ID A0A1V4LMR4_9PSED Unreviewed; 444 AA.
AC A0A1V4LMR4;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Xaa-Pro aminopeptidase {ECO:0000313|EMBL:OPK08497.1};
GN ORFNames=BZ163_21740 {ECO:0000313|EMBL:OPK08497.1};
OS Pseudomonas sp. VI4.1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1941346 {ECO:0000313|EMBL:OPK08497.1, ECO:0000313|Proteomes:UP000189889};
RN [1] {ECO:0000313|EMBL:OPK08497.1, ECO:0000313|Proteomes:UP000189889}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VI4.1 {ECO:0000313|EMBL:OPK08497.1,
RC ECO:0000313|Proteomes:UP000189889};
RA Imperato V., Thijs S., Mcammond B., Douwen Y., Broeders P., Kowalkowski L.,
RA Gawronski S., Vangronsveld J.;
RT "Draft genome sequence of Pseudomonas yorbenii VI4.1, a hydrocarbonoclastic
RT isolate from crude oil contaminated soil in Bobrka, Poland.";
RL Submitted (FEB-2017) 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}.
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:OPK08497.1}.
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DR EMBL; MULM01000169; OPK08497.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V4LMR4; -.
DR Proteomes; UP000189889; 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 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.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000313|EMBL:OPK08497.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670}.
FT DOMAIN 4..138
FT /note="Aminopeptidase P N-terminal"
FT /evidence="ECO:0000259|SMART:SM01011"
SQ SEQUENCE 444 AA; 49294 MW; 91E5BEEBB8658B87 CRC64;
MIHIPKSEYS RRRKALMAQM VPNSIAILPA AAVAIRNRDV EHVYRQDSDF QYLSGFPEPQ
AVIVLMPGRE HGEYVLFCRE RNAERELWDG LRAGQEGAIR DFGADDAFPI TDIDDILPGL
IEGRDRVYSA MGSNPEFDRH LMDWINVIRS KAHLGAQPPN EFIALDHLLH DMRLYKSAAE
VKVMREAARI SAQAHIRAMQ ASRAGLHEFS LEAELDYEFR KGGAKMPAYG SIVASGRNSC
ILHYQQNDAV LKDGDLVLID AGCEIDCYAS DITRTWPVNG KYSPEQKAIY ELVLAAQEAA
FAEIAPDKHW NQAHEATVRV ITAGLVKLGL LQGDVDELIA GEAHKAFYMH RAGHWLGMDV
HDVGEYKVGG EWRVLEVGMA LTVEPGIYIA PDNQNVAKKW RGIGVRIEDD VVVTKTGCEI
LTHGVPKTVA EIEALMAAAR THAA
//
