ARC_MYCTU
ID ARC_MYCTU Reviewed; 609 AA.
AC P9WQN5; L0T8W3; O33250; P63345; Q0G9Y7;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 48.
DE RecName: Full=Proteasome-associated ATPase {ECO:0000255|HAMAP-Rule:MF_02112};
DE AltName: Full=AAA ATPase forming ring-shaped complexes {ECO:0000255|HAMAP-Rule:MF_02112};
DE Short=ARC {ECO:0000255|HAMAP-Rule:MF_02112};
DE AltName: Full=Mycobacterial proteasome ATPase {ECO:0000255|HAMAP-Rule:MF_02112};
GN Name=mpa {ECO:0000255|HAMAP-Rule:MF_02112}; OrderedLocusNames=Rv2115c;
GN ORFNames=MTCY261.11c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION AS AN ATPASE,
RP BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, SUBUNIT, AND
RP MUTAGENESIS OF LYS-299; ASP-371; GLU-372 AND 608-TYR-GLU-609.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=15659170; DOI=10.1111/j.1365-2958.2004.04403.x;
RA Darwin K.H., Lin G., Chen Z., Li H., Nathan C.F.;
RT "Characterization of a Mycobacterium tuberculosis proteasomal ATPase
RT homologue.";
RL Mol. Microbiol. 55:561-571(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [3]
RP GENE NAME, ROLE IN RESISTANCE TO RNI, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=14671303; DOI=10.1126/science.1091176;
RA Darwin K.H., Ehrt S., Gutierrez-Ramos J.-C., Weich N., Nathan C.F.;
RT "The proteasome of Mycobacterium tuberculosis is required for resistance to
RT nitric oxide.";
RL Science 302:1963-1966(2003).
RN [4]
RP TARGET OF RNI, AND S-NITROSYLATION.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=15626759; DOI=10.1073/pnas.0406133102;
RA Rhee K.Y., Erdjument-Bromage H., Tempst P., Nathan C.F.;
RT "S-nitroso proteome of Mycobacterium tuberculosis: enzymes of intermediary
RT metabolism and antioxidant defense.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:467-472(2005).
RN [5]
RP FUNCTION IN THE PROTEASOME DEGRADATION PATHWAY, REGULATION OF MPA LEVELS,
RP PROTEASOME SUBSTRATE, AND MUTAGENESIS OF TYR-608 AND 608-TYR-GLU-609.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=17082771; DOI=10.1038/sj.emboj.7601405;
RA Pearce M.J., Arora P., Festa R.A., Butler-Wu S.M., Gokhale R.S.,
RA Darwin K.H.;
RT "Identification of substrates of the Mycobacterium tuberculosis
RT proteasome.";
RL EMBO J. 25:5423-5432(2006).
RN [6]
RP INTERACTION WITH PUP, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=18832610; DOI=10.1126/science.1163885;
RA Pearce M.J., Mintseris J., Ferreyra J., Gygi S.P., Darwin K.H.;
RT "Ubiquitin-like protein involved in the proteasome pathway of Mycobacterium
RT tuberculosis.";
RL Science 322:1104-1107(2008).
RN [7]
RP INTERACTION WITH PUP.
RX PubMed=19580545; DOI=10.1042/bj20090738;
RA Liao S., Shang Q., Zhang X., Zhang J., Xu C., Tu X.;
RT "Pup, a prokaryotic ubiquitin-like protein, is an intrinsically disordered
RT protein.";
RL Biochem. J. 422:207-215(2009).
RN [8]
RP INTERACTION WITH PUP, STOICHIOMETRY OF THE PUP-MPA COMPLEX, AND DOMAIN.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=19761766; DOI=10.1016/j.febslet.2009.09.020;
RA Sutter M., Striebel F., Damberger F.F., Allain F.H., Weber-Ban E.;
RT "A distinct structural region of the prokaryotic ubiquitin-like protein
RT (Pup) is recognized by the N-terminal domain of the proteasomal ATPase
RT Mpa.";
RL FEBS Lett. 583:3151-3157(2009).
