SIDJ_LEGPH
ID SIDJ_LEGPH Reviewed; 873 AA.
AC Q5ZTK6;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Calmodulin-dependent glutamylase SidJ {ECO:0000303|PubMed:31330532};
DE EC=6.-.-.- {ECO:0000269|PubMed:31123136, ECO:0000269|PubMed:31330531, ECO:0000269|PubMed:31330532};
GN Name=sidJ {ECO:0000303|PubMed:31330532}; OrderedLocusNames=lpg2155;
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 FUNCTION.
RX PubMed=28497808; DOI=10.1038/cr.2017.66;
RA Qiu J., Yu K., Fei X., Liu Y., Nakayasu E.S., Piehowski P.D., Shaw J.B.,
RA Puvar K., Das C., Liu X., Luo Z.Q.;
RT "A unique deubiquitinase that deconjugates phosphoribosyl-linked protein
RT ubiquitination.";
RL Cell Res. 27:865-881(2017).
RN [3]
RP FUNCTION, COFACTOR, CATALYTIC ACTIVITY, INTERACTION WITH HOST
RP CALMODULIN/CMD1, AND MUTAGENESIS OF ILE-841 AND GLN-842.
RX PubMed=31330532; DOI=10.1038/s41586-019-1440-8;
RA Bhogaraju S., Bonn F., Mukherjee R., Adams M., Pfleiderer M.M., Galej W.P.,
RA Matkovic V., Lopez-Mosqueda J., Kalayil S., Shin D., Dikic I.;
RT "Inhibition of bacterial ubiquitin ligases by SidJ-calmodulin catalysed
RT glutamylation.";
RL Nature 572:382-386(2019).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH HOST CALMODULIN, AND
RP COFACTOR.
RX PubMed=31330531; DOI=10.1038/s41586-019-1439-1;
RA Gan N., Zhen X., Liu Y., Xu X., He C., Qiu J., Liu Y., Fujimoto G.M.,
RA Nakayasu E.S., Zhou B., Zhao L., Puvar K., Das C., Ouyang S., Luo Z.Q.;
RT "Regulation of phosphoribosyl ubiquitination by a calmodulin-dependent
RT glutamylase.";
RL Nature 572:387-391(2019).
RN [5] {ECO:0007744|PDB:6OQQ}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH CALMODULIN/CMD1,
RP CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=31123136; DOI=10.1126/science.aaw7446;
RA Black M.H., Osinski A., Gradowski M., Servage K.A., Pawlowski K.,
RA Tomchick D.R., Tagliabracci V.S.;
RT "Bacterial pseudokinase catalyzes protein polyglutamylation to inhibit the
RT SidE-family ubiquitin ligases.";
RL Science 364:787-792(2019).
CC -!- FUNCTION: Glutamylase that mediates the covalent attachment of
CC glutamate moieties to SdeA on one of the catalytic residues that is
CC required for its mono-ADP-ribosyltransferase activity (PubMed:31330532,
CC PubMed:31330531). In turn, inhibits SdeA ubiquitinating activity.
CC Glutamylates also related SdeB, SdeC and SidE (PubMed:31330531,
CC PubMed:31123136). Glutamylase activity only occurs in the host since it
CC requires host calmodulin (PubMed:28497808, PubMed:31330532,
CC PubMed:31330531, PubMed:31123136). May also reverse the SdeA-mediated
CC substrate ubiquitination by cleaving the phosphodiester bond that links
CC phosphoribosylated ubiquitin to protein substrates via its
CC deubiquitinase activity (PubMed:28497808).
