ID C0MEY8_STRS7 Unreviewed; 231 AA.
AC C0MEY8;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE SubName: Full=Putative peptidase {ECO:0000313|EMBL:CAW99164.1};
GN OrderedLocusNames=SZO_09150 {ECO:0000313|EMBL:CAW99164.1};
OS Streptococcus equi subsp. zooepidemicus (strain H70).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=553483 {ECO:0000313|Proteomes:UP000001368};
RN [1] {ECO:0000313|EMBL:CAW99164.1, ECO:0000313|Proteomes:UP000001368}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H70 {ECO:0000313|EMBL:CAW99164.1,
RC ECO:0000313|Proteomes:UP000001368};
RX PubMed=19325880; DOI=10.1371/journal.ppat.1000346;
RA Holden M.T.G., Heather Z., Paillot R., Steward K.F., Webb K., Ainslie F.,
RA Jourdan T., Bason N.C., Holroyd N.E., Mungall K., Quail M.A., Sanders M.,
RA Simmonds M., Willey D., Brooks K., Aanensen D.M., Spratt B.G., Jolley K.A.,
RA Maiden M.C.J., Kehoe M., Chanter N., Bentley S.D., Robinson C.,
RA Maskell D.J., Parkhill J., Waller A.S.;
RT "Genomic evidence for the evolution of Streptococcus equi: host
RT restriction, increased virulence, and genetic exchange with human
RT pathogens.";
RL PLoS Pathog. 5:E1000346-E1000346(2009).
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DR EMBL; FM204884; CAW99164.1; -; Genomic_DNA.
DR AlphaFoldDB; C0MEY8; -.
DR KEGG; seq:SZO_09150; -.
DR eggNOG; COG2071; Bacteria.
DR HOGENOM; CLU_030756_2_1_9; -.
DR Proteomes; UP000001368; 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}.
FT ACT_SITE 112
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 209
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 211
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 231 AA; 25672 MW; 71321DF238A3B358 CRC64;
MSKTIIGITA NQRVTKALDN LPWSYAPTGF IEAVTRSGGL PLLLPIGDEA AAKSYVTMVD
KIILIGGQHV DPKYYHEKRA ALDGDFSPQR DTFELAIIKE ALAQKKPILG ICRGMQLMNV
ALGGNLNQHI DGHWQKTASD CLSQEIVVEK ASPLYPIYGP RALINSFHHQ SLKRVAKDLR
VIARDPNDGT IEAVVSCNPD IPFLGVQWHP ELLQAIREED LKLFDWFIHS L
//
