SIDD_LEGPH
ID SIDD_LEGPH Reviewed; 507 AA.
AC Q5ZSQ2;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Adenosine monophosphate-protein hydrolase SidD;
DE Short=De-AMPylase SidD;
DE Short=DeAMPylase SidD;
DE EC=3.1.4.-;
DE AltName: Full=Adenylyl-[Rab1] hydrolase;
GN Name=sidD; OrderedLocusNames=lpg2465;
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 3D-STRUCTURE MODELING, AND POSSIBLE METAL-BINDING.
RX PubMed=21843523; DOI=10.1016/j.febslet.2011.08.006;
RA Rigden D.J.;
RT "Identification and modelling of a PPM protein phosphatase fold in the
RT Legionella pneumophila deAMPylase SidD.";
RL FEBS Lett. 585:2749-2754(2011).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF ASP-60; ASP-92 AND
RP ASP-110.
RX PubMed=21734656; DOI=10.1038/nature10307;
RA Tan Y., Luo Z.Q.;
RT "Legionella pneumophila SidD is a deAMPylase that modifies Rab1.";
RL Nature 475:506-509(2011).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=21680813; DOI=10.1126/science.1207193;
RA Neunuebel M.R., Chen Y., Gaspar A.H., Backlund P.S. Jr., Yergey A.,
RA Machner M.P.;
RT "De-AMPylation of the small GTPase Rab1 by the pathogen Legionella
RT pneumophila.";
RL Science 333:453-456(2011).
RN [5]
RP FUNCTION.
RX PubMed=22228731; DOI=10.1128/jb.06306-11;
RA Neunuebel M.R., Mohammadi S., Jarnik M., Machner M.P.;
RT "Legionella pneumophila LidA affects nucleotide binding and activity of the
RT host GTPase Rab1.";
RL J. Bacteriol. 194:1389-1400(2012).
CC -!- FUNCTION: Virulence effector that plays a role in hijacking the host
CC vesicular trafficking by recruiting the small guanosine triphosphatase
CC (GTPase) Rab1 to the cytosolic face of the Legionella-containing
CC vacuole (LCVs). Acts as an adenosine monophosphate-protein hydrolase
CC (de-AMPylase) by mediating the hydrolysis of adenosine 5'-monophosphate
CC (AMP) to 'Tyr-77' of host RAB1B, thereby releasing RAB1B from bacterial
CC phagosomes and rendering RAB1B accessible for inactivation by LepB. De-
CC AMPylation of RAB1B cannot take place when LidA is bound to RAB1B.
CC {ECO:0000269|PubMed:21680813, ECO:0000269|PubMed:21734656,
CC ECO:0000269|PubMed:22228731}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[Rab1 protein]-O(4)-(5'-adenylyl)-L-tyrosine + H2O = [Rab1
CC protein]-L-tyrosine + AMP + H(+); Xref=Rhea:RHEA:53740, Rhea:RHEA-
CC COMP:13638, Rhea:RHEA-COMP:13639, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:46858, ChEBI:CHEBI:83624,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:21680813,
CC ECO:0000269|PubMed:21734656};
CC -!- SUBCELLULAR LOCATION: Host cytoplasm, host perinuclear region
CC {ECO:0000269|PubMed:21680813}.
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DR EMBL; AE017354; AAU28525.1; -; Genomic_DNA.
DR RefSeq; WP_010948167.1; NC_002942.5.
DR RefSeq; YP_096472.1; NC_002942.5.
DR PDB; 4IIK; X-ray; 1.60 A; A=37-350.
DR PDB; 4IIP; X-ray; 1.90 A; A=37-350.
DR PDB; 6RP4; X-ray; 2.50 A; A/B/C/D=350-507.
DR PDB; 6RRE; X-ray; 3.59 A; A/B/C/D/E/F=37-507.
DR PDBsum; 4IIK; -.
DR PDBsum; 4IIP; -.
DR PDBsum; 6RP4; -.
DR PDBsum; 6RRE; -.
DR AlphaFoldDB; Q5ZSQ2; -.
DR SMR; Q5ZSQ2; -.
DR STRING; 272624.lpg2465; -.
DR PaxDb; Q5ZSQ2; -.
DR EnsemblBacteria; AAU28525; AAU28525; lpg2465.
DR KEGG; lpn:lpg2465; -.
DR PATRIC; fig|272624.6.peg.2614; -.
DR HOGENOM; CLU_537243_0_0_6; -.
DR OMA; HNDRISE; -.
DR Proteomes; UP000000609; Chromosome.
DR GO; GO:0044220; C:host cell perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0044603; F:protein adenylylhydrolase activity; IDA:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IDA:UniProtKB.
DR GO; GO:0018117; P:protein adenylylation; IDA:UniProtKB.
DR GO; GO:0044602; P:protein deadenylylation; IDA:UniProtKB.
DR GO; GO:0043087; P:regulation of GTPase activity; IDA:UniProtKB.
PE 1: Evidence at protein level;
KW 3D-structure; Host cytoplasm; Hydrolase; Metal-binding; Reference proteome;
KW Virulence.
