CHED2_SHEON
ID CHED2_SHEON Reviewed; 202 AA.
AC Q8EEQ1;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2013, sequence version 2.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Probable chemoreceptor glutamine deamidase CheD 2 {ECO:0000255|HAMAP-Rule:MF_01440};
DE EC=3.5.1.44 {ECO:0000255|HAMAP-Rule:MF_01440};
GN Name=cheD2 {ECO:0000255|HAMAP-Rule:MF_01440}; Synonyms=cheD-2;
GN OrderedLocusNames=SO_2326;
OS Shewanella oneidensis (strain MR-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=211586;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR-1;
RX PubMed=12368813; DOI=10.1038/nbt749;
RA Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A., Clayton R.A.,
RA Meyer T., Tsapin A., Scott J., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R.,
RA Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J.J.,
RA Weidman J.F., Impraim M., Lee K., Berry K.J., Lee C., Mueller J.,
RA Khouri H.M., Gill J., Utterback T.R., McDonald L.A., Feldblyum T.V.,
RA Smith H.O., Venter J.C., Nealson K.H., Fraser C.M.;
RT "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT Shewanella oneidensis.";
RL Nat. Biotechnol. 20:1118-1123(2002).
CC -!- FUNCTION: Probably deamidates glutamine residues to glutamate on
CC methyl-accepting chemotaxis receptors (MCPs), playing an important role
CC in chemotaxis. {ECO:0000255|HAMAP-Rule:MF_01440}.
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_01440};
CC -!- SIMILARITY: Belongs to the CheD family. {ECO:0000255|HAMAP-
CC Rule:MF_01440}.
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DR EMBL; AE014299; AAN55360.2; -; Genomic_DNA.
DR RefSeq; NP_717916.2; NC_004347.2.
DR RefSeq; WP_011072318.1; NZ_CP053946.1.
DR AlphaFoldDB; Q8EEQ1; -.
DR SMR; Q8EEQ1; -.
DR STRING; 211586.SO_2326; -.
DR PaxDb; Q8EEQ1; -.
DR DNASU; 1170050; -.
DR KEGG; son:SO_2326; -.
DR PATRIC; fig|211586.12.peg.2241; -.
DR eggNOG; COG1871; Bacteria.
DR HOGENOM; CLU_087854_0_0_6; -.
DR OrthoDB; 1863047at2; -.
DR PhylomeDB; Q8EEQ1; -.
DR BioCyc; SONE211586:G1GMP-2125-MON; -.
DR Proteomes; UP000008186; Chromosome.
DR GO; GO:0050568; F:protein-glutamine glutaminase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-UniRule.
DR CDD; cd16352; CheD; 1.
DR Gene3D; 3.30.1330.200; -; 1.
DR HAMAP; MF_01440; CheD; 1.
DR InterPro; IPR038592; CheD-like_sf.
DR InterPro; IPR005659; Chemorcpt_Glu_NH3ase_CheD.
DR InterPro; IPR011324; Cytotoxic_necrot_fac-like_cat.
DR PANTHER; PTHR35147; PTHR35147; 1.
DR Pfam; PF03975; CheD; 1.
DR SUPFAM; SSF64438; SSF64438; 1.
PE 3: Inferred from homology;
KW Chemotaxis; Hydrolase; Reference proteome.
FT CHAIN 1..202
FT /note="Probable chemoreceptor glutamine deamidase CheD 2"
FT /id="PRO_0000251065"
SQ SEQUENCE 202 AA; 23028 MW; BD622C382D6A2FB9 CRC64;
MENMAFNQRT VVMIGPGEHY VTAKNEVIKT LLGSCVAVCL YDPKAQVIGM NHFLLAADRR
KFTHFLDSRA GYYGVHAMEI LINAMLKRGA QRKYLQSKIF GGANVLSLCA DNILNHYDIG
GMNIDFVRHF LQRERIPIIS EDIGGHCGRV IYFDPTDYSV YRSLIEHKYE EIASLQDEEY
RYFNQASEDI HSSGVPVVIW SD