RN [9]
RP INTERACTION WITH PUP, AND STOICHIOMETRY OF THE PUP-MPA COMPLEX.
RX PubMed=19607839; DOI=10.1016/j.jmb.2009.07.018;
RA Chen X., Solomon W.C., Kang Y., Cerda-Maira F., Darwin K.H., Walters K.J.;
RT "Prokaryotic ubiquitin-like protein Pup is intrinsically disordered.";
RL J. Mol. Biol. 392:208-217(2009).
RN [10]
RP INTERACTION WITH PUP, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=19448618; DOI=10.1038/nsmb.1597;
RA Striebel F., Imkamp F., Sutter M., Steiner M., Mamedov A., Weber-Ban E.;
RT "Bacterial ubiquitin-like modifier Pup is deamidated and conjugated to
RT substrates by distinct but homologous enzymes.";
RL Nat. Struct. Mol. Biol. 16:647-651(2009).
RN [11]
RP FUNCTION AS UNFOLDASE AND TRANSLOCASE, DOMAIN, MUTAGENESIS OF PHE-341 AND
RP 608-TYR-GLU-609, AND RECONSTITUTION OF THE PROTEASOME DEGRADATION PATHWAY.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=20203624; DOI=10.1038/emboj.2010.23;
RA Striebel F., Hunkeler M., Summer H., Weber-Ban E.;
RT "The mycobacterial Mpa-proteasome unfolds and degrades pupylated substrates
RT by engaging Pup's N-terminus.";
RL EMBO J. 29:1262-1271(2010).
RN [12]
RP PUPYLATION AT LYS-591, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=20066036; DOI=10.1371/journal.pone.0008589;
RA Festa R.A., McAllister F., Pearce M.J., Mintseris J., Burns K.E.,
RA Gygi S.P., Darwin K.H.;
RT "Prokaryotic ubiquitin-like protein (Pup) proteome of Mycobacterium
RT tuberculosis.";
RL PLoS ONE 5:E8589-E8589(2010).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 98-245, FUNCTION, INTERACTION WITH
RP PROTEASOME, DOMAIN, AND MUTAGENESIS OF ARG-120; ARG-173; TRP-187; LYS-225;
RP LYS-235; LYS-299; VAL-342; ASP-371 AND TYR-608.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=19836337; DOI=10.1016/j.str.2009.08.010;
RA Wang T., Li H., Lin G., Tang C., Li D., Nathan C., Darwin K.H., Li H.;
RT "Structural insights on the Mycobacterium tuberculosis proteasomal ATPase
RT Mpa.";
RL Structure 17:1377-1385(2009).
CC -!- FUNCTION: ATPase which is responsible for recognizing, binding,
CC unfolding and translocation of pupylated proteins into the bacterial
CC 20S proteasome core particle. May be essential for opening the gate of
CC the 20S proteasome via an interaction with its C-terminus, thereby
CC allowing substrate entry and access to the site of proteolysis. Thus,
CC the C-termini of the proteasomal ATPase may function like a 'key in a
CC lock' to induce gate opening and therefore regulate proteolysis. Is
CC required but not sufficient to confer resistance against the lethal
CC effects of reactive nitrogen intermediates (RNI), antimicrobial
CC molecules produced by activated macrophages and other cell types.
CC {ECO:0000255|HAMAP-Rule:MF_02112, ECO:0000269|PubMed:14671303,
CC ECO:0000269|PubMed:15659170, ECO:0000269|PubMed:17082771,
CC ECO:0000269|PubMed:19836337, ECO:0000269|PubMed:20203624}.
CC -!- ACTIVITY REGULATION: ATPase activity is inhibited by EDTA, N-
CC ethylmaleimide (NEM) and sodium azide. {ECO:0000269|PubMed:15659170}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=330 uM for ATP {ECO:0000269|PubMed:15659170};
CC Vmax=62 pmol/min/ug enzyme {ECO:0000269|PubMed:15659170};
CC pH dependence:
CC Optimum pH is 7.4-7.5. {ECO:0000269|PubMed:15659170};
CC -!- PATHWAY: Protein degradation; proteasomal Pup-dependent pathway.
