ID G2EGT2_9FLAO Unreviewed; 402 AA.
AC G2EGT2;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 22-FEB-2023, entry version 41.
DE SubName: Full=Aminopeptidase P family protein {ECO:0000313|EMBL:EGV42314.1};
GN ORFNames=BZARG_2549 {ECO:0000313|EMBL:EGV42314.1};
OS Bizionia argentinensis JUB59.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Bizionia.
OX NCBI_TaxID=1046627 {ECO:0000313|EMBL:EGV42314.1, ECO:0000313|Proteomes:UP000003730};
RN [1] {ECO:0000313|EMBL:EGV42314.1, ECO:0000313|Proteomes:UP000003730}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JUB59 {ECO:0000313|EMBL:EGV42314.1,
RC ECO:0000313|Proteomes:UP000003730};
RX PubMed=18842857; DOI=10.1099/ijs.0.65599-0;
RA Bercovich A., Vazquez S.C., Yankilevich P., Coria S.H., Foti M.,
RA Hernandez E., Vidal A., Ruberto L., Melo C., Marenssi S., Criscuolo M.,
RA Memoli M., Arguelles M., Mac Cormack W.P.;
RT "Bizionia argentinensis sp. nov., isolated from surface marine water in
RT Antarctica.";
RL Int. J. Syst. Evol. Microbiol. 58:2363-2367(2008).
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:EGV42314.1}.
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DR EMBL; AFXZ01000065; EGV42314.1; -; Genomic_DNA.
DR RefSeq; WP_008639325.1; NZ_AFXZ01000065.1.
DR AlphaFoldDB; G2EGT2; -.
DR STRING; 1046627.BZARG_2549; -.
DR PATRIC; fig|1046627.3.peg.2709; -.
DR eggNOG; COG0006; Bacteria.
DR OrthoDB; 9806388at2; -.
DR Proteomes; UP000003730; Unassembled WGS sequence.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008235; F:metalloexopeptidase activity; IEA:UniProt.
DR GO; GO:0046914; F:transition metal ion binding; IEA:UniProt.
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; IPR001714; Pept_M24_MAP.
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 PRINTS; PR00599; MAPEPTIDASE.
DR SUPFAM; SSF55920; Creatinase/aminopeptidase; 1.
DR SUPFAM; SSF53092; Creatinase/prolidase N-terminal domain; 1.
DR PROSITE; PS00491; PROLINE_PEPTIDASE; 1.
PE 4: Predicted;
KW Aminopeptidase {ECO:0000313|EMBL:EGV42314.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000313|EMBL:EGV42314.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000003730}.
FT DOMAIN 39..167
FT /note="Creatinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01321"
FT DOMAIN 181..383
FT /note="Peptidase M24"
FT /evidence="ECO:0000259|Pfam:PF00557"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..33
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 402 AA; 44885 MW; 8D5C2764B400E2C5 CRC64;
MNSNRKYGIG GSKPEQELLK LSEPTKKPSP IDGKEFQSRI DKACESLKKK GLDALYINAG
TNLQYFTNTL WNPSERLVGA ILFADGTLKY VVPEFEIGTF NDFIGIDGEL IPWAEHEWPV
EKIAEVVPEG THLAVDDSTA FTMISRFQEN KKFTISSAEE LIRDIRLLKS EAEIAHIQYP
MNLTMQVHQA VARILKPGIT TAEVESFIHK AHQKLGIASG SYFCIVLFGK DSSFPHGVKT
PKPLEENDIV LVDTGCKFKG YLSDITRTYI YGDATDKEKK IWVNEKSAQL AAFHAAQLGK
PCGHIDDQVR VQLEKDGLGP DYDLPGLPHR TGHGIGLEIH EHPFILRGND LKLQVGMAFS
IEPMIVVPDE FGVRLEDHIY MTEAGPKWFT EPAHSIENPF GV
//
