ID D4M5P1_9FIRM Unreviewed; 596 AA.
AC D4M5P1;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Xaa-Pro aminopeptidase {ECO:0000313|EMBL:CBL26553.1};
DE EC=3.4.11.9 {ECO:0000313|EMBL:CBL26553.1};
GN ORFNames=RTO_20180 {ECO:0000313|EMBL:CBL26553.1};
OS [Ruminococcus] torques L2-14.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Mediterraneibacter.
OX NCBI_TaxID=657313 {ECO:0000313|EMBL:CBL26553.1, ECO:0000313|Proteomes:UP000008956};
RN [1] {ECO:0000313|EMBL:CBL26553.1, ECO:0000313|Proteomes:UP000008956}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L2-14 {ECO:0000313|EMBL:CBL26553.1,
RC ECO:0000313|Proteomes:UP000008956};
RG metaHIT consortium -- http://www.metahit.eu/;
RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT "The genome sequence of Ruminococcus torques L2-14.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBL26553.1, ECO:0000313|Proteomes:UP000008956}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L2-14 {ECO:0000313|EMBL:CBL26553.1,
RC ECO:0000313|Proteomes:UP000008956};
RA Pajon A.;
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase M24B family.
CC {ECO:0000256|ARBA:ARBA00008766}.
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; FP929055; CBL26553.1; -; Genomic_DNA.
DR AlphaFoldDB; D4M5P1; -.
DR STRING; 33039.ERS852502_01807; -.
DR KEGG; rto:RTO_20180; -.
DR PATRIC; fig|657313.3.peg.1843; -.
DR HOGENOM; CLU_011781_2_4_9; -.
DR Proteomes; UP000008956; Chromosome.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR CDD; cd01085; APP; 1.
DR Gene3D; 3.90.230.10; Creatinase/methionine aminopeptidase superfamily; 1.
DR Gene3D; 3.40.350.10; Creatinase/prolidase N-terminal domain; 2.
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; IPR033740; Pept_M24B.
DR InterPro; IPR032416; Peptidase_M24_C.
DR PANTHER; PTHR43763; XAA-PRO AMINOPEPTIDASE 1; 1.
DR PANTHER; PTHR43763:SF6; XAA-PRO AMINOPEPTIDASE 1; 1.
DR Pfam; PF01321; Creatinase_N; 1.
DR Pfam; PF16189; Creatinase_N_2; 1.
DR Pfam; PF00557; Peptidase_M24; 1.
DR Pfam; PF16188; Peptidase_M24_C; 1.
DR SUPFAM; SSF55920; Creatinase/aminopeptidase; 1.
DR SUPFAM; SSF53092; Creatinase/prolidase N-terminal domain; 2.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000313|EMBL:CBL26553.1};
KW Hydrolase {ECO:0000313|EMBL:CBL26553.1};
KW Protease {ECO:0000313|EMBL:CBL26553.1}.
FT DOMAIN 6..125
FT /note="Creatinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01321"
FT DOMAIN 309..526
FT /note="Peptidase M24"
FT /evidence="ECO:0000259|Pfam:PF00557"
FT DOMAIN 535..594
FT /note="Peptidase M24 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16188"
SQ SEQUENCE 596 AA; 67969 MW; AB21A65C7B4535FF CRC64;
MSVLDRIERL RNVMEQQKID CYIIPTDDYH HSEYVGDYFK FREYITGFTG SAGTAVFTKD
KAGLWTDGRY FIQAEAQLKG SGITLYKSGE SDVPTIEEFL KSELKEGDVL GFDGRTVTYA
QGKRYCHIAD ENGASLKYSL DFAQNIWKER PEMSMESVFS LADEYTGEKI GSKLERIREI
MKENGCNAHV LSSLDDIAWL LNIRGNDIAY CPLVLSYAIV YNNSVELFAD IRKFSDDIVN
SLAENQVKIY PYEDIYHKVS EMTSEDKVLL DSSIMNYSLY QAISKETVII DKQNPEILMK
SVKNETQAEN LRKAHLKDAV AHTKFMYWLK KNIGRVEITE LSASARLEGL RAEQEHFLGP
SFGPISAYGE HGAIVHYSAD EKSNVPLKEG KLFMTDTGGH YLEGSTDITR TVALGEVGNL
EKEHFTLVAR AMLRLANTVF LYGCSGVNLD CIAREIFWKE GLNFNHGTGH GVGYLLNIHE
GPINFRWKEG ERSAPALEEN MVITDEPGIY IEGSYGIRLE NELLVRKTVK NEYGQFMNFE
ILTYVPIDLD AILPEKMSTE EKEMLNHYHK QVYEKVSPYL SEEERIWLKE YTRAVK
//