CC {ECO:0000255|HAMAP-Rule:MF_02112}.
CC -!- SUBUNIT: Homohexamer. Assembles into a hexameric ring structure that
CC caps the 20S proteasome core. Strongly interacts with the prokaryotic
CC ubiquitin-like protein Pup through a hydrophobic interface; the
CC interacting region of Mpa lies in its N-terminal coiled-coil domain.
CC There is one Pup binding site per Mpa hexamer ring; the K(D) measured
CC is about 3.8 uM. Upon ATP-binding, the C-terminus of Mpa interacts with
CC the alpha-rings of the proteasome core, possibly by binding to the
CC intersubunit pockets. {ECO:0000255|HAMAP-Rule:MF_02112,
CC ECO:0000269|PubMed:15659170, ECO:0000269|PubMed:18832610,
CC ECO:0000269|PubMed:19448618, ECO:0000269|PubMed:19580545,
CC ECO:0000269|PubMed:19607839, ECO:0000269|PubMed:19761766,
CC ECO:0000269|PubMed:19836337}.
CC -!- INTERACTION:
CC P9WQN5; P9WQN5: mpa; NbExp=5; IntAct=EBI-7241067, EBI-7241067;
CC P9WQN5; P9WHN5: pup; NbExp=6; IntAct=EBI-7241067, EBI-7241023;
CC -!- DOMAIN: Consists of three main regions, an N-terminal coiled-coil
CC domain (residues 1-96) that binds to protein Pup and functions as a
CC docking station, an interdomain (residues 97-245) involved in Mpa
CC hexamerization, and a C-terminal ATPase domain of the AAA type
CC (residues 246-609). {ECO:0000269|PubMed:19761766,
CC ECO:0000269|PubMed:19836337, ECO:0000269|PubMed:20203624}.
CC -!- PTM: Pupylated at Lys-591 by the prokaryotic ubiquitin-like protein
CC Pup, which leads to its degradation by the proteasome. Mpa thus
CC promotes its own turnover. {ECO:0000269|PubMed:20066036}.
CC -!- PTM: Mpa is a target of RNI, thereby is S-nitrosylated in the phagosome
CC of immunologically activated host macrophages, which causes enzyme
CC inhibition. {ECO:0000269|PubMed:15626759}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene accumulate pupylated
CC proteins. These cells also become hypersensitive to reactive nitrogen
CC intermediates (RNI) and are severely attenuated in both wild-type and
CC nitric oxide synthase 2 deficient mice. Moreover, they display
CC increased resistance to hydrogen peroxide.
CC {ECO:0000269|PubMed:14671303, ECO:0000269|PubMed:18832610}.
CC -!- MISCELLANEOUS: Was identified as a natural substrate of the
CC M.tuberculosis proteasome.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000255|HAMAP-
CC Rule:MF_02112}.
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DR EMBL; DQ888314; ABI36485.1; -; Genomic_DNA.
DR EMBL; AL123456; CCP44890.1; -; Genomic_DNA.
DR PIR; F70512; F70512.
DR RefSeq; NP_216631.1; NC_000962.3.
DR RefSeq; WP_003411035.1; NZ_NVQJ01000058.1.
DR PDB; 3FP9; X-ray; 2.00 A; A/B/C/D/E/F/G/H/I/J/K/L=98-245.
DR PDB; 3M91; X-ray; 1.80 A; A/C=46-96.
DR PDB; 3M9B; X-ray; 3.94 A; A/B/C/D/E/F/G/H/I/J/K/L=1-234.
DR PDB; 3M9D; X-ray; 4.50 A; A/B/C/D/E/F/J/K/L/M/N/O=1-234.
DR PDB; 3M9H; X-ray; 2.00 A; A/B/C/D/E/F=46-96.
DR PDB; 5KWA; X-ray; 2.90 A; A/B=95-602.
