ID G5KB76_9STRE Unreviewed; 361 AA.
AC G5KB76;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE SubName: Full=Metallopeptidase family M24 {ECO:0000313|EMBL:EHI64244.1};
DE EC=3.4.-.- {ECO:0000313|EMBL:EHI64244.1};
GN ORFNames=STRPS_1595 {ECO:0000313|EMBL:EHI64244.1};
OS Streptococcus pseudoporcinus LQ 940-04.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=875093 {ECO:0000313|EMBL:EHI64244.1, ECO:0000313|Proteomes:UP000003217};
RN [1] {ECO:0000313|EMBL:EHI64244.1, ECO:0000313|Proteomes:UP000003217}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LQ940-04 {ECO:0000313|Proteomes:UP000003217};
RX PubMed=24625962; DOI=10.1093/gbe/evu048;
RA Richards V.P., Palmer S.R., Pavinski Bitar P.D., Qin X., Weinstock G.M.,
RA Highlander S.K., Town C.D., Burne R.A., Stanhope M.J.;
RT "Phylogenomics and the dynamic genome evolution of the genus
RT Streptococcus.";
RL Genome Biol. Evol. 6:741-753(2014).
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SIMILARITY: Belongs to the peptidase M24B family.
CC {ECO:0000256|RuleBase:RU000590}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHI64244.1}.
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DR EMBL; AEUY02000005; EHI64244.1; -; Genomic_DNA.
DR RefSeq; WP_007893493.1; NZ_AEUY02000005.1.
DR AlphaFoldDB; G5KB76; -.
DR STRING; 361101.GCA_900102825_01270; -.
DR MEROPS; M24.006; -.
DR GeneID; 58556140; -.
DR OrthoDB; 9806388at2; -.
DR Proteomes; UP000003217; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd01092; APP-like; 1.
DR Gene3D; 3.90.230.10; Creatinase/methionine aminopeptidase superfamily; 1.
DR Gene3D; 3.40.350.10; Creatinase/prolidase N-terminal domain; 1.
DR InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR InterPro; IPR000587; Creatinase_N.
DR InterPro; IPR000994; Pept_M24.
DR InterPro; IPR001131; Peptidase_M24B_aminopep-P_CS.
DR PANTHER; PTHR46112; AMINOPEPTIDASE; 1.
DR PANTHER; PTHR46112:SF10; DIPEPTIDASE YKVY-RELATED; 1.
DR Pfam; PF01321; Creatinase_N; 1.
DR Pfam; PF00557; Peptidase_M24; 1.
DR SUPFAM; SSF55920; Creatinase/aminopeptidase; 1.
DR SUPFAM; SSF53092; Creatinase/prolidase N-terminal domain; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS00491; PROLINE_PEPTIDASE; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EHI64244.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU000590}.
FT DOMAIN 4..132
FT /note="Creatinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01321"
FT DOMAIN 141..343
FT /note="Peptidase M24"
FT /evidence="ECO:0000259|Pfam:PF00557"
SQ SEQUENCE 361 AA; 40277 MW; 465B6C64DCA357F8 CRC64;
MTKITQIQDF LTSKEAQLAI FSDPVTVNYL TGFACDPHER QMFLFIYDQI APVLFVPALE
VARAQKLVTF PVFGYIDSEN PWEKIKAVLP NTSPKRLYAE FDHLNVSKFQ GLQGIFSGHF
ENLTPFIQNM RLLKSADEID KMMIAGEFAD KAVQIGFENI SLEATETDII AQIEFEMKKQ
GISKMSFETM VLTGHNAANP HGIPGTNKIE NNALLLFDLG VETLGYTSDM TRTVAVGKPD
QFKIDIYNLC LEAQLTAQEF VKPGVTAAEV DAAARSVIEK AGYGEYFNHR LGHGLGMDVH
EFPSIMAGNN LEIQEGMCFS IEPGIYIPGK VGVRIEDCGH VTKEGFQAFT KTRKELQYFD
C
//
