ID RAVZ_LEGPH Reviewed; 502 AA. AC Q5ZUV9; DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot. DT 23-NOV-2004, sequence version 1. DT 22-FEB-2023, entry version 79. DE RecName: Full=Cysteine protease RavZ {ECO:0000305}; DE EC=3.4.22.- {ECO:0000269|PubMed:23112293}; DE AltName: Full=Region allowing vacuole colocalization protein Z {ECO:0000303|PubMed:20880356}; GN Name=ravZ {ECO:0000303|PubMed:20880356, ECO:0000303|PubMed:23112293}; GN OrderedLocusNames=lpg1683 {ECO:0000312|EMBL:AAU27763.1}; OS Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC OS 33152 / DSM 7513). OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; OC Legionellaceae; Legionella. OX NCBI_TaxID=272624; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Philadelphia 1 / ATCC 33152 / DSM 7513; RX PubMed=15448271; DOI=10.1126/science.1099776; RA Chien M., Morozova I., Shi S., Sheng H., Chen J., Gomez S.M., Asamani G., RA Hill K., Nuara J., Feder M., Rineer J., Greenberg J.J., Steshenko V., RA Park S.H., Zhao B., Teplitskaya E., Edwards J.R., Pampou S., Georghiou A., RA Chou I.-C., Iannuccilli W., Ulz M.E., Kim D.H., Geringer-Sameth A., RA Goldsberry C., Morozov P., Fischer S.G., Segal G., Qu X., Rzhetsky A., RA Zhang P., Cayanis E., De Jong P.J., Ju J., Kalachikov S., Shuman H.A., RA Russo J.J.; RT "The genomic sequence of the accidental pathogen Legionella pneumophila."; RL Science 305:1966-1968(2004). RN [2] RP SUBCELLULAR LOCATION. RX PubMed=20880356; DOI=10.1111/j.1462-5822.2010.01531.x; RA Huang L., Boyd D., Amyot W.M., Hempstead A.D., Luo Z.Q., O'Connor T.J., RA Chen C., Machner M., Montminy T., Isberg R.R.; RT "The E Block motif is associated with Legionella pneumophila translocated RT substrates."; RL Cell. Microbiol. 13:227-245(2011). RN [3] RP FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, SUBCELLULAR LOCATION, AND RP MUTAGENESIS OF CYS-258. RX PubMed=23112293; DOI=10.1126/science.1227026; RA Choy A., Dancourt J., Mugo B., O'Connor T.J., Isberg R.R., Melia T.J., RA Roy C.R.; RT "The Legionella effector RavZ inhibits host autophagy through irreversible RT Atg8 deconjugation."; RL Science 338:1072-1076(2012). RN [4] RP FUNCTION. RX PubMed=28971069; DOI=10.3389/fcimb.2017.00384; RA Kubori T., Bui X.T., Hubber A., Nagai H.; RT "Legionella RavZ plays a role in preventing ubiquitin recruitment to RT bacteria-containing vacuoles."; RL Front. Cell. Infect. Microbiol. 7:384-384(2017). RN [5] RP FUNCTION. RX PubMed=29458288; DOI=10.1080/15548627.2018.1437341; RA Kauffman K.J., Yu S., Jin J., Mugo B., Nguyen N., O'Brien A., Nag S., RA Lystad A.H., Melia T.J.; RT "Delipidation of mammalian Atg8-family proteins by each of the four ATG4 RT proteases."; RL Autophagy 14:992-1010(2018). RN [6] RP FUNCTION, SUBCELLULAR LOCATION, AND DOMAIN. RX PubMed=31722778; DOI=10.5483/bmbrep.2019.52.12.211; RA Park S.W., Jun Y.W., Jeon P., Lee Y.K., Park J.H., Lee S.H., Lee J.A., RA Jang D.J.; RT "LIR motifs and the membrane-targeting domain are complementary in the RT function of