PSA_MYCTU
ID PSA_MYCTU Reviewed; 248 AA.
AC P9WHU1; L0T8P4; O33244; Q7D7I3;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=Proteasome subunit alpha {ECO:0000255|HAMAP-Rule:MF_00289};
DE AltName: Full=20S proteasome alpha subunit {ECO:0000255|HAMAP-Rule:MF_00289};
DE AltName: Full=Proteasome core protein PrcA {ECO:0000255|HAMAP-Rule:MF_00289};
GN Name=prcA {ECO:0000255|HAMAP-Rule:MF_00289}; OrderedLocusNames=Rv2109c;
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 [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 [2]
RP PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE
RP SPECIFICITY, SUBUNIT, ACTIVITY REGULATION, KINETIC PARAMETERS, AND
RP MUTAGENESIS OF 1-MET--SER-8.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=16468985; DOI=10.1111/j.1365-2958.2005.05035.x;
RA Lin G., Hu G., Tsu C., Kunes Y.Z., Li H., Dick L., Parsons T., Li P.,
RA Chen Z., Zwickl P., Weich N., Nathan C.;
RT "Mycobacterium tuberculosis prcBA genes encode a gated proteasome with
RT broad oligopeptide specificity.";
RL Mol. Microbiol. 59:1405-1416(2006).
RN [3]
RP PROTEIN SUBSTRATES.
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY, DETERMINATION OF TRANSLATIONAL START
RP SITE, CLEAVAGE OF INITIATOR METHIONINE, AND ACETYLATION AT SER-2.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=17259624; DOI=10.1099/mic.0.2006/001537-0;
RA Rison S.C., Mattow J., Jungblut P.R., Stoker N.G.;
RT "Experimental determination of translational starts using peptide mass
RT mapping and tandem mass spectrometry within the proteome of Mycobacterium
RT tuberculosis.";
RL Microbiology 153:521-528(2007).
RN [5]
RP ROLE IN VIRULENCE, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=18059281; DOI=10.1038/nm1683;
RA Gandotra S., Schnappinger D., Monteleone M., Hillen W., Ehrt S.;
RT "In vivo gene silencing identifies the Mycobacterium tuberculosis
RT proteasome as essential for the bacteria to persist in mice.";
RL Nat. Med. 13:1515-1520(2007).
RN [6]
RP IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
RX PubMed=19099550; DOI=10.1186/1752-0509-2-109;
RA Raman K., Yeturu K., Chandra N.;
RT "targetTB: a target identification pipeline for Mycobacterium tuberculosis
RT through an interactome, reactome and genome-scale structural analysis.";
RL BMC Syst. Biol. 2:109-109(2008).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [8]
RP ELECTRON MICROSCOPY, AND SUBUNIT.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=20085764; DOI=10.1016/j.febslet.2009.12.057;
RA Poulsen C., Holton S., Geerlof A., Wilmanns M., Song Y.H.;
RT "Stoichiometric protein complex formation and over-expression using the
RT prokaryotic native operon structure.";
RL FEBS Lett. 584:669-674(2010).
RN [9]
RP ROLE IN PERSISTENCE, AND DISRUPTION PHENOTYPE.
RC STRAIN=H37Rv;
RX PubMed=20711362; DOI=10.1371/journal.ppat.1001040;
RA Gandotra S., Lebron M.B., Ehrt S.;
RT "The Mycobacterium tuberculosis proteasome active site threonine is
RT essential for persistence yet dispensable for replication and resistance to
RT nitric oxide.";
RL PLoS Pathog. 6:E1001040-E1001040(2010).
RN [10]
RP PHOSPHORYLATION AT THR-84; THR-178 AND THR-202.
RC STRAIN=H37Rv;
RX PubMed=25224505; DOI=10.1007/s12275-014-4416-2;
RA Anandan T., Han J., Baun H., Nyayapathy S., Brown J.T., Dial R.L.,
RA Moltalvo J.A., Kim M.S., Yang S.H., Ronning D.R., Husson R.N., Suh J.,
RA Kang C.M.;
RT "Phosphorylation regulates mycobacterial proteasome.";
RL J. Microbiol. 52:743-754(2014).
