58070; CAA41100.1; -; Genomic_DNA.
DR EMBL; U82598; AAB40859.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73758.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35308.2; -; Genomic_DNA.
DR PIR; S18194; S18194.
DR RefSeq; NP_415190.1; NC_000913.3.
DR RefSeq; WP_000853021.1; NZ_SSZK01000037.1.
DR PDB; 5N6H; X-ray; 2.90 A; A/B=1-512.
DR PDB; 5N6L; X-ray; 2.90 A; A/B=1-512.
DR PDB; 5XHQ; X-ray; 2.59 A; A/B=1-508.
DR PDB; 6NWR; X-ray; 3.50 A; A/B=1-512.
DR PDB; 6Q3A; X-ray; 3.10 A; A=1-512.
DR PDB; 7ACI; X-ray; 2.30 A; A=1-512.
DR PDBsum; 5N6H; -.
DR PDBsum; 5N6L; -.
DR PDBsum; 5XHQ; -.
DR PDBsum; 6NWR; -.
DR PDBsum; 6Q3A; -.
DR PDBsum; 7ACI; -.
DR AlphaFoldDB; P23930; -.
DR SMR; P23930; -.
DR BioGRID; 4259916; 206.
DR BioGRID; 850561; 1.
DR DIP; DIP-10111N; -.
DR IntAct; P23930; 2.
DR STRING; 511145.b0657; -.
DR jPOST; P23930; -.
DR PaxDb; P23930; -.
DR PRIDE; P23930; -.
DR EnsemblBacteria; AAC73758; AAC73758; b0657.
DR EnsemblBacteria; BAA35308; BAA35308; BAA35308.
DR GeneID; 946201; -.
DR KEGG; ecj:JW0654; -.
DR KEGG; eco:b0657; -.
DR PATRIC; fig|1411691.4.peg.1611; -.
DR EchoBASE; EB0166; -.
DR eggNOG; COG0815; Bacteria.
DR HOGENOM; CLU_019563_3_0_6; -.
DR InParanoid; P23930; -.
DR OMA; IPQSMKW; -.
DR PhylomeDB; P23930; -.
DR BioCyc; EcoCyc:EG10168-MON; -.
DR BioCyc; MetaCyc:EG10168-MON; -.
DR BRENDA; 2.3.1.269; 2026.
DR UniPathway; UPA00666; -.
DR PRO; PR:P23930; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0016410; F:N-acyltransferase activity; IDA:EcoCyc.
DR GO; GO:0042158; P:lipoprotein biosynthetic process; IDA:EcoCyc.
DR CDD; cd07571; ALP_N-acyl_transferase; 1.
DR Gene3D; 3.60.110.10; -; 1.
DR HAMAP; MF_01148; Lnt; 1.
DR InterPro; IPR004563; Apolipo_AcylTrfase.
DR InterPro; IPR003010; C-N_Hydrolase.
DR InterPro; IPR036526; C-N_Hydrolase_sf.
DR InterPro; IPR045378; LNT_N.
DR Pfam; PF00795; CN_hydrolase; 1.
DR Pfam; PF20154; LNT_N; 1.
DR SUPFAM; SSF56317; SSF56317; 1.
DR TIGRFAMs; TIGR00546; lnt; 1.
DR PROSITE; PS50263; CN_HYDROLASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Cell inner membrane; Cell membrane;
KW Membrane; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..512
FT /note="Apolipoprotein N-acyltransferase"
FT /id="PRO_0000178062"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:28675161,
FT ECO:0000269|PubMed:28885614"
FT TRANSMEM 10..27
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:28675161"
FT TOPO_DOM 28..33
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:28675161,
FT ECO:0000269|PubMed:28885614"
FT TRANSMEM 34..48
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:28675161"
FT TOPO_DOM 49..52
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:28675161,
FT ECO:0000269|PubMed:28885614"
FT TRANSMEM 53..68
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:28675161"
FT TOPO_DOM 69..86
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:28675161,
FT ECO:0000269|PubMed:28885614"
FT TRANSMEM 87..116
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:28675161"
FT TOPO_DOM 117..120
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:28675161,
FT ECO:0000269|PubMed:28885614"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:28675161"
FT TOPO_DOM 142..168
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:28675161,
FT ECO:0000269|PubMed:28885614"
FT TRANSMEM 169..189
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:28675161"
FT TOPO_DOM 190..191
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:28675161,
FT ECO:0000269|PubMed:28885614"
FT TRANSMEM 192..210
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:28675161"
FT TOPO_DOM 211..487
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:28675161,
FT ECO:0000269|PubMed:28885614"
FT TRANSMEM 488..508
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:28675161"
FT TOPO_DOM 509..512
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:28675161,
FT ECO:0000269|PubMed:28885614"
FT DOMAIN 227..476
FT /note="CN hydrolase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT ACT_SITE 267
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148,
FT ECO:0000305|PubMed:28675161"
FT ACT_SITE 335
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148,
FT ECO:0000305|PubMed:28675161"
FT ACT_SITE 387
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148,
FT ECO:0000305|PubMed:28675161"
FT MUTAGEN 78
FT /note="S->W: Loss of activity."