CC {ECO:0000269|PubMed:28497808, ECO:0000269|PubMed:31123136,
CC ECO:0000269|PubMed:31330531, ECO:0000269|PubMed:31330532}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-glutamate + L-glutamyl-[protein] = ADP + gamma-L-
CC glutamyl-L-glutamyl-[protein] + H(+) + phosphate;
CC Xref=Rhea:RHEA:60144, Rhea:RHEA-COMP:10208, Rhea:RHEA-COMP:15517,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29973, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:143622,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:31123136,
CC ECO:0000269|PubMed:31330531, ECO:0000269|PubMed:31330532};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(L-glutamyl)(n)-gamma-L-glutamyl-L-glutamyl-[protein] + ATP +
CC L-glutamate = (L-glutamyl)(n+1)-gamma-L-glutamyl-L-glutamyl-[protein]
CC + ADP + H(+) + phosphate; Xref=Rhea:RHEA:60148, Rhea:RHEA-COMP:15519,
CC Rhea:RHEA-COMP:15675, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:143623,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:31123136,
CC ECO:0000269|PubMed:31330531, ECO:0000269|PubMed:31330532};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:31123136};
CC -!- ACTIVITY REGULATION: Glytamylation catalyzed by SidJ requires host
CC calmodulin and can be regulated by intracellular changes in Ca2+
CC concentrations. Requires also ATP. {ECO:0000269|PubMed:31123136,
CC ECO:0000269|PubMed:31330531}.
CC -!- SUBUNIT: Interacts with host calmodulin/CALM1; this interaction is
CC required for glutamylase activity. {ECO:0000269|PubMed:31123136,
CC ECO:0000269|PubMed:31330531, ECO:0000269|PubMed:31330532}.
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DR EMBL; AE017354; AAU28221.1; -; Genomic_DNA.
DR RefSeq; WP_010947866.1; NC_002942.5.
DR RefSeq; YP_096168.1; NC_002942.5.
DR PDB; 6K4K; X-ray; 2.71 A; A/B=1-873.
DR PDB; 6K4L; X-ray; 2.95 A; A/B=1-873.
DR PDB; 6K4R; X-ray; 3.11 A; A/B=1-873.
DR PDB; 6OQQ; X-ray; 2.10 A; A/C=1-873.
DR PDB; 6PLM; X-ray; 2.59 A; A/B=97-853.
DR PDB; 6S5T; EM; 4.15 A; A=1-873.
DR PDB; 7MIR; EM; 2.50 A; A=97-851.
DR PDB; 7MIS; EM; 2.80 A; A=97-851.
DR PDB; 7PPO; EM; 2.91 A; C=99-873.
DR PDB; 7PQE; EM; 3.70 A; C=99-873.
DR PDBsum; 6K4K; -.
DR PDBsum; 6K4L; -.
DR PDBsum; 6K4R; -.
DR PDBsum; 6OQQ; -.
DR PDBsum; 6PLM; -.
DR PDBsum; 6S5T; -.
DR PDBsum; 7MIR; -.
DR PDBsum; 7MIS; -.
DR PDBsum; 7PPO; -.
DR PDBsum; 7PQE; -.
DR AlphaFoldDB; Q5ZTK6; -.
DR SMR; Q5ZTK6; -.
DR STRING; 272624.lpg2155; -.
DR PaxDb; Q5ZTK6; -.
DR EnsemblBacteria; AAU28221; AAU28221; lpg2155.
DR GeneID; 66491285; -.
DR KEGG; lpn:lpg2155; -.
DR PATRIC; fig|272624.6.peg.2262; -.
DR eggNOG; COG1413; Bacteria.
DR HOGENOM; CLU_349104_0_0_6; -.
DR OMA; SSEHHYK; -.
DR Proteomes; UP000000609; Chromosome.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Ligase; Magnesium; Metal-binding;
KW Multifunctional enzyme; NAD; Nucleotide-binding; Protease;
KW Reference proteome; Thiol protease; Transferase; Virulence.
FT CHAIN 1..873
FT /note="Calmodulin-dependent glutamylase SidJ"
FT /id="PRO_0000448404"
FT REGION 16..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 851..873
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 542
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:31123136,
FT ECO:0007744|PDB:6OQQ"
FT BINDING 545
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:31123136,
FT ECO:0007744|PDB:6OQQ"
FT MUTAGEN 841
FT /note="I->A: Complete loss of interaction with host
FT calmodulin; in association with A-842."
FT /evidence="ECO:0000269|PubMed:31330532"
FT MUTAGEN 842
FT /note="Q->A: Complete loss of interaction with host
FT calmodulin; in association with A-841."