FT CHAIN 1..507
FT /note="Adenosine monophosphate-protein hydrolase SidD"
FT /id="PRO_0000417547"
FT BINDING 92
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT BINDING 110
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT BINDING 192
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT BINDING 271
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT BINDING 326
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT MUTAGEN 60
FT /note="D->A: No effect."
FT /evidence="ECO:0000269|PubMed:21734656"
FT MUTAGEN 92
FT /note="D->A: Abolishes de-AMPylase activity."
FT /evidence="ECO:0000269|PubMed:21734656"
FT MUTAGEN 110
FT /note="D->A: Abolishes de-AMPylase activity."
FT /evidence="ECO:0000269|PubMed:21734656"
FT STRAND 39..46
FT /evidence="ECO:0007829|PDB:4IIK"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:4IIK"
FT STRAND 66..72
FT /evidence="ECO:0007829|PDB:4IIK"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:4IIK"
FT STRAND 92..98
FT /evidence="ECO:0007829|PDB:4IIK"
FT STRAND 104..112
FT /evidence="ECO:0007829|PDB:4IIK"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:4IIK"
FT HELIX 117..127
FT /evidence="ECO:0007829|PDB:4IIK"
FT HELIX 129..131
FT /evidence="ECO:0007829|PDB:4IIK"
FT HELIX 132..141
FT /evidence="ECO:0007829|PDB:4IIK"
FT HELIX 145..163
FT /evidence="ECO:0007829|PDB:4IIK"
FT STRAND 169..179
FT /evidence="ECO:0007829|PDB:4IIK"
FT STRAND 182..192
FT /evidence="ECO:0007829|PDB:4IIK"
FT STRAND 194..198
FT /evidence="ECO:0007829|PDB:4IIK"
FT STRAND 204..208
FT /evidence="ECO:0007829|PDB:4IIK"
FT STRAND 210..213
FT /evidence="ECO:0007829|PDB:4IIK"
FT HELIX 224..227
FT /evidence="ECO:0007829|PDB:4IIK"
FT HELIX 228..234
FT /evidence="ECO:0007829|PDB:4IIK"
FT STRAND 235..242
FT /evidence="ECO:0007829|PDB:4IIK"
FT STRAND 247..252
FT /evidence="ECO:0007829|PDB:4IIK"
FT HELIX 256..258
FT /evidence="ECO:0007829|PDB:4IIK"
FT STRAND 259..267
FT /evidence="ECO:0007829|PDB:4IIK"
FT STRAND 278..285
FT /evidence="ECO:0007829|PDB:4IIK"
FT HELIX 287..289
FT /evidence="ECO:0007829|PDB:4IIK"
FT STRAND 292..294
FT /evidence="ECO:0007829|PDB:4IIK"
FT HELIX 296..317
FT /evidence="ECO:0007829|PDB:4IIK"
FT STRAND 322..324
FT /evidence="ECO:0007829|PDB:4IIK"
FT STRAND 327..334
FT /evidence="ECO:0007829|PDB:4IIK"
FT HELIX 338..349
FT /evidence="ECO:0007829|PDB:4IIK"
FT HELIX 385..396
FT /evidence="ECO:0007829|PDB:6RP4"
FT HELIX 401..413
FT /evidence="ECO:0007829|PDB:6RP4"
FT HELIX 418..427
FT /evidence="ECO:0007829|PDB:6RP4"
FT HELIX 433..447
FT /evidence="ECO:0007829|PDB:6RP4"
FT STRAND 449..452
FT /evidence="ECO:0007829|PDB:6RP4"
FT HELIX 454..457
FT /evidence="ECO:0007829|PDB:6RP4"
FT HELIX 462..478
FT /evidence="ECO:0007829|PDB:6RP4"
FT HELIX 480..482
FT /evidence="ECO:0007829|PDB:6RP4"
FT HELIX 485..489
FT /evidence="ECO:0007829|PDB:6RP4"
FT HELIX 490..492
FT /evidence="ECO:0007829|PDB:6RP4"
SQ SEQUENCE 507 AA; 57147 MW; AC3E92E3C63F0DA3 CRC64;
MVYYEIIKDI VFTYNLQFTH LIHNDRISEV NLGGVTMRSI ITQICNGVLH GQSYQSGSND
LDKGNSEIFA SSLFVHLNEQ GKEIIKHKDS DDKIVIGYTK DGMAFQIVVD GFYGCERQAV
FSFIDNYVLP LIDNFSLDLT RYPDSKKVTE SLIHTIYSLR SKHAPLAEFT MSLCVTYQKD
EQLFCAGFGI GDTGIAIKRN EGTIEQLVCH TEVDGFKDAF DNYSSANIDL VIERNSVFNT
KVMPGDELVG YTYVPPMLEM TEKEFEVETV DGKKINKRIV RHLNLDPGNF DDKDPLFSQL
LQVVKSKQKQ LVEQAKETGQ IQRFGDDFTV GRLVIPDQLL INQLRIHALS IGVSDGLLSY
IKNENENKGF LGIYGFFTGA DKNIEKATLY KNLIAKYQNN HFISLIILSA LVSDSKTPLM
TQYLVGYLDF PSKALLANKI TELLLKELEN PDMREILGSR LATDVIEELE TKIIRYIHNP
AGSDIHSTLN LWTADKIKAA TNSSLTI
