ID A0A0Q7LGM8_9BURK Unreviewed; 465 AA.
AC A0A0Q7LGM8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Xaa-Pro aminopeptidase {ECO:0000313|EMBL:KQX91353.1};
GN ORFNames=ASD34_26275 {ECO:0000313|EMBL:KQX91353.1};
OS Variovorax sp. Root473.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=1736541 {ECO:0000313|EMBL:KQX91353.1, ECO:0000313|Proteomes:UP000051275};
RN [1] {ECO:0000313|Proteomes:UP000051275}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root473 {ECO:0000313|Proteomes:UP000051275};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQX91353.1, ECO:0000313|Proteomes:UP000051275}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root473 {ECO:0000313|EMBL:KQX91353.1,
RC ECO:0000313|Proteomes:UP000051275};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00008766, 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:KQX91353.1}.
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DR EMBL; LMEV01000013; KQX91353.1; -; Genomic_DNA.
DR RefSeq; WP_056575017.1; NZ_LMEV01000013.1.
DR AlphaFoldDB; A0A0Q7LGM8; -.
DR OrthoDB; 9806388at2; -.
DR Proteomes; UP000051275; Unassembled WGS sequence.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd01087; Prolidase; 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; IPR007865; Aminopep_P_N.
DR InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR InterPro; IPR000994; Pept_M24.
DR InterPro; IPR001131; Peptidase_M24B_aminopep-P_CS.
DR PANTHER; PTHR43226:SF9; XAA-PRO AMINOPEPTIDASE; 1.
DR PANTHER; PTHR43226; XAA-PRO AMINOPEPTIDASE 3; 1.
DR Pfam; PF05195; AMP_N; 1.
DR Pfam; PF00557; Peptidase_M24; 1.
DR SMART; SM01011; AMP_N; 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:KQX91353.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU000590};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000051275}.
FT DOMAIN 5..136
FT /note="Aminopeptidase P N-terminal"
FT /evidence="ECO:0000259|SMART:SM01011"
SQ SEQUENCE 465 AA; 51423 MW; 29E8117E162147DA CRC64;
MTFADTATIY AERRARLASQ LGKDGIAIVP TAPERQRNRD SDFLFRHDSY FYYLTGFTEP
NAWLVLAGDG RATLFCAPKD LEREIWDGYR LGPDAAPAAL GVDEACSVND LDAKLPKLLE
NRSTVWFPFA THKGLETRID DWLQSVRARV RFGALCPEEQ RDLCGPLDEM RLVKDAHEQD
IMRRAAQISA RAHIRAMQLS ARMLREGKDV REYHLDAELL HEFRLGGSQY PAYGSIVAAG
ANACVLHYRA DAAPVRKGEL VLIDAGCELD GYASDITRTF PADGTFSGPQ RALYDLVLAS
QDASAAATKA GNRFNDPHDA AVKVLAQGML DLGLLDGNKV GSVDDVIDSR AYFQFYMHRT
GHWLGMDVHD CGSYVEPTQV GEVSERKDPL SNELIKNRPS RILHPGMVLT LEPGIYVRPG
EGVPEQFHHI GIRIEDDAIV TATGCELISR GVPVKADEIE ALMRG
//
