CHEB_SALRD
ID CHEB_SALRD Reviewed; 366 AA.
AC Q2RZD2;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 2.
DT 25-MAY-2022, entry version 103.
DE RecName: Full=Protein-glutamate methylesterase/protein-glutamine glutaminase {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=cheB {ECO:0000255|HAMAP-Rule:MF_00099}; OrderedLocusNames=SRU_2601;
OS Salinibacter ruber (strain DSM 13855 / M31).
OC Bacteria; Bacteroidetes; Bacteroidetes Order II. Incertae sedis;
OC Rhodothermaceae; Salinibacter.
OX NCBI_TaxID=309807;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13855 / CECT 5946 / M31;
RX PubMed=16330755; DOI=10.1073/pnas.0509073102;
RA Mongodin E.F., Nelson K.E., Daugherty S., DeBoy R.T., Wister J., Khouri H.,
RA Weidman J., Walsh D.A., Papke R.T., Sanchez Perez G., Sharma A.K.,
RA Nesbo C.L., MacLeod D., Bapteste E., Doolittle W.F., Charlebois R.L.,
RA Legault B., Rodriguez-Valera F.;
RT "The genome of Salinibacter ruber: convergence and gene exchange among
RT hyperhalophilic bacteria and archaea.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:18147-18152(2005).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABC44192.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000159; ABC44192.1; ALT_INIT; Genomic_DNA.
DR RefSeq; YP_446699.1; NC_007677.1.
DR AlphaFoldDB; Q2RZD2; -.
DR SMR; Q2RZD2; -.
DR STRING; 309807.SRU_2601; -.
DR EnsemblBacteria; ABC44192; ABC44192; SRU_2601.
DR KEGG; sru:SRU_2601; -.
DR PATRIC; fig|309807.25.peg.2711; -.
DR eggNOG; COG2201; Bacteria.
DR HOGENOM; CLU_000445_51_0_10; -.
DR Proteomes; UP000008674; 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..366
FT /note="Protein-glutamate methylesterase/protein-glutamine
FT glutaminase"
FT /id="PRO_0000264317"
FT DOMAIN 3..120
FT /note="Response regulatory"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT DOMAIN 170..363
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT REGION 134..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 182
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT ACT_SITE 209
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT ACT_SITE 305
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT MOD_RES 54
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
SQ SEQUENCE 366 AA; 38526 MW; 31BE9CAA52333052 CRC64;
MIRVLVVDDS LVMRKAISRI FEQADDTTVV DTATNGEAGV EKARRLEPDV VTMDVEMPKM
NGIEAVRHIM EASPRPILML SSLTEKGAEV TMEAMRAGAA DFLSKGASSA TLRANDVEEK
LLGKVRALAD SNARLFREDG PSPAETVSST GSREASSSSS PTSSGTDTAT KGSYELAVIG
VSTGGPMALQ HVIPALPAAF PLPIAIVQHM PAQFTRSLAD RLDSLSELAV AEAEDGMLLE
PGRVVVAAGD RHLTVERREG ALTTCTPAEP AGDSHRPSVN VLFRSAVEAC REDVLTLVMT
GMGKDGLEGA RRIQDDGGTV YVQDEDTSVV YGMPRAVAEA GLADATFPLD DLPDAMQKAA
GAPARP