RavZ."; RL BMB Rep. 52:700-705(2019). RN [7] RP FUNCTION, SUBCELLULAR LOCATION, AND DOMAIN. RX PubMed=31719622; DOI=10.1038/s41598-019-53372-2; RA Park S.W., Jeon P., Jun Y.W., Park J.H., Lee S.H., Lee S., Lee J.A., RA Jang D.J.; RT "Monitoring LC3- or GABARAP-positive autophagic membranes using modified RT RavZ-based probes."; RL Sci. Rep. 9:16593-16593(2019). RN [8] RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF 63-MET-ASN-64 AND RP 175-GLN--GLN-177. RX PubMed=32686895; DOI=10.1002/cbic.202000359; RA Yang A., Pantoom S., Wu Y.W.; RT "Distinct mechanisms for processing autophagy protein LC3-PE by RavZ and RT ATG4B."; RL ChemBioChem 21:3377-3382(2020). RN [9] RP FUNCTION. RX PubMed=32482642; DOI=10.1128/iai.00793-19; RA Omotade T.O., Roy C.R.; RT "Legionella pneumophila excludes autophagy adaptors from the ubiquitin- RT labeled vacuole in which it resides."; RL Infect. Immun. 88:0-0(2020). RN [10] RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION. RX PubMed=33298241; DOI=10.5483/bmbrep.2021.54.2.190; RA Park J.H., Lee S.H., Park S.W., Jun Y.W., Kim K., Jeon P., Kim M., RA Lee J.A., Jang D.J.; RT "Deciphering the role of a membrane-targeting domain in assisting endosomal RT and autophagic membrane localization of a RavZ protein catalytic domain."; RL BMB Rep. 54:118-123(2021). RN [11] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=33909989; DOI=10.1016/j.molcel.2021.03.020; RA Durgan J., Lystad A.H., Sloan K., Carlsson S.R., Wilson M.I., Marcassa E., RA Ulferts R., Webster J., Lopez-Clavijo A.F., Wakelam M.J., Beale R., RA Simonsen A., Oxley D., Florey O.; RT "Non-canonical autophagy drives alternative ATG8 conjugation to RT phosphatidylserine."; RL Mol. Cell 81:2031-2040(2021). RN [12] {ECO:0007744|PDB:5CQC} RP X-RAY CRYSTALLOGRAPHY (2.98 ANGSTROMS) OF 10-458, FUNCTION, CATALYTIC RP ACTIVITY, ACTIVE SITES, SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS OF RP HIS-176; ASP-197; 211-TYR--ARG-217; 211-TYR--TYR-216; CYS-258; LYS-306; RP ARG-343; 359-LYS--LYS-362 AND LYS-404. RX PubMed=26343456; DOI=10.1016/j.devcel.2015.08.010; RA Horenkamp F.A., Kauffman K.J., Kohler L.J., Sherwood R.K., Krueger K.P., RA Shteyn V., Roy C.R., Melia T.J., Reinisch K.M.; RT "The Legionella anti-autophagy effector RavZ targets the autophagosome via RT PI3P- and curvature-sensing motifs."; RL Dev. Cell 34:569-576(2015). RN [13] {ECO:0007744|PDB:5HZY, ECO:0007744|PDB:5IO3} RP X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 49-502, DOMAIN, AND MUTAGENESIS RP OF 16-PHE--LEU-19; 29-PHE--LEU-32 AND 435-PHE--ILE-438. RX PubMed=27791457; DOI=10.1080/15548627.2016.1243199; RA Kwon D.H., Kim S., Jung Y.O., Roh K.H., Kim L., Kim B.W., Hong S.B., RA Lee I.Y., Song J.H., Lee W.C., Choi E.J., Hwang K.Y., Song H.K.; RT "The 1:2 complex between RavZ and LC3 reveals a mechanism for deconjugation RT of LC3 on the phagophore membrane."; RL Autophagy 13:70-81(2017). RN [14] {ECO:0007744|PDB:5XAD} RP X-RAY CRYSTALLOGRAPHY (1.88 ANGSTROMS) OF 12-34 IN COMPLEX WITH MAP1LC3B, RP AND DOMAIN. RX PubMed=28668392; DOI=10.1016/j.bbrc.2017.06.173; RA Kwon D.H., Kim L., Kim B.W., Kim J.H., Roh K.H., Choi E.J., Song H.K.; RT "A novel conformation of the LC3-interacting region motif revealed by the RT structure of a complex between LC3B and RavZ."; RL Biochem. Biophys. Res. Commun. 