RN [11]
RP INTERACTION WITH BPA.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=25469515; DOI=10.1371/journal.pone.0114348;
RA Delley C.L., Laederach J., Ziemski M., Bolten M., Boehringer D.,
RA Weber-Ban E.;
RT "Bacterial proteasome activator Bpa (Rv3780) is a novel ring-shaped
RT interactor of the mycobacterial proteasome.";
RL PLoS ONE 9:E114348-E114348(2014).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.99 ANGSTROMS) OF 2-248 IN COMPLEXES WITH THE BETA
RP SUBUNIT AND WITH THE MLN-273 INHIBITOR, AND SUBUNIT.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=16468986; DOI=10.1111/j.1365-2958.2005.05036.x;
RA Hu G., Lin G., Wang M., Dick L., Xu R.-M., Nathan C., Li H.;
RT "Structure of the Mycobacterium tuberculosis proteasome and mechanism of
RT inhibition by a peptidyl boronate.";
RL Mol. Microbiol. 59:1417-1428(2006).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.43 ANGSTROMS) OF WILD-TYPE AND OPEN-GATE MUTANT IN
RP COMPLEXES WITH BETA SUBUNIT; INHIBITOR HT1171 AND INHIBITOR GL1, ACTIVITY
RP REGULATION, AND BIOTECHNOLOGY.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=19759536; DOI=10.1038/nature08357;
RA Lin G., Li D., de Carvalho L.P., Deng H., Tao H., Vogt G., Wu K.,
RA Schneider J., Chidawanyika T., Warren J.D., Li H., Nathan C.;
RT "Inhibitors selective for mycobacterial versus human proteasomes.";
RL Nature 461:621-626(2009).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH BETA SUBUNIT AND
RP FELLUTAMIDE B INHIBITOR, AND ACTIVITY REGULATION.
RX PubMed=20558127; DOI=10.1016/j.abb.2010.06.009;
RA Lin G., Li D., Chidawanyika T., Nathan C., Li H.;
RT "Fellutamide B is a potent inhibitor of the Mycobacterium tuberculosis
RT proteasome.";
RL Arch. Biochem. Biophys. 501:214-220(2010).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF WILD-TYPE AND OPEN-GATE MUTANT IN
RP COMPLEX WITH BETA SUBUNIT, SUBUNIT, GATED STRUCTURE, AND PROTEASOME
RP ASSEMBLY PROCESS.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=20461058; DOI=10.1038/emboj.2010.95;
RA Li D., Li H., Wang T., Pan H., Lin G., Li H.;
RT "Structural basis for the assembly and gate closure mechanisms of the
RT Mycobacterium tuberculosis 20S proteasome.";
RL EMBO J. 29:2037-2047(2010).
CC -!- FUNCTION: Component of the proteasome core, a large protease complex
CC with broad specificity involved in protein degradation. The
CC M.tuberculosis proteasome is able to cleave oligopeptides not only
CC after hydrophobic but also after basic, acidic and small neutral
CC residues (PubMed:16468985). In complex with the ATPase Mpa, degrades
CC protein targets conjugated to a prokaryotic ubiquitin-like protein
CC (Pup). Among the identified substrates of the M.tuberculosis proteasome
CC are the pupylated FabD, PanB and Mpa proteins (PubMed:17082771). One
CC function of the proteasome is to contribute to M.tuberculosis ability
CC to resist killing by host macrophages, since the core proteasome is
CC essential for persistence of the pathogen during the chronic phase of
CC infection in mice (PubMed:18059281). Likely functions to recycle amino
CC acids under nutrient starvation, thereby enabling the cell to maintain
CC basal metabolic activities (PubMed:20711362) (By similarity). The
CC mechanism of protection against bactericidal chemistries of the host's
CC immune response probably involves the degradation of proteins that are
CC irreversibly oxidized, nitrated, or nitrosated. A proteolysis-
CC independent activity of the proteasome core is required for optimal
CC growth of M.tuberculosis in mouse lungs and for RNI resistance; in
CC contrast, long-term survival of M.tuberculosis in stationary phase and
CC during starvation in vitro and in the chronic phase of mouse infection
CC required a proteolytically active proteasome (PubMed:20711362).
CC {ECO:0000250|UniProtKB:A0QZ46, ECO:0000255|HAMAP-Rule:MF_00289,
CC ECO:0000269|PubMed:16468985, ECO:0000269|PubMed:17082771,
CC ECO:0000269|PubMed:18059281, ECO:0000269|PubMed:20711362}.