FT /evidence="ECO:0000269|PubMed:28885614"
FT MUTAGEN 145
FT /note="G->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:28885614"
FT MUTAGEN 148
FT /note="W->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:17416655"
FT MUTAGEN 237
FT /note="W->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:17416655"
FT MUTAGEN 267
FT /note="E->A,Q: Loss of activity."
FT /evidence="ECO:0000269|PubMed:17416655,
FT ECO:0000269|PubMed:28675161, ECO:0000269|PubMed:28885614"
FT MUTAGEN 335
FT /note="K->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:17416655,
FT ECO:0000269|PubMed:28675161, ECO:0000269|PubMed:28885614"
FT MUTAGEN 339
FT /note="V->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:28885614"
FT MUTAGEN 339
FT /note="V->G: Loss of activity."
FT /evidence="ECO:0000269|PubMed:28885614"
FT MUTAGEN 342
FT /note="G->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:28885614"
FT MUTAGEN 343
FT /note="E->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:17416655,
FT ECO:0000269|PubMed:28885614"
FT MUTAGEN 352
FT /note="R->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:28885614"
FT MUTAGEN 387
FT /note="C->A,S: Loss of activity."
FT /evidence="ECO:0000269|PubMed:17416655,
FT ECO:0000269|PubMed:28675161, ECO:0000269|PubMed:28885614"
FT MUTAGEN 388
FT /note="Y->A,W: Loss of activity."
FT /evidence="ECO:0000269|PubMed:17416655,
FT ECO:0000269|PubMed:28885614"
FT MUTAGEN 389
FT /note="E->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:17416655,
FT ECO:0000269|PubMed:28885614"
FT MUTAGEN 416
FT /note="F->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:28885614"
FT CONFLICT 186
FT /note="A -> V (in Ref. 2)"
FT /evidence="ECO:0000305"
FT HELIX 2..4
FT /evidence="ECO:0007829|PDB:7ACI"
FT HELIX 6..23
FT /evidence="ECO:0007829|PDB:7ACI"
FT HELIX 24..27
FT /evidence="ECO:0007829|PDB:7ACI"
FT TURN 29..31
FT /evidence="ECO:0007829|PDB:7ACI"
FT HELIX 35..47
FT /evidence="ECO:0007829|PDB:7ACI"
FT TURN 48..50
FT /evidence="ECO:0007829|PDB:7ACI"
FT HELIX 53..71
FT /evidence="ECO:0007829|PDB:7ACI"
FT HELIX 75..82
FT /evidence="ECO:0007829|PDB:7ACI"
FT HELIX 87..115
FT /evidence="ECO:0007829|PDB:7ACI"
FT HELIX 121..125
FT /evidence="ECO:0007829|PDB:7ACI"
FT HELIX 127..139
FT /evidence="ECO:0007829|PDB:7ACI"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:7ACI"
FT HELIX 151..155
FT /evidence="ECO:0007829|PDB:7ACI"
FT STRAND 156..158
FT /evidence="ECO:0007829|PDB:5N6H"
FT HELIX 161..163
FT /evidence="ECO:0007829|PDB:7ACI"
FT HELIX 164..167
FT /evidence="ECO:0007829|PDB:7ACI"
FT HELIX 169..188