490:1093-1099(2017). RN [15] {ECO:0007744|PDB:5MS2, ECO:0007744|PDB:5MS5} RP X-RAY CRYSTALLOGRAPHY (1.53 ANGSTROMS) OF 24-36 AND 39-46 IN COMPLEX WITH RP MAP1LC3B, FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, DOMAIN, AND RP MUTAGENESIS OF PHE-29; 139-LEU--LEU-143; 180-LEU--ILE-182; LEU-208; RP 211-TYR--TYR-216; TYR-211; PHE-212; TYR-216; 224-LEU--ILE-232; RP 237-PHE--PHE-242 AND CYS-258. RX PubMed=28395732; DOI=10.7554/elife.23905; RA Yang A., Pantoom S., Wu Y.W.; RT "Elucidation of the anti-autophagy mechanism of the Legionella effector RT RavZ using semisynthetic LC3 proteins."; RL Elife 6:0-0(2017). CC -!- FUNCTION: Cysteine protease effector that inhibits host cell autophagy CC by targeting lipid-conjugated ATG8 family proteins on pre- CC autophagosomal structures (PubMed:23112293, PubMed:29458288, CC PubMed:32686895, PubMed:31722778, PubMed:31719622, PubMed:33298241, CC PubMed:26343456, PubMed:28395732). Specifically hydrolyzes the amide CC bond between the C-terminal glycine residue and an adjacent aromatic CC residue in ATG8 proteins conjugated to phosphatidylethanolamine (PE), CC producing an ATG8 protein that cannot be reconjugated by host ATG7 and CC ATG3 (PubMed:23112293, PubMed:29458288, PubMed:32686895, CC PubMed:26343456, PubMed:28395732). Mechanistically, Ravz interacts with CC ATG8 proteins conjugated to PE via its LIR motifs, extracts them from CC the membrane of autophagosomes and integrates the PE part into its own CC lipid-binding site (PubMed:28395732). It then removes the lipid CC component of the ATG8 protein (PubMed:28395732). Also able to mediate CC delipidation of ATG8 proteins conjugated to phosphatidylserine (PS) CC during non-canonical autophagy (PubMed:33909989). Inhibits host CC ubiquitin recruitment to bacteria-containing vacuoles, suggesting that CC it is able to mediate delipidation of other proteins in addition to CC ATG8 proteins (PubMed:28971069). It is however not involved in the CC exclusion of autophagy adapters from bacteria-containing vacuoles CC decorated with ubiquitin (PubMed:32482642). CC {ECO:0000269|PubMed:23112293, ECO:0000269|PubMed:26343456, CC ECO:0000269|PubMed:28395732, ECO:0000269|PubMed:28971069, CC ECO:0000269|PubMed:29458288, ECO:0000269|PubMed:31719622, CC ECO:0000269|PubMed:31722778, ECO:0000269|PubMed:32482642, CC ECO:0000269|PubMed:32686895, ECO:0000269|PubMed:33298241, CC ECO:0000269|PubMed:33909989}. CC -!