FT /evidence="ECO:0000269|PubMed:31330532"
FT STRAND 104..109
FT /evidence="ECO:0007829|PDB:6OQQ"
FT STRAND 120..124
FT /evidence="ECO:0007829|PDB:6OQQ"
FT STRAND 127..133
FT /evidence="ECO:0007829|PDB:6OQQ"
FT HELIX 136..157
FT /evidence="ECO:0007829|PDB:6OQQ"
FT HELIX 159..162
FT /evidence="ECO:0007829|PDB:6OQQ"
FT HELIX 165..181
FT /evidence="ECO:0007829|PDB:6OQQ"
FT HELIX 185..205
FT /evidence="ECO:0007829|PDB:6OQQ"
FT HELIX 207..217
FT /evidence="ECO:0007829|PDB:6OQQ"
FT HELIX 223..227
FT /evidence="ECO:0007829|PDB:6OQQ"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:7PPO"
FT HELIX 231..234
FT /evidence="ECO:0007829|PDB:6OQQ"
FT HELIX 237..245
FT /evidence="ECO:0007829|PDB:6OQQ"
FT HELIX 252..260
FT /evidence="ECO:0007829|PDB:6OQQ"
FT TURN 261..263
FT /evidence="ECO:0007829|PDB:6OQQ"
FT HELIX 265..268
FT /evidence="ECO:0007829|PDB:6OQQ"
FT HELIX 271..280
FT /evidence="ECO:0007829|PDB:6OQQ"
FT STRAND 283..285
FT /evidence="ECO:0007829|PDB:6K4L"
FT STRAND 290..294
FT /evidence="ECO:0007829|PDB:6OQQ"
FT STRAND 297..300
FT /evidence="ECO:0007829|PDB:6OQQ"
FT HELIX 302..310
FT /evidence="ECO:0007829|PDB:6OQQ"
FT STRAND 316..320
FT /evidence="ECO:0007829|PDB:6OQQ"
FT TURN 325..327
FT /evidence="ECO:0007829|PDB:6OQQ"
FT TURN 343..345
FT /evidence="ECO:0007829|PDB:6OQQ"
FT STRAND 346..350
FT /evidence="ECO:0007829|PDB:6OQQ"
FT STRAND 353..357
FT /evidence="ECO:0007829|PDB:6OQQ"
FT STRAND 361..368
FT /evidence="ECO:0007829|PDB:6OQQ"
FT STRAND 370..372
FT /evidence="ECO:0007829|PDB:7MIR"
FT HELIX 375..390
FT /evidence="ECO:0007829|PDB:6OQQ"
FT HELIX 392..395
FT /evidence="ECO:0007829|PDB:6OQQ"
FT STRAND 403..411
FT /evidence="ECO:0007829|PDB:6OQQ"
FT HELIX 412..419
FT /evidence="ECO:0007829|PDB:6OQQ"
FT STRAND 420..422
FT /evidence="ECO:0007829|PDB:6K4K"
FT HELIX 425..431
FT /evidence="ECO:0007829|PDB:6OQQ"
FT STRAND 434..445
FT /evidence="ECO:0007829|PDB:6OQQ"
FT HELIX 447..450
FT /evidence="ECO:0007829|PDB:6OQQ"
FT STRAND 456..458
FT /evidence="ECO:0007829|PDB:6K4L"
FT HELIX 460..479
FT /evidence="ECO:0007829|PDB:6OQQ"
FT STRAND 491..494
FT /evidence="ECO:0007829|PDB:6PLM"
FT HELIX 497..499
FT /evidence="ECO:0007829|PDB:6OQQ"
FT TURN 501..504
FT /evidence="ECO:0007829|PDB:6OQQ"
FT HELIX 510..513
FT /evidence="ECO:0007829|PDB:6OQQ"
FT STRAND 514..516
FT /evidence="ECO:0007829|PDB:7MIR"
FT STRAND 523..525
FT /evidence="ECO:0007829|PDB:6PLM"
FT HELIX 526..529
FT /evidence="ECO:0007829|PDB:6OQQ"
