ID U2YGM6_STRAP Unreviewed; 353 AA.
AC U2YGM6;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Xaa-Pro aminopeptidase {ECO:0000313|EMBL:GAD47095.1};
GN ORFNames=ANG6_1590 {ECO:0000313|EMBL:GAD47095.1};
OS Streptococcus anginosus T5.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus; Streptococcus anginosus group.
OX NCBI_TaxID=1163302 {ECO:0000313|EMBL:GAD47095.1, ECO:0000313|Proteomes:UP000016981};
RN [1] {ECO:0000313|EMBL:GAD47095.1, ECO:0000313|Proteomes:UP000016981}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T5 {ECO:0000313|EMBL:GAD47095.1,
RC ECO:0000313|Proteomes:UP000016981};
RA Maruyama F., Sakurai A., Ogura Y., Homma H., Takahashi N., Ohtsubo Y.,
RA Hoshino T., Okahashi N., Nakagawa I., Kimura S., Fujiwara T., Hayashi T.,
RA Shintani S.;
RT "Genome Sequences of seven clinical isolates and type strains of anginosus
RT group streptococci.";
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
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:GAD47095.1}.
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DR EMBL; BASY01000019; GAD47095.1; -; Genomic_DNA.
DR RefSeq; WP_022527027.1; NZ_BASY01000019.1.
DR AlphaFoldDB; U2YGM6; -.
DR Proteomes; UP000016981; Unassembled WGS sequence.
DR GO; GO:0004177; F:aminopeptidase 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:SF3; AMINOPEPTIDASE YPDF; 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; PS00491; PROLINE_PEPTIDASE; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000313|EMBL:GAD47095.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU000590}; Protease {ECO:0000313|EMBL:GAD47095.1}.
FT DOMAIN 4..127
FT /note="Creatinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01321"
FT DOMAIN 135..337
FT /note="Peptidase M24"
FT /evidence="ECO:0000259|Pfam:PF00557"
SQ SEQUENCE 353 AA; 39440 MW; 21D6FFC7EC7AB4D6 CRC64;
MLSRVEKFEV ALKQTECDAV LVTNLKNIYY LTGFSGTEAT VFISKNRRIF LTDSRYTLIA
KGVVKGFDIV ETRDALSEIA KIIADDKIEK IGFDDQVSYA YFKMLKSVFA AYELIPMSSF
IENLRMIKDA EEIDTIRKAC QISDQAFLDV LDFIKPGETT ELAVMNFLDA RMRKLGASGA
SFDFIIASGY RSAMPHGVAS EKVIQTGETL TMDFGCYYNH YVSDMTRTIH VGHVTDEERE
IYDIVLCANK ALIDQAKAGV SRIDFDRIPR QIINDAGYGT YFTHGIGHGI GLDIHEIPYF
GKSSEPIEAG MVLTDEPGIY LDGKYGVRIE DDILITDTGC ELLTLAPKEL IVI
//
