CHEB1_DESVH
ID CHEB1_DESVH Reviewed; 357 AA.
AC P62636;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 102.
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}; OrderedLocusNames=DVU_1596;
OS Desulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / NCIMB 8303 / VKM
OS B-1760 / Hildenborough).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Desulfovibrio.
OX NCBI_TaxID=882;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29579 / DSM 644 / NCIMB 8303 / VKM B-1760 / Hildenborough;
RX PubMed=15077118; DOI=10.1038/nbt959;
RA Heidelberg J.F., Seshadri R., Haveman S.A., Hemme C.L., Paulsen I.T.,
RA Kolonay J.F., Eisen J.A., Ward N.L., Methe B.A., Brinkac L.M.,
RA Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R.,
RA Nelson W.C., Sullivan S.A., Fouts D.E., Haft D.H., Selengut J.,
RA Peterson J.D., Davidsen T.M., Zafar N., Zhou L., Radune D., Dimitrov G.,
RA Hance M., Tran K., Khouri H.M., Gill J., Utterback T.R., Feldblyum T.V.,
RA Wall J.D., Voordouw G., Fraser C.M.;
RT "The genome sequence of the anaerobic, sulfate-reducing bacterium
RT Desulfovibrio vulgaris Hildenborough.";
RL Nat. Biotechnol. 22:554-559(2004).
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; AE017285; AAS96074.1; -; Genomic_DNA.
DR RefSeq; WP_010938887.1; NZ_CABHLV010000001.1.
DR RefSeq; YP_010815.1; NC_002937.3.
DR AlphaFoldDB; P62636; -.
DR SMR; P62636; -.
DR IntAct; P62636; 1.
DR STRING; 882.DVU_1596; -.
DR PaxDb; P62636; -.
DR EnsemblBacteria; AAS96074; AAS96074; DVU_1596.
DR KEGG; dvu:DVU_1596; -.
DR PATRIC; fig|882.5.peg.1471; -.
DR eggNOG; COG2201; Bacteria.
DR HOGENOM; CLU_000445_51_0_7; -.
DR OMA; HAMAQTT; -.
DR PhylomeDB; P62636; -.
DR Proteomes; UP000002194; 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..357
FT /note="Protein-glutamate methylesterase/protein-glutamine
FT glutaminase 1"
FT /id="PRO_0000157990"
FT DOMAIN 6..123
FT /note="Response regulatory"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT DOMAIN 165..351
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT ACT_SITE 177
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT ACT_SITE 203
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT ACT_SITE 299
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 357 AA; 38232 MW; 44DD7F9E15B22AD5 CRC64;
MARPCRVLIV DDSALVRQTL ADLLSADPGI EVVGTASDPF VAAKRMEAVV PDVILLDIEM
PRMDGLTFLR KIMTQHPLPV VICSSVTEQG AEATFKAMEY GAVEVITKPR LGTKRFLEES
SIRICDAVKA AARARLHRLG HRTRDVAPKL TADAMLPGPT NFTRVQTTEK VVVVGASTGG
TEALQVFLEA MPPDAPPIAI VQHMPEHFTG AFSRRLDGIC RIRVREAEDG DIMARGQALI
APGSSHMLLK RNGSRYTVEV KDGPLVRRHR PSVDVLFRSA ARYAGANAVA AILTGMGDDG
AAGMKELHDM GAHTIAQDEA TCIVFGMPHE AIRLGGVDRV LPLDAIAPAV LKACAGS
