CHEB2_PSEAE
ID CHEB2_PSEAE Reviewed; 349 AA.
AC Q9I6V9;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Protein-glutamate methylesterase/protein-glutamine glutaminase 2 {ECO:0000255|HAMAP-Rule:MF_00099};
DE EC=3.1.1.61 {ECO:0000255|HAMAP-Rule:MF_00099};
DE EC=3.5.1.44 {ECO:0000255|HAMAP-Rule:MF_00099};
GN Name=cheB2 {ECO:0000255|HAMAP-Rule:MF_00099, ECO:0000303|PubMed:12142407};
GN OrderedLocusNames=PA0173;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2]
RP FUNCTION IN CHEMOTAXIS, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=12142407; DOI=10.1128/jb.184.16.4374-4383.2002;
RA Ferrandez A., Hawkins A.C., Summerfield D.T., Harwood C.S.;
RT "Cluster II che genes from Pseudomonas aeruginosa are required for an
RT optimal chemotactic response.";
RL J. Bacteriol. 184:4374-4383(2002).
RN [3]
RP FUNCTION IN VIRULENCE, AND DISRUPTION PHENOTYPE.
RC STRAIN=TBCF10839;
RX PubMed=19662168; DOI=10.1371/journal.ppat.1000540;
RA Garvis S., Munder A., Ball G., de Bentzmann S., Wiehlmann L., Ewbank J.J.,
RA Tuemmler B., Filloux A.;
RT "Caenorhabditis elegans semi-automated liquid screen reveals a specialized
RT role for the chemotaxis gene cheB2 in Pseudomonas aeruginosa virulence.";
RL PLoS Pathog. 5:e1000540-e1000540(2009).
RN [4]
RP FUNCTION, INTERACTION WITH MCPB, AND MUTAGENESIS OF ASP-55.
RX PubMed=33187094; DOI=10.3390/ijms21228459;
RA Velando F., Gavira J.A., Rico-Jimenez M., Matilla M.A., Krell T.;
RT "Evidence for pentapeptide-dependent and independent CheB
RT methylesterases.";
RL Int. J. Mol. Sci. 21:0-0(2020).
CC -!- FUNCTION: Involved in chemotaxis. Part of a chemotaxis signal
CC transduction system that modulates chemotaxis in response to various
CC stimuli. Catalyzes the demethylation of specific methylglutamate
CC residues introduced into the chemoreceptors (methyl-accepting
CC chemotaxis proteins or MCP) by CheR. Also mediates the irreversible
CC deamidation of specific glutamine residues to glutamic acid (By
CC similarity) (PubMed:12142407). Acts on the methyl-accepting chemotaxis
CC protein McpB (Probable). May be involved in a specific chemotactic
CC response, which takes place during infection and is required for
CC P.aeruginosa pathogenicity (PubMed:19662168). {ECO:0000255|HAMAP-
CC Rule:MF_00099, ECO:0000269|PubMed:12142407,
CC ECO:0000269|PubMed:19662168, ECO:0000305|PubMed:33187094}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-L-glutamate 5-O-methyl ester + H2O = H(+) + L-
CC glutamyl-[protein] + methanol; Xref=Rhea:RHEA:23236, Rhea:RHEA-
CC COMP:10208, Rhea:RHEA-COMP:10311, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17790, ChEBI:CHEBI:29973,
CC ChEBI:CHEBI:82795; EC=3.1.1.61; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00099};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+);
CC Xref=Rhea:RHEA:16441, Rhea:RHEA-COMP:10207, Rhea:RHEA-COMP:10208,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:29973,
CC ChEBI:CHEBI:30011; EC=3.5.1.44; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00099};
CC -!- SUBUNIT: Interacts with the C-terminal pentapeptide GWEEF of McpB.
CC {ECO:0000269|PubMed:33187094}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00099}.
CC -!- DOMAIN: Contains a C-terminal catalytic domain, and an N-terminal
CC region which modulates catalytic activity. {ECO:0000255|HAMAP-
CC Rule:MF_00099}.
CC -!- PTM: Phosphorylated by CheA. Phosphorylation of the N-terminal
CC regulatory domain activates the methylesterase activity.
CC {ECO:0000255|HAMAP-Rule:MF_00099}.