DR PDB; 5KZF; X-ray; 3.49 A; A/B/C/D/E/F/G/H/I/J/K/L=98-609.
DR PDB; 7LJF; EM; 4.00 A; A/B/C/D/E/F=1-601.
DR PDB; 7PXC; EM; 3.84 A; 1/A/B/C/D/E/F=1-609.
DR PDBsum; 3FP9; -.
DR PDBsum; 3M91; -.
DR PDBsum; 3M9B; -.
DR PDBsum; 3M9D; -.
DR PDBsum; 3M9H; -.
DR PDBsum; 5KWA; -.
DR PDBsum; 5KZF; -.
DR PDBsum; 7LJF; -.
DR PDBsum; 7PXC; -.
DR AlphaFoldDB; P9WQN5; -.
DR SMR; P9WQN5; -.
DR IntAct; P9WQN5; 1.
DR MINT; P9WQN5; -.
DR STRING; 83332.Rv2115c; -.
DR PaxDb; P9WQN5; -.
DR DNASU; 887297; -.
DR GeneID; 887297; -.
DR KEGG; mtu:Rv2115c; -.
DR TubercuList; Rv2115c; -.
DR eggNOG; COG1222; Bacteria.
DR OMA; CVDEFKE; -.
DR PhylomeDB; P9WQN5; -.
DR BRENDA; 5.6.1.5; 3445.
DR UniPathway; UPA00997; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0022623; C:proteasome-activating nucleotidase complex; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0004176; F:ATP-dependent peptidase activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0140035; F:ubiquitination-like modification-dependent protein binding; IDA:UniProtKB.
DR GO; GO:0071732; P:cellular response to nitric oxide; IMP:UniProtKB.
DR GO; GO:0030682; P:mitigation of host defenses by symbiont; IMP:UniProtKB.
DR GO; GO:0019941; P:modification-dependent protein catabolic process; IDA:UniProtKB.
DR GO; GO:0010498; P:proteasomal protein catabolic process; IDA:UniProtKB.
DR GO; GO:0010499; P:proteasomal ubiquitin-independent protein catabolic process; IDA:MTBBASE.
DR GO; GO:0043335; P:protein unfolding; IDA:UniProtKB.
DR GO; GO:0051409; P:response to nitrosative stress; IMP:MTBBASE.
DR Gene3D; 2.40.50.140; -; 2.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_02112; ARC_ATPase; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR032501; Prot_ATP_ID_OB_C.
DR InterPro; IPR041626; Prot_ATP_ID_OB_N.
DR InterPro; IPR022482; Proteasome_ATPase.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF16450; Prot_ATP_ID_OB; 1.
DR Pfam; PF17758; Prot_ATP_OB_N; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR03689; pup_AAA; 1.
DR PROSITE; PS00674; AAA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Chaperone; Coiled coil; Isopeptide bond;
KW Nucleotide-binding; Proteasome; Reference proteome; S-nitrosylation;
KW Ubl conjugation; Virulence.
FT CHAIN 1..609
FT /note="Proteasome-associated ATPase"
FT /id="PRO_0000084778"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 608..609
FT /note="Docks into pockets in the proteasome alpha-ring"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02112"
FT COILED 20..96
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02112"
FT BINDING 296..301
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02112"
FT CROSSLNK 591
FT /note="Isoglutamyl lysine isopeptide (Lys-Gln) (interchain
FT with Q-Cter in protein Pup)"
FT /evidence="ECO:0000269|PubMed:20066036"
FT MUTAGEN 120
FT /note="R->A: Does not dramatically affect proteasome
FT substrate degradation."
FT /evidence="ECO:0000269|PubMed:19836337"
FT MUTAGEN 173
FT /note="R->E: Impairs Mpa hexamerization; when associated
FT with A-187 and E-235."
FT /evidence="ECO:0000269|PubMed:19836337"
FT MUTAGEN 187
FT /note="W->A: Impairs Mpa hexamerization; when associated
FT with E-173 and E-235."
