ATXE2_ASTEC
ID ATXE2_ASTEC Reviewed; 695 AA.
AC E8RUP5;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 52.
DE RecName: Full=Lasso peptide isopeptidase AtxE2 {ECO:0000303|PubMed:23862624, ECO:0000303|PubMed:26534965, ECO:0000303|PubMed:27998080};
DE EC=3.4.-.-;
DE AltName: Full=Isopeptide hydrolase AtxE2 {ECO:0000303|PubMed:23862624};
DE Flags: Precursor;
GN Name=atxE2 {ECO:0000303|PubMed:23862624, ECO:0000303|PubMed:26534965,
GN ECO:0000303|PubMed:27998080};
GN OrderedLocusNames=Astex_2444 {ECO:0000312|EMBL:ADU14095.1};
OS Asticcacaulis excentricus (strain ATCC 15261 / DSM 4724 / KCTC 12464 /
OS NCIMB 9791 / VKM B-1370 / CB 48).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Asticcacaulis.
OX NCBI_TaxID=573065;
RN [1] {ECO:0000312|Proteomes:UP000001492}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15261 / DSM 4724 / KCTC 12464 / NCIMB 9791 / VKM B-1370 / CB
RC 48;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Teshima H., Davenport K., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G.,
RA Brun Y.V., Woyke T.;
RT "Complete sequence of chromosome 2 of Asticcacaulis excentricus CB 48.";
RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, EXPRESSION IN E.COLI, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVE SITE,
RP AND MUTAGENESIS OF SER-527.
RX PubMed=23862624; DOI=10.1021/ja4054256;
RA Maksimov M.O., Link A.J.;
RT "Discovery and characterization of an isopeptidase that linearizes lasso
RT peptides.";
RL J. Am. Chem. Soc. 135:12038-12047(2013).
RN [3]
RP FUNCTION, AND EXPRESSION IN E.COLI.
RX PubMed=26534965; DOI=10.1074/jbc.m115.694083;
RA Maksimov M.O., Koos J.D., Zong C., Lisko B., Link A.J.;
RT "Elucidating the specificity determinants of the AtxE2 lasso peptide
RT isopeptidase.";
RL J. Biol. Chem. 290:30806-30812(2015).
RN [4] {ECO:0007744|PDB:5TXC, ECO:0007744|PDB:5TXE}
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) ALONE AND IN COMPLEX WITH ASTEXIN-3,
RP DISULFIDE BONDS, AND MUTAGENESIS OF TRP-111; TRP-116; ASN-121; TYR-438 AND
RP ASN-562.
RX PubMed=27998080; DOI=10.1021/jacs.6b10389;
RA Chekan J.R., Koos J.D., Zong C., Maksimov M.O., Link A.J., Nair S.K.;
RT "Structure of the lasso peptide isopeptidase identifies a topology for
RT processing threaded substrates.";
RL J. Am. Chem. Soc. 138:16452-16458(2016).
CC -!- FUNCTION: Lasso peptide isopeptidase that specifically hydrolyzes
CC Astexin-2 and Astexin-3, converting them to linear peptides
CC (PubMed:23862624). Has only a few specific contacts with subrates,
CC because it recognizes Astexin knotted structure (principally the loop
CC structure) (PubMed:26534965, PubMed:27998080). Its binding to lasso
CC peptides opens them to expose the isopeptide bonds for hydrolysis
CC (PubMed:27998080). {ECO:0000269|PubMed:23862624,
CC ECO:0000269|PubMed:26534965, ECO:0000269|PubMed:27998080}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=131 uM for Astexin-3 {ECO:0000269|PubMed:23862624};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:23862624}.
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DR EMBL; CP002396; ADU14095.1; -; Genomic_DNA.
DR RefSeq; WP_013479920.1; NC_014817.1.
DR PDB; 5TXC; X-ray; 2.40 A; A/B=1-695.
DR PDB; 5TXE; X-ray; 2.20 A; A/B=1-695.
DR PDBsum; 5TXC; -.
DR PDBsum; 5TXE; -.
DR AlphaFoldDB; E8RUP5; -.
DR SMR; E8RUP5; -.
DR STRING; 573065.Astex_2444; -.
DR ESTHER; astec-e8rup5; ACPH_Peptidase_S9.
DR MEROPS; S09.035; -.
DR EnsemblBacteria; ADU14095; ADU14095; Astex_2444.
DR KEGG; aex:Astex_2444; -.
DR eggNOG; COG0823; Bacteria.
DR eggNOG; COG1506; Bacteria.
DR HOGENOM; CLU_391760_0_0_5; -.
DR OMA; KWQPAHR; -.
DR OrthoDB; 821953at2; -.
DR Proteomes; UP000001492; Chromosome 2.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 2.120.10.30; -; 1.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001375; Peptidase_S9.
