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Database: UniProt
Entry: F5Y2Z2_RAMTT
LinkDB: F5Y2Z2_RAMTT
Original site: F5Y2Z2_RAMTT 
ID   F5Y2Z2_RAMTT            Unreviewed;       267 AA.
AC   F5Y2Z2;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AEG94872.1};
GN   OrderedLocusNames=Rta_37570 {ECO:0000313|EMBL:AEG94872.1};
OS   Ramlibacter tataouinensis (strain ATCC BAA-407 / DSM 14655 / LMG 21543 /
OS   TTB310).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Ramlibacter.
OX   NCBI_TaxID=365046 {ECO:0000313|EMBL:AEG94872.1, ECO:0000313|Proteomes:UP000008385};
RN   [1] {ECO:0000313|Proteomes:UP000008385}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-407 / DSM 14655 / LMG 21543 / TTB310
RC   {ECO:0000313|Proteomes:UP000008385};
RA   Barakat M., Ortet P., De Luca G., Jourlin-Castelli C., Ansaldi M., Py B.,
RA   Fichant G., Coutinho P., Voulhoux R., Bastien O., Roy S., Marechal E.,
RA   Henrissat B., Quentin Y., Noirot P., Filloux A., Mejean V., DuBow M.,
RA   Barras F., Heulin T.;
RT   "Genome of the cyst-dividing bacterium Ramlibacter tataouinensis.";
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AEG94872.1, ECO:0000313|Proteomes:UP000008385}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-407 / DSM 14655 / LMG 21543 / TTB310
RC   {ECO:0000313|Proteomes:UP000008385};
RX   PubMed=21912644; DOI=10.1371/journal.pone.0023784;
RA   De Luca G., Barakat M., Ortet P., Fochesato S., Jourlin-Castelli C.,
RA   Ansaldi M., Py B., Fichant G., Coutinho P.M., Voulhoux R., Bastien O.,
RA   Marechal E., Henrissat B., Quentin Y., Noirot P., Filloux A., Mejean V.,
RA   Dubow M.S., Barras F., Barbe V., Weissenbach J., Mihalcescu I.,
RA   Vermeglio A., Achouak W., Heulin T.;
RT   "The Cyst-Dividing Bacterium Ramlibacter tataouinensis TTB310 Genome
RT   Reveals a Well-Stocked Toolbox for Adaptation to a Desert Environment.";
RL   PLoS ONE 6:E23784-E23784(2011).
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DR   EMBL; CP000245; AEG94872.1; -; Genomic_DNA.
DR   RefSeq; WP_013903100.1; NC_015677.1.
DR   AlphaFoldDB; F5Y2Z2; -.
DR   STRING; 365046.Rta_37570; -.
DR   KEGG; rta:Rta_37570; -.
DR   PATRIC; fig|365046.3.peg.3849; -.
DR   eggNOG; COG2071; Bacteria.
DR   HOGENOM; CLU_030756_2_1_4; -.
DR   OrthoDB; 9813383at2; -.
DR   Proteomes; UP000008385; Chromosome.
DR   GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:InterPro.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd01745; GATase1_2; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR011697; Peptidase_C26.
DR   InterPro; IPR044668; PuuD-like.
DR   PANTHER; PTHR43235; GLUTAMINE AMIDOTRANSFERASE PB2B2.05-RELATED; 1.
DR   PANTHER; PTHR43235:SF1; GLUTAMINE AMIDOTRANSFERASE PB2B2.05-RELATED; 1.
DR   Pfam; PF07722; Peptidase_C26; 1.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
PE   4: Predicted;
KW   Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008385}.
FT   ACT_SITE        125
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        232
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        234
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ   SEQUENCE   267 AA;  29676 MW;  460EEED30743670A CRC64;
     MIAASRLKIG LSACFSHADP TRSLFTNKTL QYVEQSIAHW IMSSGAMVVM VPCPTGSTAR
     GDVTYEHYAQ WLDGLVLHGG ADVWPGSYGE VPLEERWSGD RIRDEYDKAL VAAFESHGKP
     VFGVCRGLQL LNVAFGGTLW QDINTQIPDS LRHRDPDIYD LNHHSIEILP GSRLSQLYPG
     VERARVNSIH HQGIKRLSDE FVAEAVSHED GVVEAIRRKD PDKPYIAAVQ WHPEFHQPDM
     ATIDDAALLQ DFLAAVSAAK ERGSLRQ
//
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