FT /evidence="ECO:0000269|PubMed:19836337"
FT MUTAGEN 225
FT /note="K->A: Does not dramatically affect proteasome
FT substrate degradation."
FT /evidence="ECO:0000269|PubMed:19836337"
FT MUTAGEN 235
FT /note="K->E: Impairs Mpa hexamerization; when associated
FT with E-173 and A-187."
FT /evidence="ECO:0000269|PubMed:19836337"
FT MUTAGEN 299
FT /note="K->Q: Reduces both ATPase activity and ATP affinity.
FT Abolishes proteasome substrate degradation and protection
FT against RNI."
FT /evidence="ECO:0000269|PubMed:15659170,
FT ECO:0000269|PubMed:19836337"
FT MUTAGEN 341
FT /note="F->A: Abolishes unfolding capacity."
FT /evidence="ECO:0000269|PubMed:20203624"
FT MUTAGEN 341
FT /note="F->Y: No effect on unfolding capacity."
FT /evidence="ECO:0000269|PubMed:20203624"
FT MUTAGEN 342
FT /note="V->A: Abolishes proteasome substrate degradation."
FT /evidence="ECO:0000269|PubMed:19836337"
FT MUTAGEN 371
FT /note="D->A: Severely reduces ATPase activity. Abolishes
FT proteasome substrate degradation and protection against
FT RNI."
FT /evidence="ECO:0000269|PubMed:15659170,
FT ECO:0000269|PubMed:19836337"
FT MUTAGEN 372
FT /note="E->A: Severely reduces ATPase activity. Abolishes
FT protection against RNI."
FT /evidence="ECO:0000269|PubMed:15659170"
FT MUTAGEN 372
FT /note="E->Q: Abolishes protection against RNI."
FT /evidence="ECO:0000269|PubMed:15659170"
FT MUTAGEN 608..609
FT /note="Missing: Retains ATPase and unfolding activities,
FT yet abolishes proteasome substrate degradation and
FT protection against RNI. Is also highly attenuated in mice."
FT /evidence="ECO:0000269|PubMed:15659170,
FT ECO:0000269|PubMed:17082771, ECO:0000269|PubMed:20203624"
FT MUTAGEN 608
FT /note="Y->E,F: Abolishes proteasome substrate degradation
FT and protection against RNI."
FT /evidence="ECO:0000269|PubMed:17082771,
FT ECO:0000269|PubMed:19836337"
FT HELIX 53..94
FT /evidence="ECO:0007829|PDB:3M91"
FT STRAND 99..107
FT /evidence="ECO:0007829|PDB:3FP9"
FT STRAND 109..117
FT /evidence="ECO:0007829|PDB:3FP9"
FT STRAND 120..126
FT /evidence="ECO:0007829|PDB:3FP9"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:5KWA"
FT STRAND 140..143
FT /evidence="ECO:0007829|PDB:3FP9"
FT STRAND 149..152
FT /evidence="ECO:0007829|PDB:3FP9"
FT STRAND 158..167
FT /evidence="ECO:0007829|PDB:3FP9"
FT STRAND 171..177
FT /evidence="ECO:0007829|PDB:3FP9"
FT STRAND 183..188
FT /evidence="ECO:0007829|PDB:3FP9"
FT HELIX 190..193
FT /evidence="ECO:0007829|PDB:3FP9"
FT HELIX 203..205
FT /evidence="ECO:0007829|PDB:3FP9"
FT STRAND 219..223
