CHEB_SALTY
ID CHEB_SALTY Reviewed; 349 AA.
AC P04042;
DT 01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1986, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Protein-glutamate methylesterase/protein-glutamine glutaminase {ECO:0000255|HAMAP-Rule:MF_00099, ECO:0000305};
DE EC=3.1.1.61 {ECO:0000255|HAMAP-Rule:MF_00099, ECO:0000269|PubMed:2677005, ECO:0000269|PubMed:2991277, ECO:0000269|PubMed:9760239};
DE EC=3.5.1.44 {ECO:0000250|UniProtKB:P07330, ECO:0000255|HAMAP-Rule:MF_00099};
GN Name=cheB {ECO:0000255|HAMAP-Rule:MF_00099}; OrderedLocusNames=STM1917;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, AND DOMAIN.
RX PubMed=2991277; DOI=10.1016/s0021-9258(17)39227-x;
RA Simms S.A., Keane M.G., Stock J.;
RT "Multiple forms of the CheB methylesterase in bacterial chemosensing.";
RL J. Biol. Chem. 260:10161-10168(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [3]
RP PROTEIN SEQUENCE OF 277-306, AND MUTAGENESIS OF CYS-207; GLY-284 AND
RP CYS-309.
RX PubMed=3539934; DOI=10.1016/s0021-9258(19)75880-3;
RA Simms S.A., Cornman E.W., Mottonen J., Stock J.;
RT "Active site of the enzyme which demethylates receptors during bacterial
RT chemotaxis.";
RL J. Biol. Chem. 262:29-31(1987).
RN [4]
RP PHOSPHORYLATION.
RX PubMed=3280143; DOI=10.1016/0092-8674(88)90489-8;
RA Hess J.F., Oosawa K., Kaplan N., Simon M.I.;
RT "Phosphorylation of three proteins in the signaling pathway of bacterial
RT chemotaxis.";
RL Cell 53:79-87(1988).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND PHOSPHORYLATION.
RX PubMed=2677005; DOI=10.1016/s0021-9258(18)71497-x;
RA Lupas A., Stock J.;
RT "Phosphorylation of an N-terminal regulatory domain activates the CheB
RT methylesterase in bacterial chemotaxis.";
RL J. Biol. Chem. 264:17337-17342(1989).
RN [6]
RP CHARACTERIZATION, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION,
RP DOMAIN, AND PHOSPHORYLATION.
RX PubMed=9760239; DOI=10.1021/bi980865d;
RA Anand G.S., Goudreau P.N., Stock A.M.;
RT "Activation of methylesterase CheB: evidence of a dual role for the
RT regulatory domain.";
RL Biochemistry 37:14038-14047(1998).
RN [7]
RP DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 14028 / SGSC 2980 / CDC 6516-60 / NCTC 12023;
RX PubMed=20346719; DOI=10.1016/j.molcel.2010.03.001;
RA Paul K., Nieto V., Carlquist W.C., Blair D.F., Harshey R.M.;
RT "The c-di-GMP binding protein YcgR controls flagellar motor direction and
RT speed to affect chemotaxis by a 'backstop brake' mechanism.";
RL Mol. Cell 38:128-139(2010).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 152-349, AND ACTIVE SITE.
RX PubMed=7608974; DOI=10.1006/jmbi.1995.0376;
RA West A.H., Martinez-Hackert E., Stock A.M.;
RT "Crystal structure of the catalytic domain of the chemotaxis receptor
RT methylesterase, CheB.";
RL J. Mol. Biol. 250:276-290(1995).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS), AND PHOSPHORYLATION AT ASP-56.
RX PubMed=9465023; DOI=10.1073/pnas.95.4.1381;
RA Djordjevic S., Goudreau P.N., Xu Q., Stock A.M., West A.H.;
RT "Structural basis for methylesterase CheB regulation by a phosphorylation-
RT activated domain.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:1381-1386(1998).
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 (PubMed:2991277, PubMed:2677005,
CC PubMed:9760239). Also mediates the irreversible deamidation of specific
CC glutamine residues to glutamic acid (By similarity).
CC {ECO:0000250|UniProtKB:P07330, ECO:0000269|PubMed:2677005,
CC ECO:0000269|PubMed:2991277, ECO:0000269|PubMed:9760239}.