CC -!- ACTIVITY REGULATION: The formation of the proteasomal ATPase ARC-20S
CC proteasome complex, likely via the docking of the C-termini of ARC into
CC the intersubunit pockets in the alpha-rings, may trigger opening of the
CC gate for substrate entry. Interconversion between the open-gate and
CC close-gate conformations leads to a dynamic regulation of the 20S
CC proteasome proteolysis activity. In vitro, chymotryptic and tryptic
CC activities of the proteasome are both completely inhibited by
CC epoxomicin and by the peptidyl boronate inhibitor MLN-273. Also
CC inhibited by Mg(2+), Ca(2+) and SDS. It was also shown that certain
CC oxathiazol-2-one compounds can act as selective suicide-substrate
CC inhibitors of the M.tuberculosis proteasome by irreversibly
CC cyclocarbonylating its active site threonine. Proteasome activity is
CC potently inhibited by fellutamide B (Ki=6.8 nM), a lipopeptide aldehyde
CC that forms a reversible bond with the beta-OH of the active site
CC threonine (PubMed:20558127). {ECO:0000255|HAMAP-Rule:MF_00289,
CC ECO:0000269|PubMed:16468985, ECO:0000269|PubMed:19759536,
CC ECO:0000269|PubMed:20558127}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=56 uM for succinyl-LLVY-7-amino-4-methylcoumarin
CC {ECO:0000269|PubMed:16468985};
CC Vmax=0.24 nmol/min/mg enzyme with succinyl-LLVY-7-amino-4-
CC methylcoumarin as substrate {ECO:0000269|PubMed:16468985};
CC -!- PATHWAY: Protein degradation; proteasomal Pup-dependent pathway.
CC {ECO:0000255|HAMAP-Rule:MF_00289}.
CC -!- SUBUNIT: The 20S proteasome core is composed of 14 alpha and 14 beta
CC subunits that assemble into four stacked heptameric rings, resulting in
CC a barrel-shaped structure. The two inner rings, each composed of seven
CC catalytic beta subunits, are sandwiched by two outer rings, each
CC composed of seven alpha subunits. The catalytic chamber with the active
CC sites is on the inside of the barrel. Has a gated structure, the ends
CC of the cylinder being occluded by the N-termini of the alpha-subunits.
CC Is capped by the proteasome-associated ATPase, ARC (Mpa). Can also
CC interact with the bacterial proteasome activator Bpa through the C-
CC terminal hydrophobic-tyrosine-X motif (HbYX motif) of Bpa; Bpa forms a
CC homooligomeric ring-like structure which stacks co-axially with the
CC proteasomal alpha-rings (PubMed:25469515). {ECO:0000255|HAMAP-
CC Rule:MF_00289, ECO:0000269|PubMed:16468985,
CC ECO:0000269|PubMed:16468986, ECO:0000269|PubMed:20085764,
CC ECO:0000269|PubMed:20461058, ECO:0000269|PubMed:25469515}.
CC -!- INTERACTION:
CC P9WHU1; P9WHT9: prcB; NbExp=6; IntAct=EBI-7948002, EBI-7947958;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00289}.
CC -!- PTM: Phosphorylated by the PknB kinase at three threonine residues
CC (Thr-84, Thr-202, and Thr-178) in a sequential manner. Phosphorylation
CC enhances proteolytic activity of the proteasome.
CC {ECO:0000269|PubMed:25224505}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking the core proteasome prcBA subunits
CC exhibit reduced growth and persistence in mice. They are also
CC attenuated in interferon-gamma-deficient mice. They also display
CC increased sensitivity to reactive nitrogen intermediates (RNI) and
CC increased resistance to oxidative stress. {ECO:0000269|PubMed:18059281,
CC ECO:0000269|PubMed:20711362}.
CC -!- BIOTECHNOLOGY: In the course of search for new antibiotics, a class of
CC oxathiazol-2-one compounds has been identified that selectively
CC inhibits the M.tuberculosis proteasome over the human proteasome and
CC that kills non-replicating M.tuberculosis.
CC {ECO:0000269|PubMed:19759536}.
CC -!- MISCELLANEOUS: Was identified as a high-confidence drug target.
CC -!- SIMILARITY: Belongs to the peptidase T1A family. {ECO:0000255|HAMAP-
CC Rule:MF_00289}.
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DR EMBL; AL123456; CCP44884.1; -; Genomic_DNA.
DR PIR; H70511; H70511.
DR RefSeq; NP_216625.1; NC_000962.3.
DR RefSeq; WP_003906749.1; NZ_NVQJ01000058.1.
DR PDB; 2FHG; X-ray; 3.23 A; 1/A/B/D/F/I/K/M/O/Q/S/U/W/Y=2-248.
DR PDB; 2FHH; X-ray; 2.99 A; 1/A/B/D/F/I/K/M/O/Q/S/U/W/Y=2-248.
DR PDB; 3H6F; X-ray; 2.51 A; 1/A/B/D/F/I/K/M/O/Q/S/U/W/Y=1-248.
