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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
 
 
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