CC -!- DISRUPTION PHENOTYPE: Mutant is defective in chemotaxis, but does not
CC have an obvious defect in swimming behavior (PubMed:12142407). Mutant
CC shows strongly reduced adherence to a biological surface such as the
CC human epithelial cell line, and a reduction in swimming motility
CC (PubMed:19662168). Also shows a highly attenuated virulence in
CC C.elegans and in a murine lung infection model, and fails to induce
CC strong inflammatory response in the infected mice lungs
CC (PubMed:19662168). {ECO:0000269|PubMed:12142407,
CC ECO:0000269|PubMed:19662168}.
CC -!- MISCELLANEOUS: This protein is able to restore chemotaxis to a
CC completely non-chemotactic CheB1 mutant to near wild-type levels.
CC {ECO:0000269|PubMed:12142407}.
CC -!- SIMILARITY: Belongs to the CheB family. {ECO:0000255|HAMAP-
CC Rule:MF_00099}.
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DR EMBL; AE004091; AAG03563.1; -; Genomic_DNA.
DR PIR; F83623; F83623.
DR RefSeq; NP_248863.1; NC_002516.2.
DR RefSeq; WP_003083922.1; NZ_QZGE01000015.1.
DR AlphaFoldDB; Q9I6V9; -.
DR SMR; Q9I6V9; -.
DR STRING; 287.DR97_3129; -.
DR PaxDb; Q9I6V9; -.
DR PRIDE; Q9I6V9; -.
DR EnsemblBacteria; AAG03563; AAG03563; PA0173.
DR GeneID; 882256; -.
DR KEGG; pae:PA0173; -.
DR PATRIC; fig|208964.12.peg.179; -.
DR PseudoCAP; PA0173; -.
DR HOGENOM; CLU_000445_51_0_6; -.
DR InParanoid; Q9I6V9; -.
DR OMA; MLEMHRA; -.
DR PhylomeDB; Q9I6V9; -.
DR BioCyc; PAER208964:G1FZ6-174-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000156; F:phosphorelay response regulator activity; IEA:InterPro.
DR GO; GO:0008984; F:protein-glutamate methylesterase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0050568; F:protein-glutamine glutaminase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-UniRule.
DR GO; GO:0018277; P:protein deamination; IEA:UniProtKB-UniRule.
DR GO; GO:0006482; P:protein demethylation; IEA:UniProtKB-UniRule.
DR CDD; cd16432; CheB_Rec; 1.
DR Gene3D; 3.40.50.180; -; 1.
DR HAMAP; MF_00099; CheB_chemtxs; 1.
DR InterPro; IPR008248; CheB-like.
DR InterPro; IPR035909; CheB_C.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR000673; Sig_transdc_resp-reg_Me-estase.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR Pfam; PF01339; CheB_methylest; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PIRSF; PIRSF000876; RR_chemtxs_CheB; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF52172; SSF52172; 1.
DR SUPFAM; SSF52738; SSF52738; 1.
DR PROSITE; PS50122; CHEB; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 1: Evidence at protein level;
KW Chemotaxis; Cytoplasm; Hydrolase; Phosphoprotein; Reference proteome.
FT CHAIN 1..349
FT /note="Protein-glutamate methylesterase/protein-glutamine
FT glutaminase 2"
FT /id="PRO_0000158009"
FT DOMAIN 4..121
FT /note="Response regulatory"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT DOMAIN 151..343
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT ACT_SITE 163
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT ACT_SITE 189
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT ACT_SITE 285
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT MOD_RES 55
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT MUTAGEN 55
FT /note="D->E: Mimics phosphorylation. Shows a slight
FT increase in affinity for McpB."
FT /evidence="ECO:0000269|PubMed:33187094"
SQ SEQUENCE 349 AA; 37347 MW; 0DA7F70AF44A4F7C CRC64;
MPISVLVVDD SALIRSLLKE IIQADPELRL VGCAPDAFVA RDLIKQHAPD VISLDVEMPR
MDGLTFLDKL MKARPTPVLM ISSLTERGSE ATLRALELGA VDFIAKPRLG IAEGMQAYAE
EIRAKLKTVA RARLRRRAAD APAPPESAAP LLSTEKIIAL GASTGGTEAL KEVLLGLPAH
SPGVVITQHM PPGFTRSFAE RLDRLTRLSV SEARDGDRIL PGHALVAPGD HHMEVQRSGA
NYVVRLNRQA QVNGHRPAVD VMFESLARCA GRNLLAGLLT GMGKDGARGL LAIRQAGGYT
LAQDEATCVV YGMPREAVEL GAAEDVLPLE RIAAALLQQA ARRGSGNRL
