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CHEB3_LEPIN
ID   CHEB3_LEPIN             Reviewed;         347 AA.
AC   Q8F3H4;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 105.
DE   RecName: Full=Protein-glutamate methylesterase/protein-glutamine glutaminase 3 {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=cheB3 {ECO:0000255|HAMAP-Rule:MF_00099}; OrderedLocusNames=LA_2429;
OS   Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain
OS   56601).
OC   Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX   NCBI_TaxID=189518;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=56601;
RX   PubMed=12712204; DOI=10.1038/nature01597;
RA   Ren S.-X., Fu G., Jiang X.-G., Zeng R., Miao Y.-G., Xu H., Zhang Y.-X.,
RA   Xiong H., Lu G., Lu L.-F., Jiang H.-Q., Jia J., Tu Y.-F., Jiang J.-X.,
RA   Gu W.-Y., Zhang Y.-Q., Cai Z., Sheng H.-H., Yin H.-F., Zhang Y., Zhu G.-F.,
RA   Wan M., Huang H.-L., Qian Z., Wang S.-Y., Ma W., Yao Z.-J., Shen Y.,
RA   Qiang B.-Q., Xia Q.-C., Guo X.-K., Danchin A., Saint Girons I.,
RA   Somerville R.L., Wen Y.-M., Shi M.-H., Chen Z., Xu J.-G., Zhao G.-P.;
RT   "Unique physiological and pathogenic features of Leptospira interrogans
RT   revealed by whole-genome sequencing.";
RL   Nature 422:888-893(2003).
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; AE010300; AAN49628.1; -; Genomic_DNA.
DR   RefSeq; NP_712610.1; NC_004342.2.
DR   RefSeq; WP_000616854.1; NC_004342.2.
DR   AlphaFoldDB; Q8F3H4; -.
DR   SMR; Q8F3H4; -.
DR   STRING; 189518.LA_2429; -.
DR   EnsemblBacteria; AAN49628; AAN49628; LA_2429.
DR   GeneID; 61144819; -.
DR   KEGG; lil:LA_2429; -.
DR   PATRIC; fig|189518.3.peg.2409; -.
DR   HOGENOM; CLU_000445_51_0_12; -.
DR   InParanoid; Q8F3H4; -.
DR   OMA; YGMPMAV; -.
DR   Proteomes; UP000001408; Chromosome I.
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..347
FT                   /note="Protein-glutamate methylesterase/protein-glutamine
FT                   glutaminase 3"
FT                   /id="PRO_0000158004"
FT   DOMAIN          3..120
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT   DOMAIN          159..347
FT                   /note="CheB-type methylesterase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT   ACT_SITE        171
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT   ACT_SITE        197
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT   ACT_SITE        293
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   347 AA;  37987 MW;  98953DDDB2F7DCB9 CRC64;
     MIQVFIVDDS AVVRQVLTQI LNKDPEIEII GFASDPIFAS EKLSSVWPDV FILDIEMPRM
     DGISFLKKIM SEKPTPVIIC SSLAEKESET AVLAMKLGAV DIIEKPKVGL KNFLEESEIL
     FIDSVRAASN ARVKTHSFQN DDSKFLENHK QPKTDFSKID TTDKLIAIGT STGGTQALEF
     ILTQLNIHCP GIVIVQHMPE KFTEAFANRL NQVCKIQVKE AKDGDRVQLG SAYIAPGNKH
     MEIYLSGAQF HIRVLDGPLV NRHRPSVDTL FHSVAKAAGK NAKGIIMTGM GNDGANGLLK
     MKQSGAHTIA QDEASCVVFG MPKEAILKGA VNTILPLSKI VGEVQYF
 
 
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