ID W1F274_ECOLX Unreviewed; 697 AA.
AC W1F274;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Nondeblocking aminopeptidase YpdE (X-X-[^PR]-specific) {ECO:0000313|EMBL:CDL27783.1};
OS Escherichia coli ISC7.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=1432555 {ECO:0000313|EMBL:CDL27783.1, ECO:0000313|Proteomes:UP000019199};
RN [1] {ECO:0000313|EMBL:CDL27783.1, ECO:0000313|Proteomes:UP000019199}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISC7 {ECO:0000313|EMBL:CDL27783.1,
RC ECO:0000313|Proteomes:UP000019199};
RA Barisic I., Mitteregger D., Hirschl A.M., Noehammer C., Wiesinger-Mayr H.;
RT "Antibiotic resistance diversity of beta-lactamase producers in the General
RT Hospital Vienna.";
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase M42 family.
CC {ECO:0000256|ARBA:ARBA00006272}.
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:CDL27783.1}.
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DR EMBL; CBWN010000103; CDL27783.1; -; Genomic_DNA.
DR AlphaFoldDB; W1F274; -.
DR Proteomes; UP000019199; Unassembled WGS sequence.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd01092; APP-like; 1.
DR CDD; cd05638; M42; 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 Gene3D; 2.40.30.40; Peptidase M42, domain 2; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 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; IPR008007; Peptidase_M42.
DR InterPro; IPR023367; Peptidase_M42_dom2.
DR PANTHER; PTHR32481; AMINOPEPTIDASE; 1.
DR PANTHER; PTHR32481:SF0; AMINOPEPTIDASE YPDE-RELATED; 1.
DR Pfam; PF01321; Creatinase_N; 1.
DR Pfam; PF00557; Peptidase_M24; 1.
DR Pfam; PF05343; Peptidase_M42; 1.
DR SUPFAM; SSF101821; Aminopeptidase/glucanase lid domain; 1.
DR SUPFAM; SSF55920; Creatinase/aminopeptidase; 1.
DR SUPFAM; SSF53092; Creatinase/prolidase N-terminal domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW ECO:0000313|EMBL:CDL27783.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670}.
FT DOMAIN 4..125
FT /note="Creatinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01321"
FT DOMAIN 134..306
FT /note="Peptidase M24"
FT /evidence="ECO:0000259|Pfam:PF00557"
SQ SEQUENCE 697 AA; 75971 MW; 3CD95F817861BD32 CRC64;
MTLLASLRDW LKAQQLDAVL LSSRQNKQPH LGISTGSGYV VISRESAHIL VDSRYFVEVE
ARAQGYQLHL LDATNTLTTI VNQIIADEQL QTLGFEGQQV SWETAHRWKS ELNAKLVSAT
PDVLRQIKTP EEVEIIRLAC GIADRGAEHI RRFIQAGMSE REIAAELEWF MRQQGAEKAS
FDTIVASGWR GALPHGKASD KIVAAGEFVT LDFGALYQGY CSDMTRTLLV NGEGVSAESH
PLFDVYQIVL QAQLAAISAI RPGVRCQQID DAARRVITEA GFGDYFGHNT GHAIGIEVHE
DPRFFTAGHH DATARHVADR GAGDLFARAR GRAHRRCCAG YPARRRSALR HAENSVAHGR
GIMDLSLLKA LSEADAIASS EQEVRQILLE EADRLQKEVR FDGLGSVLIR LNESTGPKVM
ICAHMDEVGF MVRSISREGA IDVLPVGNVR MAARQLQPVR ITTREECKIP GLLDGDRQGN
DVSAMRVDIG ARSYDEVMQA GIRPGDRVTF DTTFQVLPHQ RVMGKAFDDR LGCYLLVTLL
RELHDAELPA EVWLVASSSE EVGLRGGQTA TRAVSPDVAI VLDTACWAKN FDYSAANHRQ
IGNGPMLVLS DKSLIAPPKL TAWIETVAAE IGVPLQADMF SNGGTDGGAV HLTGTGVPTV
VMGPATRHGH CAASIADCRD IFADAATFIC PYSTSYP
//