FT TURN 530..532
FT /evidence="ECO:0007829|PDB:6OQQ"
FT STRAND 534..536
FT /evidence="ECO:0007829|PDB:6OQQ"
FT HELIX 549..552
FT /evidence="ECO:0007829|PDB:6OQQ"
FT TURN 553..555
FT /evidence="ECO:0007829|PDB:6OQQ"
FT HELIX 557..562
FT /evidence="ECO:0007829|PDB:6OQQ"
FT HELIX 564..568
FT /evidence="ECO:0007829|PDB:6OQQ"
FT HELIX 573..575
FT /evidence="ECO:0007829|PDB:6OQQ"
FT TURN 578..581
FT /evidence="ECO:0007829|PDB:6OQQ"
FT STRAND 582..586
FT /evidence="ECO:0007829|PDB:6OQQ"
FT HELIX 587..592
FT /evidence="ECO:0007829|PDB:6OQQ"
FT HELIX 594..623
FT /evidence="ECO:0007829|PDB:6OQQ"
FT HELIX 628..654
FT /evidence="ECO:0007829|PDB:6OQQ"
FT HELIX 658..668
FT /evidence="ECO:0007829|PDB:6OQQ"
FT HELIX 671..681
FT /evidence="ECO:0007829|PDB:6OQQ"
FT STRAND 682..684
FT /evidence="ECO:0007829|PDB:6OQQ"
FT HELIX 685..688
FT /evidence="ECO:0007829|PDB:6OQQ"
FT HELIX 691..702
FT /evidence="ECO:0007829|PDB:6OQQ"
FT STRAND 703..705
FT /evidence="ECO:0007829|PDB:6K4K"
FT TURN 716..718
FT /evidence="ECO:0007829|PDB:6OQQ"
FT STRAND 722..726
FT /evidence="ECO:0007829|PDB:6OQQ"
FT HELIX 739..774
FT /evidence="ECO:0007829|PDB:6OQQ"
FT STRAND 775..777
FT /evidence="ECO:0007829|PDB:6OQQ"
FT HELIX 781..793
FT /evidence="ECO:0007829|PDB:6OQQ"
FT HELIX 800..816
FT /evidence="ECO:0007829|PDB:6OQQ"
FT TURN 823..825
FT /evidence="ECO:0007829|PDB:6OQQ"
FT HELIX 826..845
FT /evidence="ECO:0007829|PDB:6OQQ"
SQ SEQUENCE 873 AA; 100201 MW; 8D9CDEEA5ADA679C CRC64;
MFGFIKKVLD FFGVDQSEDN PSETAVETTD VSTKIKTTDT TQEESSVKTK TVVPTQPGGS
VKPETIAPDQ QKKHQIKTET TTSTTKQKGP KVTLMDGHVK QYYFARRGET STHDTSLPPP
VKVLSGRSIP LKEIPFEATR NELVQIYLTS IDKLIKSNKL NSIPSQQIAS HYLFLRSLAN
SETDGIKKNQ ILSLAKPLGT YLASKEPHVW KMINELIEKS EYPIIHYLKN NRAHSNFMLA
LIHEYHKEPL TKNQSAFVQK FRDSSVFLFP NPIYTAWLAH SYDEDSSFNP MFRERLSTNF
YHSTLTDNLL LRTEPKEVTL SSEHHYKKEK GPIDSSFRYQ MSSDRLLRIQ GRTLLFSTPQ
NDVVAVKVQK KGEPKSTLEE EFEMADYLLK HQRRLDVHSK LPQPLGQYSV KKSEILEISR
GSLDFERFKT LIDDSKDLEV YVYKAPQSYF TYLHDKNQDL EDLTASVKTN VHDLFVLLRE
GIVFPQLADI FHTHFGEDER EDKGRYQALV QLLNVLQFQL GRIDKWQKAV EYVNLRSSGL
ADLGDSLPIT SLFTSSDFTK HYFSELLTGG YHPTFFDKSS GTANSLFTGK RRLFGNYLYL
NTIAEYLLVI QLTLGSYGDK VTRDMMDKPK KEAVWRELAN VMFTSCAEAI HIMTGIPQSR
ALTLLKQRAN IEKHFRQTQF WMTPDYSKLD EDTLQMEQYS IYSGEPEYEF TDKLVSGVGL
SVDGVHQDLG GYNRESPLRE LEKLLYATVT LIEGTMQLDK EFFKQLEQVE KILSGEIKTD
ANSCFEAVAQ LLDLARPGCH FQKRLVLSYY EEAKLKYPSA PTDAYDSRFQ VVARTNAAIT
IQRFWREARK NLSEKSDIDS EKPESERTTD KRL