DR Pfam; PF00326; Peptidase_S9; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Disulfide bond; Hydrolase; Reference proteome;
KW Signal.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..695
FT /note="Lasso peptide isopeptidase AtxE2"
FT /id="PRO_5003230865"
FT ACT_SITE 527
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:23862624"
FT ACT_SITE 610
FT /note="Charge relay system"
FT /evidence="ECO:0000305|PubMed:27998080"
FT ACT_SITE 638
FT /note="Charge relay system"
FT /evidence="ECO:0000305|PubMed:27998080"
FT SITE 116
FT /note="Important for activity. Binds to Astexin-3"
FT /evidence="ECO:0000269|PubMed:27998080"
FT SITE 438
FT /note="Catalytically important residue that stabilizes the
FT alkoxide intermediate. Moves to point toward the isopeptide
FT bond"
FT /evidence="ECO:0000269|PubMed:27998080"
FT SITE 562
FT /note="Important for activity. Binds to Astexin-3"
FT /evidence="ECO:0000269|PubMed:27998080"
FT DISULFID 296..301
FT /evidence="ECO:0007744|PDB:5TXC, ECO:0007744|PDB:5TXE"
FT DISULFID 354..363
FT /evidence="ECO:0007744|PDB:5TXC, ECO:0007744|PDB:5TXE"
FT DISULFID 551..552
FT /evidence="ECO:0007744|PDB:5TXC, ECO:0007744|PDB:5TXE"
FT MUTAGEN 111
FT /note="W->A: No change in activity."
FT /evidence="ECO:0000269|PubMed:27998080"
FT MUTAGEN 116
FT /note="W->A: Decrease in activity."
FT /evidence="ECO:0000269|PubMed:27998080"
FT MUTAGEN 121
FT /note="N->A: Increase in activity."
FT /evidence="ECO:0000269|PubMed:27998080"
FT MUTAGEN 438
FT /note="Y->F: Loss of activity."
FT /evidence="ECO:0000269|PubMed:27998080"
FT MUTAGEN 527
FT /note="S->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:23862624"
FT MUTAGEN 562
FT /note="N->A: Decrease in activity."
FT /evidence="ECO:0000269|PubMed:27998080"
FT HELIX 40..44
FT /evidence="ECO:0007829|PDB:5TXE"
FT STRAND 48..53
FT /evidence="ECO:0007829|PDB:5TXE"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:5TXE"
FT STRAND 67..78
FT /evidence="ECO:0007829|PDB:5TXE"
FT TURN 79..82
FT /evidence="ECO:0007829|PDB:5TXE"
FT STRAND 83..92
FT /evidence="ECO:0007829|PDB:5TXE"
FT STRAND 100..104
FT /evidence="ECO:0007829|PDB:5TXE"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:5TXE"
FT STRAND 138..147
FT /evidence="ECO:0007829|PDB:5TXE"
FT STRAND 150..157
FT /evidence="ECO:0007829|PDB:5TXE"
FT STRAND 163..167
FT /evidence="ECO:0007829|PDB:5TXE"
FT STRAND 173..180
FT /evidence="ECO:0007829|PDB:5TXE"
FT STRAND 183..188
FT /evidence="ECO:0007829|PDB:5TXE"
FT HELIX 190..202
FT /evidence="ECO:0007829|PDB:5TXE"
FT HELIX 203..205
FT /evidence="ECO:0007829|PDB:5TXE"
FT TURN 215..217
FT /evidence="ECO:0007829|PDB:5TXE"
FT STRAND 218..220
FT /evidence="ECO:0007829|PDB:5TXE"
FT STRAND 230..235
FT /evidence="ECO:0007829|PDB:5TXE"
FT TURN 236..238
FT /evidence="ECO:0007829|PDB:5TXE"
FT STRAND 241..243
FT /evidence="ECO:0007829|PDB:5TXE"
FT HELIX 246..253
FT /evidence="ECO:0007829|PDB:5TXE"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:5TXE"
FT STRAND 266..271
FT /evidence="ECO:0007829|PDB:5TXE"
FT STRAND 283..288
