ID A0A0F0KJ10_9MICO Unreviewed; 476 AA.
AC A0A0F0KJ10;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Xaa-Pro aminopeptidase 1 {ECO:0000313|EMBL:KJL20877.1};
DE EC=3.4.11.9 {ECO:0000313|EMBL:KJL20877.1};
GN Name=pepPI {ECO:0000313|EMBL:KJL20877.1};
GN ORFNames=RL72_02804 {ECO:0000313|EMBL:KJL20877.1};
OS Microbacterium azadirachtae.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=582680 {ECO:0000313|EMBL:KJL20877.1, ECO:0000313|Proteomes:UP000033448};
RN [1] {ECO:0000313|EMBL:KJL20877.1, ECO:0000313|Proteomes:UP000033448}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23848 {ECO:0000313|EMBL:KJL20877.1,
RC ECO:0000313|Proteomes:UP000033448};
RA Corretto E.;
RT "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT metal contaminated environments.";
RL Submitted (FEB-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:KJL20877.1}.
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DR EMBL; JYIT01000082; KJL20877.1; -; Genomic_DNA.
DR RefSeq; WP_045251456.1; NZ_JYIT01000082.1.
DR AlphaFoldDB; A0A0F0KJ10; -.
DR PATRIC; fig|582680.7.peg.2860; -.
DR OrthoDB; 9806388at2; -.
DR Proteomes; UP000033448; Unassembled WGS sequence.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
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; XAA-PRO AMINOPEPTIDASE 3; 1.
DR PANTHER; PTHR43226:SF4; 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:KJL20877.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KJL20877.1};
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:UP000033448}.
FT DOMAIN 52..190
FT /note="Aminopeptidase P N-terminal"
FT /evidence="ECO:0000259|SMART:SM01011"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 476 AA; 51911 MW; 0F86DB49EBBDCA1B CRC64;
MTSEHDTIEQ QGDAATATTS TSANRRQPFP QGFLDTISTG WAERPETLPA PRAQAPYAAK
RRDALSAAFP GKRLVIPAGS LKQRSNDTDY PFRAHSAFAH LTGWAADAEP DSLLVFEPTT
DGHDVTLYFR ERADRTTSEF YSDATIGEFW IGPRPALAGV AADLGLATAH LDDFAAGEHD
LVVDEDAELT QVVSELRLIK DEYEIAEMRR AVEITANGFD DIVRDLPRAV AHPRGERIVE
GVFHQRARSD GNWEGYDTIA ASGPHACYLH WTRNDGAVLP GDLILIDAGA EADSLYTADI
TRTLPVSGTF SDVQRRIYDT VVEAADAAFG AAKIGVPFRE VHAAAMDVIA RRTAEWGLLP
VTAEEALDAD KGGQHRRYMV HGTSHHLGID VHDCAQARRE MYYDGLIQEG MVFTIEPGLY
FQIDDVTVPE EYRGIGVRIE DDILITADGP VNLSAGIPRT SAEIEAWIAT VQGAAS
//