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, ECO:0000269|PubMed:2677005,
CC ECO:0000269|PubMed:2991277, ECO:0000269|PubMed:9760239};
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;
CC Evidence={ECO:0000250|UniProtKB:P07330, ECO:0000255|HAMAP-
CC Rule:MF_00099};
CC -!- ACTIVITY REGULATION: Phosphorylation of the N-terminal regulatory
CC domain activates the methylesterase activity.
CC {ECO:0000269|PubMed:2677005, ECO:0000269|PubMed:9760239}.
CC -!- SUBUNIT: Interacts with CheA. {ECO:0000250|UniProtKB:P07330}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P07330,
CC ECO:0000255|HAMAP-Rule:MF_00099}.
CC -!- DOMAIN: Contains a C-terminal catalytic domain, and an N-terminal
CC region which modulates catalytic activity (PubMed:2991277,
CC PubMed:9760239). The N-terminal domain is not essential for catalysis
CC (PubMed:2991277). {ECO:0000269|PubMed:2991277,
CC ECO:0000269|PubMed:9760239}.
CC -!- PTM: Phosphorylated by CheA (PubMed:3280143, PubMed:2677005,
CC PubMed:9465023). Phosphorylation of the N-terminal regulatory domain
CC activates the methylesterase activity (PubMed:2677005, PubMed:9760239).
CC {ECO:0000269|PubMed:2677005, ECO:0000269|PubMed:3280143,
CC ECO:0000269|PubMed:9465023, ECO:0000269|PubMed:9760239}.
CC -!- PTM: Two forms were isolated, the intact protein and a proteolytic
CC fragment (147-349) that is 15-fold more active than its precursor.
CC {ECO:0000269|PubMed:2991277}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene display a strong
CC clockwise motor bias; in combination with a yhjH disruption cells
CC switch to a counterclockwise bias. {ECO:0000269|PubMed:20346719}.
CC -!- SIMILARITY: Belongs to the CheB family. {ECO:0000255|HAMAP-
CC Rule:MF_00099, ECO:0000305}.
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DR EMBL; AE006468; AAL20833.1; -; Genomic_DNA.
DR PIR; A00547; XYEBET.
DR RefSeq; NP_460874.1; NC_003197.2.
DR RefSeq; WP_000036392.1; NC_003197.2.
DR PDB; 1A2O; X-ray; 2.40 A; A/B=1-349.
DR PDB; 1CHD; X-ray; 1.75 A; A=147-349.
DR PDBsum; 1A2O; -.
DR PDBsum; 1CHD; -.
DR AlphaFoldDB; P04042; -.
DR SMR; P04042; -.
DR STRING; 99287.STM1917; -.
DR PaxDb; P04042; -.
DR EnsemblBacteria; AAL20833; AAL20833; STM1917.
DR GeneID; 1253438; -.
DR KEGG; stm:STM1917; -.
DR PATRIC; fig|99287.12.peg.2033; -.
DR HOGENOM; CLU_000445_51_0_6; -.
DR OMA; MLEMHRA; -.
DR PhylomeDB; P04042; -.
DR BioCyc; SENT99287:STM1917-MON; -.
DR EvolutionaryTrace; P04042; -.
DR PHI-base; PHI:6461; -.
DR Proteomes; UP000001014; 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 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 3D-structure; Chemotaxis; Cytoplasm; Direct protein sequencing; Hydrolase;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..349
FT /note="Protein-glutamate methylesterase/protein-glutamine
FT glutaminase"
FT /id="PRO_0000158027"
FT DOMAIN 5..122
FT /note="Response regulatory"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT DOMAIN 152..344
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT ACT_SITE 164
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099,
FT ECO:0000305|PubMed:7608974"
FT ACT_SITE 190
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099,
FT ECO:0000305|PubMed:7608974"
FT ACT_SITE 286
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099,
FT ECO:0000305|PubMed:7608974"
FT MOD_RES 56
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099,
FT ECO:0000269|PubMed:9465023"
FT MUTAGEN 207
FT /note="C->A: Slight increase in methylesterase activity."
FT /evidence="ECO:0000269|PubMed:3539934"
FT MUTAGEN 284
FT /note="G->V: Loss of methylesterase activity."