FT /evidence="ECO:0007829|PDB:3FP9"
FT TURN 224..227
FT /evidence="ECO:0007829|PDB:3FP9"
FT STRAND 228..233
FT /evidence="ECO:0007829|PDB:3FP9"
FT HELIX 238..245
FT /evidence="ECO:0007829|PDB:3FP9"
FT TURN 251..253
FT /evidence="ECO:0007829|PDB:5KWA"
FT HELIX 258..268
FT /evidence="ECO:0007829|PDB:5KWA"
FT HELIX 270..273
FT /evidence="ECO:0007829|PDB:5KWA"
FT HELIX 275..280
FT /evidence="ECO:0007829|PDB:5KWA"
FT STRAND 288..294
FT /evidence="ECO:0007829|PDB:5KWA"
FT HELIX 299..312
FT /evidence="ECO:0007829|PDB:5KWA"
FT STRAND 328..333
FT /evidence="ECO:0007829|PDB:5KWA"
FT HELIX 334..338
FT /evidence="ECO:0007829|PDB:5KWA"
FT HELIX 345..360
FT /evidence="ECO:0007829|PDB:5KWA"
FT TURN 361..363
FT /evidence="ECO:0007829|PDB:5KWA"
FT STRAND 366..371
FT /evidence="ECO:0007829|PDB:5KWA"
FT HELIX 393..403
FT /evidence="ECO:0007829|PDB:5KWA"
FT STRAND 409..416
FT /evidence="ECO:0007829|PDB:5KWA"
FT HELIX 418..420
FT /evidence="ECO:0007829|PDB:5KWA"
FT HELIX 423..426
FT /evidence="ECO:0007829|PDB:5KWA"
FT STRAND 433..436
FT /evidence="ECO:0007829|PDB:5KWA"
FT HELIX 442..449
FT /evidence="ECO:0007829|PDB:5KWA"
FT TURN 450..452
FT /evidence="ECO:0007829|PDB:5KWA"
FT HELIX 461..465
FT /evidence="ECO:0007829|PDB:5KWA"
FT TURN 466..469
FT /evidence="ECO:0007829|PDB:5KWA"
FT HELIX 471..486
FT /evidence="ECO:0007829|PDB:5KWA"
FT HELIX 491..493
FT /evidence="ECO:0007829|PDB:5KWA"
FT STRAND 494..500
FT /evidence="ECO:0007829|PDB:5KWA"
FT STRAND 505..509
FT /evidence="ECO:0007829|PDB:5KWA"
FT HELIX 510..513
FT /evidence="ECO:0007829|PDB:5KWA"
FT HELIX 516..537
FT /evidence="ECO:0007829|PDB:5KWA"
FT HELIX 544..559
FT /evidence="ECO:0007829|PDB:5KWA"
FT HELIX 567..577
FT /evidence="ECO:0007829|PDB:5KWA"
FT STRAND 581..586
FT /evidence="ECO:0007829|PDB:5KWA"
FT STRAND 597..599
FT /evidence="ECO:0007829|PDB:5KWA"
SQ SEQUENCE 609 AA; 67401 MW; 4D5F4E630614C58D CRC64;
MGESERSEAF GIPRDSPLSS GDAAELEQLR REAAVLREQL ENAVGSHAPT RSARDIHQLE
ARIDSLAARN SKLMETLKEA RQQLLALREE VDRLGQPPSG YGVLLATHDD DTVDVFTSGR
KMRLTCSPNI DAASLKKGQT VRLNEALTVV EAGTFEAVGE ISTLREILAD GHRALVVGHA
DEERVVWLAD PLIAEDLPDG LPEALNDDTR PRKLRPGDSL LVDTKAGYAF ERIPKAEVED
LVLEEVPDVS YADIGGLSRQ IEQIRDAVEL PFLHKELYRE YSLRPPKGVL LYGPPGCGKT
LIAKAVANSL AKKMAEVRGD DAHEAKSYFL NIKGPELLNK FVGETERHIR LIFQRAREKA
SEGTPVIVFF DEMDSIFRTR GTGVSSDVET TVVPQLLSEI DGVEGLENVI VIGASNREDM
IDPAILRPGR LDVKIKIERP DAEAAQDIYS KYLTEFLPVH ADDLAEFDGD RSACIKAMIE
KVVDRMYAEI DDNRFLEVTY ANGDKEVMYF KDFNSGAMIQ NVVDRAKKNA IKSVLETGQP
GLRIQHLLDS IVDEFAENED LPNTTNPDDW ARISGKKGER IVYIRTLVTG KSSSASRAID
TESNLGQYL