FT /evidence="ECO:0007829|PDB:5TXE"
FT HELIX 299..301
FT /evidence="ECO:0007829|PDB:5TXE"
FT STRAND 302..310
FT /evidence="ECO:0007829|PDB:5TXE"
FT TURN 311..314
FT /evidence="ECO:0007829|PDB:5TXE"
FT STRAND 315..323
FT /evidence="ECO:0007829|PDB:5TXE"
FT HELIX 324..326
FT /evidence="ECO:0007829|PDB:5TXE"
FT STRAND 328..335
FT /evidence="ECO:0007829|PDB:5TXE"
FT STRAND 342..357
FT /evidence="ECO:0007829|PDB:5TXE"
FT STRAND 360..367
FT /evidence="ECO:0007829|PDB:5TXE"
FT STRAND 370..378
FT /evidence="ECO:0007829|PDB:5TXE"
FT TURN 379..381
FT /evidence="ECO:0007829|PDB:5TXE"
FT STRAND 384..388
FT /evidence="ECO:0007829|PDB:5TXE"
FT HELIX 394..396
FT /evidence="ECO:0007829|PDB:5TXE"
FT STRAND 401..408
FT /evidence="ECO:0007829|PDB:5TXE"
FT STRAND 414..421
FT /evidence="ECO:0007829|PDB:5TXE"
FT STRAND 431..436
FT /evidence="ECO:0007829|PDB:5TXE"
FT TURN 447..450
FT /evidence="ECO:0007829|PDB:5TXE"
FT HELIX 454..459
FT /evidence="ECO:0007829|PDB:5TXE"
FT STRAND 463..467
FT /evidence="ECO:0007829|PDB:5TXE"
FT HELIX 473..476
FT /evidence="ECO:0007829|PDB:5TXE"
FT HELIX 482..490
FT /evidence="ECO:0007829|PDB:5TXE"
FT HELIX 491..493
FT /evidence="ECO:0007829|PDB:5TXE"
FT HELIX 494..512
FT /evidence="ECO:0007829|PDB:5TXE"
FT STRAND 516..526
FT /evidence="ECO:0007829|PDB:5TXE"
FT HELIX 528..539
FT /evidence="ECO:0007829|PDB:5TXE"
FT STRAND 544..550
FT /evidence="ECO:0007829|PDB:5TXE"
FT HELIX 555..558
FT /evidence="ECO:0007829|PDB:5TXE"
FT TURN 559..562
FT /evidence="ECO:0007829|PDB:5TXE"
FT HELIX 563..570
FT /evidence="ECO:0007829|PDB:5TXE"
FT HELIX 571..573
FT /evidence="ECO:0007829|PDB:5TXE"
FT HELIX 586..588
FT /evidence="ECO:0007829|PDB:5TXE"
FT HELIX 591..594
FT /evidence="ECO:0007829|PDB:5TXE"
FT HELIX 595..597
FT /evidence="ECO:0007829|PDB:5TXE"
FT STRAND 602..607
FT /evidence="ECO:0007829|PDB:5TXE"
FT HELIX 608..611
FT /evidence="ECO:0007829|PDB:5TXE"
FT HELIX 612..614
FT /evidence="ECO:0007829|PDB:5TXE"
FT HELIX 615..623
FT /evidence="ECO:0007829|PDB:5TXE"
FT STRAND 628..633
FT /evidence="ECO:0007829|PDB:5TXE"
FT HELIX 643..662
FT /evidence="ECO:0007829|PDB:5TXE"
FT HELIX 669..671
FT /evidence="ECO:0007829|PDB:5TXE"
FT HELIX 672..684
FT /evidence="ECO:0007829|PDB:5TXE"
SQ SEQUENCE 695 AA; 77392 MW; 462FF5A7D52B028C CRC64;
MRSSKIRCPG AIRVGTLVTA FGCLPHVAFA AAREAPPVTP EVLVRLADIG TMSASETTPL
LSLSPDGRYV AFQVRQADPV TNLNVFRMVV KATDGATDAI DVDVGGEYLF WTIPSWGYAR
NAPSGANLTI QPRWSPSGTH LAYLRQDQGR VRVWRASVKG EGASPVIEDA YDIEDVQWLD
DNTLIYSGRP GFVEAEAEIE REGRRGWVYD ERFHPLTGAR PRVLEPISIV YQVLDLKTGT
RRAATPTEVA RLREKPDPLR AMVGRTTFSV SRTDPQNINA PTTLVARRGE GEPVRCDEEA
CQNITRMWGD ETANVLYFLR REGWASNEMA LYRMPADALK PVRIWHATGL LQGCERQAKR
LICAQESALQ PRRLVTLNLT SGQMSPLYDP NPDLSRYRLP KVERLTLRNR NGIEVFSDLV
LPPDYQLGTR LPLVIVQYSS RGFLRGGTGD ENPILPLATA GFAVLSFHSP RSEASYQRFT
SPIAQSKAEY SNWRNRWNIL HTLEDLIDDL DRRGVIDPAR VGLTGLSDGA TTVHFGLINS
HRFAAAVTSS CCTDSFTASV MNGPRISGAL KAYGIETDQA DDGPFWAATS FVVNASRLDT
PLLIQSADEE YLGALPGFTA LQQARKPVEL IIYPNEHHVK WQPAHRLAVY NRTIDWFRFW
LMDQSDPAPD KAAQYDRWRA LRALRQKSPS PTPAP
