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Database: UniProt
Entry: A0LIT0_SYNFM
LinkDB: A0LIT0_SYNFM
Original site: A0LIT0_SYNFM 
ID   A0LIT0_SYNFM            Unreviewed;       669 AA.
AC   A0LIT0;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   27-MAR-2024, entry version 98.
DE   RecName: Full=protein-glutamate methylesterase {ECO:0000256|ARBA:ARBA00039140};
DE            EC=3.1.1.61 {ECO:0000256|ARBA:ARBA00039140};
GN   OrderedLocusNames=Sfum_1645 {ECO:0000313|EMBL:ABK17332.1};
OS   Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB).
OC   Bacteria; Thermodesulfobacteriota; Syntrophobacteria; Syntrophobacterales;
OC   Syntrophobacteraceae; Syntrophobacter.
OX   NCBI_TaxID=335543 {ECO:0000313|EMBL:ABK17332.1, ECO:0000313|Proteomes:UP000001784};
RN   [1] {ECO:0000313|EMBL:ABK17332.1, ECO:0000313|Proteomes:UP000001784}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10017 / MPOB {ECO:0000313|Proteomes:UP000001784};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.G.,
RA   Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Boone D.R., Brockman F., Culley D., Ferry J., Gunsalus R.,
RA   McInerney M.J., Morrison M., Plugge C., Rohlin L., Scholten J., Sieber J.,
RA   Stams A.J.M., Worm P., Henstra A.M., Richardson P.;
RT   "Complete sequence of Syntrophobacter fumaroxidans MPOB.";
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
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;
CC         Evidence={ECO:0000256|ARBA:ARBA00000941};
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00050}.
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DR   EMBL; CP000478; ABK17332.1; -; Genomic_DNA.
DR   RefSeq; WP_011698502.1; NC_008554.1.
DR   AlphaFoldDB; A0LIT0; -.
DR   STRING; 335543.Sfum_1645; -.
DR   KEGG; sfu:Sfum_1645; -.
DR   eggNOG; COG2201; Bacteria.
DR   HOGENOM; CLU_410445_0_0_7; -.
DR   InParanoid; A0LIT0; -.
DR   OrthoDB; 9793421at2; -.
DR   Proteomes; UP000001784; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0000156; F:phosphorelay response regulator activity; IEA:InterPro.
DR   GO; GO:0008984; F:protein-glutamate methylesterase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR   CDD; cd17541; REC_CheB-like; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 3.40.50.180; Methylesterase CheB, C-terminal domain; 1.
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   PANTHER; PTHR42872; PROTEIN-GLUTAMATE METHYLESTERASE/PROTEIN-GLUTAMINE GLUTAMINASE; 1.
DR   PANTHER; PTHR42872:SF6; PROTEIN-GLUTAMATE METHYLESTERASE_PROTEIN-GLUTAMINE GLUTAMINASE; 1.
DR   Pfam; PF01339; CheB_methylest; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF52172; CheY-like; 1.
DR   SUPFAM; SSF52738; Methylesterase CheB, C-terminal domain; 1.
DR   PROSITE; PS50122; CHEB; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ABK17332.1};
KW   Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001784}.
FT   DOMAIN          314..431
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          474..660
FT                   /note="CheB-type methylesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50122"
FT   MOD_RES         365
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   669 AA;  74294 MW;  2AFE1AD2A8F932CB CRC64;
     MNVLLLDPQQ KYAERLRDLS SVVEGANVIS ADEIRICPSD SANIDIIVAG YDRANPRTLD
     ALLEWRSHPH TYLVPCWILA DARSFEAVCQ WPRLSVDRFD EQLDIPAFCS WLETVAEWQQ
     NRMQLPGTNR FISHSPLELT TSLALRKASG KLSLFDEEGG EGAFLLRDGY LTGSTLKHLS
     GTEAFLEFLT WSKGSYLWEP LDTIEFTDQS SPIEFMFHEA LKLFREANLL YHFVPDLNRS
     LTKTESESAL DDGAVYYFAE LKVLYNLIDG KATVRQVVEA SPLSQLRTLC CLSKWFSLGD
     VAVVPEESPI PRRGLLIVDD SHLMCKALRD VFAKDPRFEV LGFAHDGLQA LELIEQLKPD
     VLTLDMQMPR MDGLTALKHI MIRNPRPVVV VSAFTKETSL LTYQSFKYGA VDVLTKPSGG
     NPGSREHESR LIRDRVAQAS CVRIEAAQYI RSGGRSKPAE KDGAFSPEAR DRAEHASNGL
     AVILCGSGGF PSLLKMLFSI ENTDRLPTLL GGIALSKKAV ESMVPNMEKD SSMRMTELTP
     PGGILLPNSS YLFSCEDSFH LVRENDQTMA RCDQDSAAEH RPFDRLLFSL GDGFGEHAMA
     VLLSGTGHDG IEGMEHVRRA GGKTYVLSPE ACLEPDLPRR ILQYGFAQEV KSASELASLL
     QNVGSENGK
//
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