- CATALYTIC ACTIVITY: CC Reaction=[protein]-C-terminal L-amino acid-glycyl- CC phosphatidylethanolamide + H2O = 1,2-diacyl-sn-glycero-3- CC phosphoethanolamine-N-glycine + [protein]-C-terminal CC L-amino acid; Xref=Rhea:RHEA:67664, Rhea:RHEA- CC COMP:17323, Rhea:RHEA-COMP:17349, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:90782, ChEBI:CHEBI:172870, ChEBI:CHEBI:172941; CC Evidence={ECO:0000269|PubMed:23112293, ECO:0000269|PubMed:26343456, CC ECO:0000269|PubMed:28395732, ECO:0000269|PubMed:32686895, CC ECO:0000269|PubMed:33298241}; CC -!- CATALYTIC ACTIVITY: CC Reaction=[protein]-C-terminal L-amino acid-glycyl-phosphatidylserine + CC H2O = 1,2-diacyl-sn-glycero-3-phospho-L-serine-N-glycine + [protein]- CC C-terminal L-amino acid; Xref=Rhea:RHEA:67912, CC Rhea:RHEA-COMP:17326, Rhea:RHEA-COMP:17349, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:90782, ChEBI:CHEBI:172942, ChEBI:CHEBI:176543; CC Evidence={ECO:0000269|PubMed:33909989}; CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20880356}. Host CC cytoplasmic vesicle membrane {ECO:0000269|PubMed:23112293, CC ECO:0000269|PubMed:26343456, ECO:0000269|PubMed:31719622, CC ECO:0000269|PubMed:31722778, ECO:0000269|PubMed:33298241}. CC Note=Translocated into the host cell via the type IV secretion system CC (T4SS) (Probable). In host cells, localizes to mature autophagosome CC membranes (PubMed:23112293, PubMed:31722778, PubMed:31719622, CC PubMed:33298241, PubMed:26343456). {ECO:0000269|PubMed:23112293, CC ECO:0000269|PubMed:26343456, ECO:0000269|PubMed:31719622, CC ECO:0000269|PubMed:31722778, ECO:0000269|PubMed:33298241, CC ECO:0000305|PubMed:23112293}. CC -!- DOMAIN: The LIR motifs (LC3-interacting regions) are required for the CC interaction with ATG8 family proteins (PubMed:31722778, CC PubMed:27791457, PubMed:28668392, PubMed:28395732). The LIR motifs 1 CC and 2 at the N-terminus bind one ATG8 protein and the LIR motif 3 at CC the C-terminus binds another ATG8 protein (PubMed:31722778, CC PubMed:27791457). Among ATG8 proteins, the LIR motif 3 has preference CC for host GABARAP (GABARAP GABARAPL1, GABARAPL2) compared to LC3 CC (MAP1LC3A, MAP1LC3B, MAP1LC3C) (PubMed:31719622). CC {ECO:0000269|PubMed:27791457, ECO:0000269|PubMed:28395732, CC ECO:0000269|PubMed:28668392, ECO:0000269|PubMed:31719622, CC ECO:0000269|PubMed:31722778}. CC -!- DOMAIN: The membrane targeting (MT) region binds phosphatidylinositol CC 3-monophosphate (PI3P) (PubMed:26343456). The MT region, together with CC the alpha-3 helix promote localization to high-curvature membranes, CC intimating localization to highly curved domains in autophagosome CC intermediate membranes (PubMed:26343456). The alpha-3 helix is involved CC in extraction of the phosphatidylethanolamine (PE) moiety and docking CC of the acyl chains into the lipid-binding site (PubMed:28395732). CC {ECO:0000269|PubMed:26343456, ECO:0000269|PubMed:28395732}. 