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Database: UniProt
Entry: H2CLF0_9LEPT
LinkDB: H2CLF0_9LEPT
Original site: H2CLF0_9LEPT 
ID   H2CLF0_9LEPT            Unreviewed;       173 AA.
AC   H2CLF0;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=Probable chemoreceptor glutamine deamidase CheD {ECO:0000256|HAMAP-Rule:MF_01440};
DE            EC=3.5.1.44 {ECO:0000256|HAMAP-Rule:MF_01440};
GN   Name=cheD {ECO:0000256|HAMAP-Rule:MF_01440};
GN   ORFNames=Lepil_4083 {ECO:0000313|EMBL:EHQ04561.1};
OS   Leptonema illini DSM 21528.
OC   Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC   Leptonema.
OX   NCBI_TaxID=929563 {ECO:0000313|EMBL:EHQ04561.1, ECO:0000313|Proteomes:UP000005737};
RN   [1] {ECO:0000313|EMBL:EHQ04561.1, ECO:0000313|Proteomes:UP000005737}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21528 {ECO:0000313|EMBL:EHQ04561.1,
RC   ECO:0000313|Proteomes:UP000005737};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Held B.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Markowitz V., Cheng J.-F.,
RA   Hugenholtz P., Woyke T., Wu D., Gronow S., Wellnitz S., Brambilla E.-M.,
RA   Klenk H.-P., Eisen J.A.;
RT   "The Improved High-Quality Draft genome of Leptonema illini DSM 21528.";
RL   Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Probably deamidates glutamine residues to glutamate on
CC       methyl-accepting chemotaxis receptors (MCPs), playing an important role
CC       in chemotaxis. {ECO:0000256|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:0000256|HAMAP-
CC         Rule:MF_01440};
CC   -!- SIMILARITY: Belongs to the CheD family. {ECO:0000256|HAMAP-
CC       Rule:MF_01440}.
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DR   EMBL; JH597775; EHQ04561.1; -; Genomic_DNA.
DR   AlphaFoldDB; H2CLF0; -.
DR   STRING; 183.GCA_002009735_00300; -.
DR   HOGENOM; CLU_087854_2_0_12; -.
DR   Proteomes; UP000005737; Unassembled WGS sequence.
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; CHEMORECEPTOR GLUTAMINE DEAMIDASE CHED-RELATED; 1.
DR   PANTHER; PTHR35147:SF1; CHEMORECEPTOR GLUTAMINE DEAMIDASE CHED-RELATED; 1.
DR   Pfam; PF03975; CheD; 1.
DR   SUPFAM; SSF64438; CNF1/YfiH-like putative cysteine hydrolases; 1.
PE   3: Inferred from homology;
KW   Chemotaxis {ECO:0000256|ARBA:ARBA00022500, ECO:0000256|HAMAP-
KW   Rule:MF_01440};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01440};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005737}.
SQ   SEQUENCE   173 AA;  18925 MW;  023CFFF4308F6231 CRC64;
     MPNLRRSALK TENSSVIHVG VSEWKTAKHP DALRTTLGSC VGIVLYSKKD RAGGMCHALL
     DEPPAGKIAQ KGKYARTAIE ELLRELQRQG IDKANLTARL FGGASMFDAD KSKFFHNIGE
     SNVAVSRATL EKEGIAIIEE DVGGSSGRTI TFFLDDGRIL LRSGTQERYI YKA
//
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