CHEB1_PSEAE
ID CHEB1_PSEAE Reviewed; 368 AA.
AC O87125;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 08-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Protein-glutamate methylesterase/protein-glutamine glutaminase 1 {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=cheB1 {ECO:0000255|HAMAP-Rule:MF_00099};
GN Synonyms=cheB {ECO:0000303|PubMed:12142407}; OrderedLocusNames=PA1459;
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 [GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10052136; DOI=10.1271/bbb.63.155;
RA Kato J., Nakamura T., Kuroda A., Ohtake H.;
RT "Cloning and characterization of chemotaxis genes in Pseudomonas
RT aeruginosa.";
RL Biosci. Biotechnol. Biochem. 63:155-161(1999).
RN [2]
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 [3]
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 [4]
RP 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).
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.
CC {ECO:0000255|HAMAP-Rule:MF_00099}.
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 -!- 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: Deletion mutant is nonchemotactic
CC (PubMed:12142407). Mutant is not attenuated for virulence in C.elegans
CC whereas in vitro motility and chemotaxis are severely impaired
CC (PubMed:19662168). {ECO:0000269|PubMed:12142407,
CC ECO:0000269|PubMed:19662168}.
CC -!- SIMILARITY: Belongs to the CheB family. {ECO:0000255|HAMAP-
CC Rule:MF_00099}.
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DR EMBL; AB012767; BAA33550.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG04848.1; -; Genomic_DNA.
DR PIR; G83463; G83463.
DR PIR; T46615; T46615.
DR RefSeq; NP_250150.1; NC_002516.2.
DR RefSeq; WP_010895569.1; NZ_CP053028.1.
DR AlphaFoldDB; O87125; -.
DR SMR; O87125; -.
DR STRING; 287.DR97_564; -.
DR PaxDb; O87125; -.
DR PRIDE; O87125; -.
DR DNASU; 882084; -.
DR EnsemblBacteria; AAG04848; AAG04848; PA1459.
DR GeneID; 882084; -.
DR KEGG; pae:PA1459; -.
DR PATRIC; fig|208964.12.peg.1510; -.
DR PseudoCAP; PA1459; -.
DR HOGENOM; CLU_000445_51_0_6; -.
DR InParanoid; O87125; -.
DR OMA; YGMPMAV; -.
DR PhylomeDB; O87125; -.
DR BioCyc; PAER208964:G1FZ6-1485-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..368
FT /note="Protein-glutamate methylesterase/protein-glutamine
FT glutaminase 1"
FT /id="PRO_0000158008"
FT DOMAIN 4..121
FT /note="Response regulatory"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT DOMAIN 172..368
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT REGION 138..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 192
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT ACT_SITE 219
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT ACT_SITE 312
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 CONFLICT 34
FT /note="G -> A (in Ref. 1; BAA33550)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 368 AA; 39004 MW; FE4801DC220C613B CRC64;
MAVKVLVVDD SGFFRRRVSE ILSADGQIQV VGTGTNGREA IEQALALRPD VITMDYEMPL
MDGITAVRNI MQRCPTPVLM FSSLTHEGAR VTLDALDAGA VDYLPKNFED ISRNPDKVRQ
LLCEKVLTIA RSNRRSISLP PLPSATSSSH APASSSSVGA SARVGAGASP APASTSAAPK
RKAYRLVAIG TSTGGPVALQ RVLTQLPANF PAPLVLIQHM PAAFTKAFAE RLDKLCRINV
KEAEDGDILR PGLALLAPGG KQMMVDGRGT VRILPGDERL NYKPCVDVTF GSAAKAYNDK
VLAVVLTGMG ADGREGARLL KQGGSQVWAQ DEASCVIYGM PMAVVKANLA DAVYGLDDIG
RHLVEACQ