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; AE017354; AAU27763.1; -; Genomic_DNA. DR RefSeq; WP_010947410.1; NC_002942.5. DR RefSeq; YP_095710.1; NC_002942.5. DR PDB; 5CQC; X-ray; 2.98 A; A=10-458. DR PDB; 5HZY; X-ray; 2.55 A; A=49-502. DR PDB; 5IO3; X-ray; 2.74 A; A=1-502. DR PDB; 5IZV; X-ray; 2.81 A; A/B=1-502. DR PDB; 5MS2; X-ray; 2.47 A; A=1-431. DR PDB; 5MS5; X-ray; 1.53 A; A/B=24-36, A/B=39-46. DR PDB; 5MS7; X-ray; 2.80 A; A=20-502. DR PDB; 5MS8; X-ray; 2.85 A; A=1-487. DR PDB; 5XAD; X-ray; 1.88 A; C/D=12-34. DR PDBsum; 5CQC; -. DR PDBsum; 5HZY; -. DR PDBsum; 5IO3; -. DR PDBsum; 5IZV; -. DR PDBsum; 5MS2; -. DR PDBsum; 5MS5; -. DR PDBsum; 5MS7; -. DR PDBsum; 5MS8; -. DR PDBsum; 5XAD; -. DR AlphaFoldDB; Q5ZUV9; -. DR SMR; Q5ZUV9; -. DR STRING; 272624.lpg1683; -. DR PaxDb; Q5ZUV9; -. DR EnsemblBacteria; AAU27763; AAU27763; lpg1683. DR GeneID; 66490815; -. DR KEGG; lpn:lpg1683; -. DR PATRIC; fig|272624.6.peg.1764; -. DR eggNOG; ENOG5031DWI; Bacteria. DR HOGENOM; CLU_559960_0_0_6; -. DR OMA; EITAFCA; -. DR OrthoDB; 5646986at2; -. DR Proteomes; UP000000609; Chromosome. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0044162; C:host cell cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell. DR GO; GO:0033648; C:host intracellular membrane-bounded organelle; IDA:UniProtKB. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW. DR GO; GO:0008234; F:cysteine-type peptidase activity; IDA:UniProtKB. DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IDA:UniProtKB. DR GO; GO:0051697; P:protein delipidation; IDA:UniProtKB. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR GO; GO:0140321; P:suppression of host autophagy; IDA:UniProtKB. PE 1: Evidence at protein level; KW 3D-structure; Host cytoplasmic vesicle; Host membrane; Hydrolase; Membrane; KW Protease; Reference proteome; Secreted; Thiol protease; Virulence. FT CHAIN 1..502 FT /note="Cysteine protease RavZ" FT /id="PRO_0000454158" FT REGION 49..325 FT /note="Catalytic region" FT /evidence="ECO:0000303|PubMed:27791457" FT REGION 211..217 FT /note="Alpha-3 helix" FT /evidence="ECO:0000303|PubMed:26343456" FT REGION 326..431 FT /note="Membrane targeting region" FT /evidence="ECO:0000303|PubMed:27791457" FT MOTIF 9..23 FT /note="LIR 1" FT /evidence="ECO:0000269|PubMed:27791457" FT MOTIF 23..37 FT /note="LIR 2" FT /evidence="ECO:0000269|PubMed:27791457" FT MOTIF 429..443 FT /note="LIR 3" FT /evidence="ECO:0000269|PubMed:27791457" FT ACT_SITE 176 FT /evidence="ECO:0000269|PubMed:26343456" FT ACT_SITE 197 FT /evidence="ECO:0000269|PubMed:26343456" FT ACT_SITE 258 FT /evidence="ECO:0000269|PubMed:23112293, FT ECO:0000269|PubMed:26343456, ECO:0000269|PubMed:28395732" FT MUTAGEN 16..19 FT /note="FEEL->AEEA: In mLIR1; only binds one ATG8 protein FT instead of two." FT /evidence="ECO:0000269|PubMed:27791457" FT MUTAGEN 29..32 FT /note="FDLL->ADLA: In mLIR2; only binds one ATG8 protein FT instead of two." FT /evidence="ECO:0000269|PubMed:27791457" FT MUTAGEN 29 FT /note="F->A: Reduced ability to cleave lipid-conjugated FT ATG8 family proteins." FT /evidence="ECO:0000269|PubMed:28395732" FT MUTAGEN 63..64 FT /note="MN->AA: Abolished ability to cleave lipid-conjugated FT ATG8 family proteins." FT /evidence="ECO:0000269|PubMed:32686895" FT MUTAGEN 139..143 FT /note="LDRRL->DDRRD: Reduced ability to cleave lipid- FT conjugated