DR PDB; 3H6I; X-ray; 2.43 A; 1/A/B/D/F/I/K/M/O/Q/S/U/W/Y=1-248.
DR PDB; 3HF9; X-ray; 2.88 A; 1/3/A/B/D/F/I/K/M/O/Q/S/U/W/Y/a/b/d/f/i/k/m/o/q/s/u/w/y=10-248.
DR PDB; 3HFA; X-ray; 2.50 A; 1/A/B/D/F/I/K/M/O/Q/S/U/W/Y=10-248.
DR PDB; 3KRD; X-ray; 2.50 A; 1/A/B/D/F/I/K/M/O/Q/S/U/W/Y=1-248.
DR PDB; 3MFE; X-ray; 2.60 A; 1/A/B/D/F/I/K/M/O/Q/S/U/W/Y=10-248.
DR PDB; 3MI0; X-ray; 2.20 A; 1/A/B/D/F/I/K/M/O/Q/S/U/W/Y=1-248.
DR PDB; 3MKA; X-ray; 2.51 A; 1/A/B/D/F/I/K/M/O/Q/S/U/W/Y=1-248.
DR PDB; 5LZP; EM; 3.45 A; 0/2/4/6/8/B/D/H/J/M/Q/S/W/Y=8-248.
DR PDB; 5THO; X-ray; 3.00 A; A/B/C/D/E/F/G/O/P/Q/R/S/T/U=10-248.
DR PDB; 5TRG; X-ray; 2.80 A; A/B/C/D/E/F/G/O/P/Q/R/S/T/U=10-248.
DR PDB; 5TRR; X-ray; 3.10 A; A/B/C/D/E/F/G/O/P/Q/R/S/T/U=10-248.
DR PDB; 5TRS; X-ray; 3.08 A; A/B/C/D/E/F/G/O/P/Q/R/S/T/U=10-248.
DR PDB; 5TRY; X-ray; 3.00 A; A/B/C/D/E/F/G/O/P/Q/R/S/T/U=10-248.
DR PDB; 5TS0; X-ray; 2.85 A; A/B/C/D/E/F/G/O/P/Q/R/S/T/U=10-248.
DR PDB; 6BGL; EM; 3.40 A; A/C/D/E/F/G/H/I/J/K/L/M/N/O=1-248.
DR PDB; 6BGO; EM; 4.20 A; A/C/D/E/F/G/H/I/J/K/L/M/N/O=1-248.
DR PDB; 6OCW; X-ray; 2.60 A; A/B/C/D/E/F/G/O/P/Q/R/S/T/U=10-248.
DR PDB; 6OCZ; X-ray; 2.65 A; A/B/C/D/E/F/G/O/P/Q/R/S/T/U=10-248.
DR PDB; 6ODE; X-ray; 2.90 A; A/B/C/D/E/F/G/O/P/Q/R/S/T/U=10-248.
DR PDB; 6WNK; X-ray; 2.28 A; A/B/C/D/E/F/G/O/P/Q/R/S/T/U=10-248.
DR PDB; 7PXC; EM; 3.84 A; 0/2/4/6/8/I/K/O/Q/T/X/Z/d/f=1-248.
DR PDBsum; 2FHG; -.
DR PDBsum; 2FHH; -.
DR PDBsum; 3H6F; -.
DR PDBsum; 3H6I; -.
DR PDBsum; 3HF9; -.
DR PDBsum; 3HFA; -.
DR PDBsum; 3KRD; -.
DR PDBsum; 3MFE; -.
DR PDBsum; 3MI0; -.
DR PDBsum; 3MKA; -.
DR PDBsum; 5LZP; -.
DR PDBsum; 5THO; -.
DR PDBsum; 5TRG; -.
DR PDBsum; 5TRR; -.
DR PDBsum; 5TRS; -.
DR PDBsum; 5TRY; -.
DR PDBsum; 5TS0; -.
DR PDBsum; 6BGL; -.
DR PDBsum; 6BGO; -.
DR PDBsum; 6OCW; -.
DR PDBsum; 6OCZ; -.
DR PDBsum; 6ODE; -.
DR PDBsum; 6WNK; -.
DR PDBsum; 7PXC; -.
DR AlphaFoldDB; P9WHU1; -.
DR SMR; P9WHU1; -.
DR IntAct; P9WHU1; 1.
DR MINT; P9WHU1; -.
DR STRING; 83332.Rv2109c; -.
