ID Y914_STRS7 Reviewed; 225 AA.
AC C0MEY7;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE RecName: Full=UPF0758 protein SZO_09140;
GN OrderedLocusNames=SZO_09140;
OS Streptococcus equi subsp. zooepidemicus (strain H70).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=553483;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H70;
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).
CC -!- SIMILARITY: Belongs to the UPF0758 family. {ECO:0000305}.
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DR EMBL; FM204884; CAW99162.1; -; Genomic_DNA.
DR AlphaFoldDB; C0MEY7; -.
DR SMR; C0MEY7; -.
DR KEGG; seq:SZO_09140; -.
DR eggNOG; COG2003; Bacteria.
DR HOGENOM; CLU_073529_0_2_9; -.
DR Proteomes; UP000001368; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd08071; MPN_DUF2466; 1.
DR Gene3D; 3.40.140.10; Cytidine Deaminase, domain 2; 1.
DR InterPro; IPR037518; MPN.
DR InterPro; IPR025657; RadC_JAB.
DR InterPro; IPR010994; RuvA_2-like.
DR InterPro; IPR001405; UPF0758.
DR InterPro; IPR020891; UPF0758_CS.
DR InterPro; IPR046778; UPF0758_N.
DR NCBIfam; TIGR00608; radc; 1.
DR PANTHER; PTHR30471; DNA REPAIR PROTEIN RADC; 1.
DR PANTHER; PTHR30471:SF3; UPF0758 PROTEIN YEES-RELATED; 1.
DR Pfam; PF04002; RadC; 1.
DR Pfam; PF20582; UPF0758_N; 1.
DR SUPFAM; SSF47781; RuvA domain 2-like; 1.
DR PROSITE; PS50249; MPN; 1.
DR PROSITE; PS01302; UPF0758; 1.
PE 3: Inferred from homology;
KW Hydrolase; Metal-binding; Metalloprotease; Protease; Zinc.
FT CHAIN 1..225
FT /note="UPF0758 protein SZO_09140"
FT /id="PRO_1000201881"
FT DOMAIN 102..224
FT /note="MPN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT MOTIF 173..186
FT /note="JAMM motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 173
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 175
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 186
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
SQ SEQUENCE 225 AA; 25497 MW; C69B7A563CB25137 CRC64;
MYSIKTDHKL MPRERLIRLG PEKLSNQELL AILLRTGNKE KHVLELSAYL LSSLDSLADL
KKFSLQELQR LSGIGKVKAI EIKAMLELAD RIQIAGQAVA DPVLSSAQVA EKMMIELGDK
QQEHLVAIYL DSQNKIIEEK TIFIGTVRKS IAEPREILYY ACKNMATSLI VVHNHPSGLT
KPSANDYHFT EKIKRSCDYL GLICLDHIIV SKHGYYSFRE KSDLF
//
