CHEB2_RHORT
ID CHEB2_RHORT Reviewed; 363 AA.
AC Q2RUI8;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 25-MAY-2022, entry version 98.
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}; OrderedLocusNames=Rru_A1406;
OS Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 /
OS NCIMB 8255 / S1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Rhodospirillum.
OX NCBI_TaxID=269796;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1;
RX PubMed=21886856; DOI=10.4056/sigs.1804360;
RA Munk A.C., Copeland A., Lucas S., Lapidus A., Del Rio T.G., Barry K.,
RA Detter J.C., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Kyrpides N.C.,
RA Mavromatis K., Richardson P., Rohde M., Goeker M., Klenk H.P., Zhang Y.,
RA Roberts G.P., Reslewic S., Schwartz D.C.;
RT "Complete genome sequence of Rhodospirillum rubrum type strain (S1).";
RL Stand. Genomic Sci. 4:293-302(2011).
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 -!- SIMILARITY: Belongs to the CheB family. {ECO:0000255|HAMAP-
CC Rule:MF_00099}.
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DR EMBL; CP000230; ABC22207.1; -; Genomic_DNA.
DR RefSeq; WP_011389160.1; NC_007643.1.
DR RefSeq; YP_426494.1; NC_007643.1.
DR AlphaFoldDB; Q2RUI8; -.
DR SMR; Q2RUI8; -.
DR STRING; 269796.Rru_A1406; -.
DR PRIDE; Q2RUI8; -.
DR EnsemblBacteria; ABC22207; ABC22207; Rru_A1406.
DR KEGG; rru:Rru_A1406; -.
DR PATRIC; fig|269796.9.peg.1476; -.
DR eggNOG; COG2201; Bacteria.
DR HOGENOM; CLU_000445_51_0_5; -.
DR OMA; HAMAQTT; -.
DR OrthoDB; 1655418at2; -.
DR PhylomeDB; Q2RUI8; -.
DR Proteomes; UP000001929; 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 3: Inferred from homology;
KW Chemotaxis; Cytoplasm; Hydrolase; Phosphoprotein; Reference proteome.
FT CHAIN 1..363
FT /note="Protein-glutamate methylesterase/protein-glutamine
FT glutaminase 2"
FT /id="PRO_0000264312"
FT DOMAIN 6..123
FT /note="Response regulatory"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT DOMAIN 172..363
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT ACT_SITE 184
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT ACT_SITE 210
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT ACT_SITE 306
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT MOD_RES 57
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
SQ SEQUENCE 363 AA; 38944 MW; 6BD2BCB0C2FE4D05 CRC64;
MPRKIRVLIV DDSASVRQTM TEILESDPGI EVIGTAPDPY VAARRIQQEV PDVITLDVEM
PRMDGITFLR KIMAQRPIPV VVCSSLTETD SETASQAWEA GAVEIILKPR VGTAQFLLES
KIHICDVVKA AAGARLRSMP AAGRANRPRV PEKKLTADAV LPPPVAGRNA MARTTESVIC
IGASTGGTES LREVLEALPA ASPAIVIVQH MPEKFTEAFA RRLDSLCDME VKEAVDGDTV
MRGRVLIAPG NHHMLLQRSG ARYYVSVKDG PLVSRHRPSV DVLFRSAASH AGSNAVGIIM
TGMGDDGARG LLEMRKAGAY TIAQDEATSV VFGMPKEAIA LGAADKILPL EMLAMEILRA
GNR