ATG8 family proteins." FT /evidence="ECO:0000269|PubMed:28395732" FT MUTAGEN 175..177 FT /note="QHQ->AQA: Does not affect ability to cleave lipid- FT conjugated ATG8 family proteins." FT /evidence="ECO:0000269|PubMed:32686895" FT MUTAGEN 176 FT /note="H->A: Abolished ability to cleave lipid-conjugated FT ATG8 family proteins; when associated with A-258." FT /evidence="ECO:0000269|PubMed:26343456" FT MUTAGEN 180..182 FT /note="LTI->DTD: Reduced ability to cleave lipid-conjugated FT ATG8 family proteins." FT /evidence="ECO:0000269|PubMed:28395732" FT MUTAGEN 197 FT /note="D->A: Abolished ability to cleave lipid-conjugated FT ATG8 family proteins." FT /evidence="ECO:0000269|PubMed:26343456" FT MUTAGEN 208 FT /note="L->D: Reduced ability to cleave lipid-conjugated FT ATG8 family proteins." FT /evidence="ECO:0000269|PubMed:28395732" FT MUTAGEN 211..217 FT /note="YFKGKYR->AAAGAAA: Reduced binding to membranes." FT /evidence="ECO:0000269|PubMed:26343456" FT MUTAGEN 211..216 FT /note="YFKGKY->DDKGKD: Reduced binding to membranes. FT Abolished ability to cleave lipid-conjugated ATG8 family FT proteins." FT /evidence="ECO:0000269|PubMed:26343456, FT ECO:0000269|PubMed:28395732" FT MUTAGEN 211 FT /note="Y->D: Reduced ability to cleave lipid-conjugated FT ATG8 family proteins." FT /evidence="ECO:0000269|PubMed:28395732" FT MUTAGEN 212 FT /note="F->D: Reduced ability to cleave lipid-conjugated FT ATG8 family proteins." FT /evidence="ECO:0000269|PubMed:28395732" FT MUTAGEN 216 FT /note="Y->D: Slightly reduced ability to cleave lipid- FT conjugated ATG8 family proteins." FT /evidence="ECO:0000269|PubMed:28395732" FT MUTAGEN 224..232 FT /note="LTQSIEKAI->DTQSDEKAD: Reduced ability to cleave FT lipid-conjugated ATG8 family proteins." FT /evidence="ECO:0000269|PubMed:28395732" FT MUTAGEN 237..242 FT /note="FTLGKF->DTDGKD: Reduced ability to cleave lipid- FT conjugated ATG8 family proteins." FT /evidence="ECO:0000269|PubMed:28395732" FT MUTAGEN 258 FT /note="C->A,S: Abolished ability to cleave lipid-conjugated FT ATG8 family proteins. Abolished ability to cleave lipid- FT conjugated ATG8 family proteins; when associated with A- FT 176." FT /evidence="ECO:0000269|PubMed:23112293, FT ECO:0000269|PubMed:28395732, ECO:0000269|PubMed:31719622" FT MUTAGEN 306 FT /note="K->A: Reduced binding to phosphatidylinositol 3- FT monophosphate (PI3P); when associated with A-404." FT /evidence="ECO:0000269|PubMed:26343456" FT MUTAGEN 343 FT /note="R->A: Strongly reduced binding to FT phosphatidylinositol 3-monophosphate (PI3P); when FT associated with 359-A--A-362." FT /evidence="ECO:0000269|PubMed:26343456" FT MUTAGEN 359..362 FT /note="KTAK->ATAA: Strongly reduced binding to FT phosphatidylinositol 3-monophosphate (PI3P); when FT associated with A-343." FT /evidence="ECO:0000269|PubMed:26343456" FT MUTAGEN 404 FT /note="K->A: Reduced binding to phosphatidylinositol 3- FT monophosphate (PI3P); when associated with A-306." FT /evidence="ECO:0000269|PubMed:26343456" FT MUTAGEN 