DR DrugBank; DB04732; N-(4-MORPHOLINE)CARBONYL-B-(1-NAPHTHYL)-L-ALANINE-L-LEUCINE BORONIC ACID.
DR iPTMnet; P9WHU1; -.
DR PaxDb; P9WHU1; -.
DR DNASU; 887538; -.
DR GeneID; 887538; -.
DR KEGG; mtu:Rv2109c; -.
DR TubercuList; Rv2109c; -.
DR eggNOG; COG0638; Bacteria.
DR OMA; QIYRLPH; -.
DR PhylomeDB; P9WHU1; -.
DR UniPathway; UPA00997; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0019773; C:proteasome core complex, alpha-subunit complex; IDA:UniProtKB.
DR GO; GO:0004298; F:threonine-type endopeptidase activity; IDA: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:0051603; P:proteolysis involved in protein catabolic process; IDA:MTBBASE.
DR Gene3D; 3.60.20.10; -; 1.
DR HAMAP; MF_00289_B; Proteasome_A_B; 1.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR023332; Proteasome_alpha-type.
DR InterPro; IPR022296; Proteasome_asu_bac.
DR InterPro; IPR001353; Proteasome_sua/b.
DR PANTHER; PTHR11599:SF69; PTHR11599:SF69; 1.
DR Pfam; PF00227; Proteasome; 1.
DR SUPFAM; SSF56235; SSF56235; 1.
DR TIGRFAMs; TIGR03691; 20S_bact_alpha; 1.
DR PROSITE; PS51475; PROTEASOME_ALPHA_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW Phosphoprotein; Proteasome; Reference proteome; Virulence.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:17259624,
FT ECO:0007744|PubMed:21969609"
FT CHAIN 2..248
FT /note="Proteasome subunit alpha"
FT /id="PRO_0000383482"
FT MOD_RES 2
FT /note="N-acetylserine; partial"
FT /evidence="ECO:0000269|PubMed:17259624,
FT ECO:0007744|PubMed:21969609"
FT MOD_RES 84
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:25224505"
FT MOD_RES 178
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:25224505"
FT MOD_RES 202
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:25224505"
FT MUTAGEN 1..8
FT /note="Missing: Markedly increases peptidolytic activity.
FT Disappearance of the apparent obstruction in alpha rings.
FT Designated open-gate mutant."
FT /evidence="ECO:0000269|PubMed:16468985"
FT HELIX 9..25
FT /evidence="ECO:0007829|PDB:3MI0"
FT STRAND 30..35
FT /evidence="ECO:0007829|PDB:3MI0"
FT STRAND 38..44
FT /evidence="ECO:0007829|PDB:3MI0"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:3MI0"
FT STRAND 52..57
FT /evidence="ECO:0007829|PDB:3MI0"
FT STRAND 60..66
FT /evidence="ECO:0007829|PDB:3MI0"
FT HELIX 68..88
FT /evidence="ECO:0007829|PDB:3MI0"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:3MI0"
FT HELIX 96..113
FT /evidence="ECO:0007829|PDB:3MI0"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:3MI0"
FT STRAND 120..126
FT /evidence="ECO:0007829|PDB:3MI0"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:3HF9"
FT STRAND 137..141
FT /evidence="ECO:0007829|PDB:3MI0"
FT STRAND 147..158
FT /evidence="ECO:0007829|PDB:3MI0"
FT HELIX 160..170
FT /evidence="ECO:0007829|PDB:3MI0"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:3HFA"
FT HELIX 177..190
FT /evidence="ECO:0007829|PDB:3MI0"
FT HELIX 205..207
FT /evidence="ECO:0007829|PDB:6WNK"
FT STRAND 208..214
FT /evidence="ECO:0007829|PDB:3MI0"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:3MI0"
FT STRAND 222..224
FT /evidence="ECO:0007829|PDB:3MI0"
FT HELIX 227..232
FT /evidence="ECO:0007829|PDB:3MI0"
SQ SEQUENCE 248 AA; 26881 MW; 0356FED74869998A CRC64;
MSFPYFISPE QAMRERSELA RKGIARAKSV VALAYAGGVL FVAENPSRSL QKISELYDRV
GFAAAGKFNE FDNLRRGGIQ FADTRGYAYD RRDVTGRQLA NVYAQTLGTI FTEQAKPYEV
ELCVAEVAHY GETKRPELYR ITYDGSIADE PHFVVMGGTT EPIANALKES YAENASLTDA
LRIAVAALRA GSADTSGGDQ PTLGVASLEV AVLDANRPRR AFRRITGSAL QALLVDQESP
QSDGESSG