FT /evidence="ECO:0000269|PubMed:3539934"
FT MUTAGEN 309
FT /note="C->A: Loss of methylesterase activity."
FT /evidence="ECO:0000269|PubMed:3539934"
FT STRAND 4..9
FT /evidence="ECO:0007829|PDB:1A2O"
FT HELIX 13..24
FT /evidence="ECO:0007829|PDB:1A2O"
FT STRAND 29..37
FT /evidence="ECO:0007829|PDB:1A2O"
FT HELIX 38..48
FT /evidence="ECO:0007829|PDB:1A2O"
FT STRAND 51..56
FT /evidence="ECO:0007829|PDB:1A2O"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:1A2O"
FT HELIX 64..73
FT /evidence="ECO:0007829|PDB:1A2O"
FT STRAND 79..83
FT /evidence="ECO:0007829|PDB:1A2O"
FT HELIX 87..99
FT /evidence="ECO:0007829|PDB:1A2O"
FT STRAND 103..106
FT /evidence="ECO:0007829|PDB:1A2O"
FT STRAND 108..111
FT /evidence="ECO:0007829|PDB:1A2O"
FT HELIX 116..132
FT /evidence="ECO:0007829|PDB:1A2O"
FT HELIX 135..138
FT /evidence="ECO:0007829|PDB:1A2O"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:1CHD"
FT STRAND 158..163
FT /evidence="ECO:0007829|PDB:1CHD"
FT HELIX 167..175
FT /evidence="ECO:0007829|PDB:1CHD"
FT STRAND 184..189
FT /evidence="ECO:0007829|PDB:1CHD"
FT HELIX 195..206
FT /evidence="ECO:0007829|PDB:1CHD"
FT STRAND 208..213
FT /evidence="ECO:0007829|PDB:1CHD"
FT STRAND 224..227
FT /evidence="ECO:0007829|PDB:1CHD"
FT STRAND 232..239
FT /evidence="ECO:0007829|PDB:1CHD"
FT STRAND 242..248
FT /evidence="ECO:0007829|PDB:1CHD"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:1A2O"
FT STRAND 256..258
FT /evidence="ECO:0007829|PDB:1CHD"
FT HELIX 260..270
FT /evidence="ECO:0007829|PDB:1CHD"
FT HELIX 272..274
FT /evidence="ECO:0007829|PDB:1CHD"
FT STRAND 275..279
FT /evidence="ECO:0007829|PDB:1CHD"
FT STRAND 281..285
FT /evidence="ECO:0007829|PDB:1CHD"
FT HELIX 288..296
FT /evidence="ECO:0007829|PDB:1CHD"
FT STRAND 300..304
FT /evidence="ECO:0007829|PDB:1CHD"
FT TURN 306..308
FT /evidence="ECO:0007829|PDB:1CHD"
FT STRAND 310..313
FT /evidence="ECO:0007829|PDB:1CHD"
FT HELIX 314..320
FT /evidence="ECO:0007829|PDB:1CHD"
FT STRAND 325..328
FT /evidence="ECO:0007829|PDB:1CHD"
FT HELIX 330..332
FT /evidence="ECO:0007829|PDB:1CHD"
FT HELIX 333..341
FT /evidence="ECO:0007829|PDB:1CHD"
FT TURN 342..346
FT /evidence="ECO:0007829|PDB:1CHD"
SQ SEQUENCE 349 AA; 37552 MW; 79BAFC2D202F2F8B CRC64;
MSKIRVLSVD DSALMRQIMT EIINSHSDME MVATAPDPLV ARDLIKKFNP DVLTLDVEMP
RMDGLDFLEK LMRLRPMPVV MVSSLTGKGS EVTLRALELG AIDFVTKPQL GIREGMLAYS
EMIAEKVRTA ARARIAAHKP MAAPTTLKAG PLLSSEKLIA IGASTGGTEA IRHVLQPLPL
SSPAVIITQH MPPGFTRSFA ERLNKLCQIS VKEAEDGERV LPGHAYIAPG DKHMELARSG
ANYQIKIHDG PPVNRHRPSV DVLFHSVAKH AGRNAVGVIL TGMGNDGAAG MLAMYQAGAW
TIAQNEASCV VFGMPREAIN MGGVSEVVDL SQVSQQMLAK ISAGQAIRI