435..438 FT /note="FVTI->AVTA: In mLIR3; only binds one ATG8 protein FT instead of two." FT /evidence="ECO:0000269|PubMed:27791457" FT STRAND 12..17 FT /evidence="ECO:0007829|PDB:5XAD" FT STRAND 23..25 FT /evidence="ECO:0007829|PDB:5XAD" FT STRAND 29..34 FT /evidence="ECO:0007829|PDB:5XAD" FT HELIX 41..43 FT /evidence="ECO:0007829|PDB:5MS2" FT TURN 44..46 FT /evidence="ECO:0007829|PDB:5MS2" FT STRAND 49..51 FT /evidence="ECO:0007829|PDB:5MS2" FT HELIX 59..61 FT /evidence="ECO:0007829|PDB:5MS2" FT HELIX 65..71 FT /evidence="ECO:0007829|PDB:5MS2" FT HELIX 72..74 FT /evidence="ECO:0007829|PDB:5MS2" FT STRAND 78..80 FT /evidence="ECO:0007829|PDB:5CQC" FT TURN 85..87 FT /evidence="ECO:0007829|PDB:5MS2" FT STRAND 88..90 FT /evidence="ECO:0007829|PDB:5MS2" FT STRAND 92..94 FT /evidence="ECO:0007829|PDB:5MS7" FT STRAND 99..108 FT /evidence="ECO:0007829|PDB:5MS2" FT STRAND 110..114 FT /evidence="ECO:0007829|PDB:5MS2" FT STRAND 121..124 FT /evidence="ECO:0007829|PDB:5MS2" FT STRAND 126..130 FT /evidence="ECO:0007829|PDB:5MS8" FT STRAND 133..135 FT /evidence="ECO:0007829|PDB:5HZY" FT HELIX 137..152 FT /evidence="ECO:0007829|PDB:5MS2" FT STRAND 157..170 FT /evidence="ECO:0007829|PDB:5MS2" FT STRAND 176..185 FT /evidence="ECO:0007829|PDB:5MS2" FT TURN 186..189 FT /evidence="ECO:0007829|PDB:5MS2" FT STRAND 190..198 FT /evidence="ECO:0007829|PDB:5MS2" FT HELIX 206..211 FT /evidence="ECO:0007829|PDB:5MS2" FT TURN 212..214 FT /evidence="ECO:0007829|PDB:5MS2" FT STRAND 218..220 FT /evidence="ECO:0007829|PDB:5IO3" FT HELIX 221..232 FT /evidence="ECO:0007829|PDB:5MS2" FT STRAND 233..236 FT /evidence="ECO:0007829|PDB:5IO3" FT STRAND 237..239 FT /evidence="ECO:0007829|PDB:5MS7" FT STRAND 243..247 FT /evidence="ECO:0007829|PDB:5MS2" FT HELIX 255..275 FT /evidence="ECO:0007829|PDB:5MS2" FT STRAND 284..288 FT /evidence="ECO:0007829|PDB:5MS2" FT HELIX 289..292 FT /evidence="ECO:0007829|PDB:5MS2" FT HELIX 295..307 FT /evidence="ECO:0007829|PDB:5MS2" FT HELIX 312..321 FT /evidence="ECO:0007829|PDB:5MS2" FT HELIX 329..345 FT /evidence="ECO:0007829|PDB:5MS2" FT STRAND 352..354 FT /evidence="ECO:0007829|PDB:5IO3" FT HELIX 359..379 FT /evidence="ECO:0007829|PDB:5MS2" FT HELIX 384..397 FT /evidence="ECO:0007829|PDB:5MS2" FT HELIX 400..412 FT /evidence="ECO:0007829|PDB:5MS2" FT HELIX 418..422 FT /evidence="ECO:0007829|PDB:5MS2" FT HELIX 423..425 FT /evidence="ECO:0007829|PDB:5MS2" SQ SEQUENCE 502 AA; 56242 MW; 698B442E58770745 CRC64; MKGKLTGKDK LIVDEFEELG EQESDIDEFD LLEGDEKLPG DSELDKTTSI YPPETSWEVN KGMNSSRLHK LYSLFFDKSS AFYLGDDVSV LEDKPLTGAY GFQSKKNDQQ IFLFRPDSDY VAGYHVDAKS DAGWVNDKLD RRLSEISEFC SKATQPATFI LPFVEMPTDI TKGVQHQVLL TISYDPKSKQ LTPTVYDSIG RDTYSESLSS YFKGKYRTTC DEILTQSIEK AIKSTDFTLG KFTRAAYNHQ NRLTEGNCGS YTFRTIKEVI SSSAQGTEVK IPGSGYITSN SYLTSQHVQD IESCIKYRNL GVVDIESALT EGKTLPVQLS EFIVALEDYG KLRSQQSEKS MLNFIGYSKT AKLTAVELLI GILNDIKGKN EISESQYDKL VKEVDCLMDS SLGKLVQFHL KNLGAESLQK LVLPCVKFDD TIDDFVTIEK DELFDVPDIT GEELASKKGI EQGALDKEAL LKQKQIKTDL LDLREEDKTG LKKPLHGGIK VK //