ID Q5M4L2_STRT2 Unreviewed; 247 AA.
AC Q5M4L2;
DT 01-FEB-2005, integrated into UniProtKB/TrEMBL.
DT 01-FEB-2005, sequence version 1.
DT 27-MAR-2024, entry version 105.
DE SubName: Full=Agmatinase (Arginase family), putative {ECO:0000313|EMBL:AAV60587.1};
GN Name=speB {ECO:0000313|EMBL:AAV60587.1};
GN OrderedLocusNames=stu0921 {ECO:0000313|EMBL:AAV60587.1};
OS Streptococcus thermophilus (strain ATCC BAA-250 / LMG 18311).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=264199 {ECO:0000313|EMBL:AAV60587.1, ECO:0000313|Proteomes:UP000001170};
RN [1] {ECO:0000313|EMBL:AAV60587.1, ECO:0000313|Proteomes:UP000001170}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-250 / LMG 18311 {ECO:0000313|Proteomes:UP000001170};
RX PubMed=15543133; DOI=10.1038/nbt1034;
RA Bolotin A., Quinquis B., Renault P., Sorokin A., Ehrlich S.D.,
RA Kulakauskas S., Lapidus A., Goltsman E., Mazur M., Pusch G.D., Fonstein M.,
RA Overbeek R., Kyprides N., Purnelle B., Prozzi D., Ngui K., Masuy D.,
RA Hancy F., Burteau S., Boutry M., Delcour J., Goffeau A., Hols P.;
RT "Complete sequence and comparative genome analysis of the dairy bacterium
RT Streptococcus thermophilus.";
RL Nat. Biotechnol. 22:1554-1558(2004).
CC -!- SIMILARITY: Belongs to the arginase family. {ECO:0000256|PROSITE-
CC ProRule:PRU00742}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000023; AAV60587.1; -; Genomic_DNA.
DR RefSeq; WP_011225905.1; NC_006448.1.
DR AlphaFoldDB; Q5M4L2; -.
DR STRING; 264199.stu0921; -.
DR GeneID; 66898789; -.
DR KEGG; stl:stu0921; -.
DR eggNOG; COG0010; Bacteria.
DR HOGENOM; CLU_1092973_0_0_9; -.
DR Proteomes; UP000001170; Chromosome.
DR GO; GO:0016813; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR Gene3D; 3.40.800.10; Ureohydrolase domain; 1.
DR InterPro; IPR006035; Ureohydrolase.
DR InterPro; IPR023696; Ureohydrolase_dom_sf.
DR PANTHER; PTHR11358; ARGINASE/AGMATINASE; 1.
DR Pfam; PF00491; Arginase; 1.
DR PIRSF; PIRSF036979; Arginase; 1.
DR SUPFAM; SSF52768; Arginase/deacetylase; 1.
DR PROSITE; PS51409; ARGINASE_2; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000001170}.
SQ SEQUENCE 247 AA; 28412 MW; F2F763D460CF77FA CRC64;
MKILSIIYDG GSRIPGARFA PTKYYQEAML YDRKDSDIIT INLGNQDLFS IDLESLSRTI
AESKVQIALG GDHSVTYLLA KATVREGAYL IVLDAHLDYF KDFESVVKNW NFLSFLTDIF
EKIIIIGERN FEFPSSFDNK IIILSMEEYW LNKSRVLKKL DSYIDESKDI YLSIDIDVLD
PSVFDSVSYP IIGGFQMNDF LGIISKILCS DKVYFCDIVE YNPMVGSDNA HIFYQMIQFV
KSKLRRI
//