FT /evidence="ECO:0007829|PDB:7ACI"
FT HELIX 193..203
FT /evidence="ECO:0007829|PDB:7ACI"
FT HELIX 206..210
FT /evidence="ECO:0007829|PDB:7ACI"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:7ACI"
FT HELIX 218..220
FT /evidence="ECO:0007829|PDB:7ACI"
FT STRAND 222..228
FT /evidence="ECO:0007829|PDB:7ACI"
FT TURN 233..237
FT /evidence="ECO:0007829|PDB:5XHQ"
FT HELIX 239..253
FT /evidence="ECO:0007829|PDB:7ACI"
FT HELIX 254..256
FT /evidence="ECO:0007829|PDB:7ACI"
FT TURN 257..259
FT /evidence="ECO:0007829|PDB:7ACI"
FT STRAND 261..264
FT /evidence="ECO:0007829|PDB:7ACI"
FT STRAND 270..273
FT /evidence="ECO:0007829|PDB:7ACI"
FT HELIX 274..277
FT /evidence="ECO:0007829|PDB:7ACI"
FT HELIX 278..289
FT /evidence="ECO:0007829|PDB:7ACI"
FT TURN 290..292
FT /evidence="ECO:0007829|PDB:7ACI"
FT STRAND 294..304
FT /evidence="ECO:0007829|PDB:7ACI"
FT STRAND 310..320
FT /evidence="ECO:0007829|PDB:7ACI"
FT STRAND 332..334
FT /evidence="ECO:0007829|PDB:7ACI"
FT TURN 340..342
FT /evidence="ECO:0007829|PDB:7ACI"
FT TURN 346..351
FT /evidence="ECO:0007829|PDB:7ACI"
FT TURN 352..356
FT /evidence="ECO:0007829|PDB:5XHQ"
FT HELIX 357..359
FT /evidence="ECO:0007829|PDB:7ACI"
FT STRAND 375..377
FT /evidence="ECO:0007829|PDB:7ACI"
FT STRAND 380..386
FT /evidence="ECO:0007829|PDB:7ACI"
FT HELIX 387..391
FT /evidence="ECO:0007829|PDB:7ACI"
FT HELIX 393..399
FT /evidence="ECO:0007829|PDB:7ACI"
FT STRAND 406..411
FT /evidence="ECO:0007829|PDB:7ACI"
FT HELIX 414..416
FT /evidence="ECO:0007829|PDB:7ACI"
FT HELIX 421..436
FT /evidence="ECO:0007829|PDB:7ACI"
FT STRAND 440..447
FT /evidence="ECO:0007829|PDB:7ACI"
FT STRAND 449..452
FT /evidence="ECO:0007829|PDB:7ACI"
FT STRAND 458..462
FT /evidence="ECO:0007829|PDB:7ACI"
FT STRAND 464..466
FT /evidence="ECO:0007829|PDB:5XHQ"
FT STRAND 468..474
FT /evidence="ECO:0007829|PDB:7ACI"
FT HELIX 482..486
FT /evidence="ECO:0007829|PDB:7ACI"
FT HELIX 489..507
FT /evidence="ECO:0007829|PDB:7ACI"
SQ SEQUENCE 512 AA; 57066 MW; 70CFD6627C286615 CRC64;
MAFASLIERQ RIRLLLALLF GACGTLAFSP YDVWPAAIIS LMGLQALTFN RRPLQSAAIG
FCWGFGLFGS GINWVYVSIA TFGGMPGPVN IFLVVLLAAY LSLYTGLFAG VLSRLWPKTT
WLRVAIAAPA LWQVTEFLRG WVLTGFPWLQ FGYSQIDGPL KGLAPIMGVE AINFLLMMVS
GLLALALVKR NWRPLVVAVV LFALPFPLRY IQWFTPQPEK TIQVSMVQGD IPQSLKWDEG
QLLNTLKIYY NATAPLMGKS SLIIWPESAI TDLEINQQPF LKALDGELRD KGSSLVTGIV
DARLNKQNRY DTYNTIITLG KGAPYSYESA DRYNKNHLVP FGEFVPLESI LRPLAPFFDL
PMSSFSRGPY IQPPLSANGI ELTAAICYEI ILGEQVRDNF RPDTDYLLTI SNDAWFGKSI
GPWQHFQMAR MRALELARPL LRSTNNGITA VIGPQGEIQA MIPQFTREVL TTNVTPTTGL
TPYARTGNWP LWVLTALFGF AAVLMSLRQR RK
