ID A0A160KV62_9MICO Unreviewed; 561 AA.
AC A0A160KV62;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Peptidase M28 {ECO:0008006|Google:ProtNLM};
GN ORFNames=A6122_2104 {ECO:0000313|EMBL:AND17228.1};
OS Rathayibacter tritici.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Rathayibacter.
OX NCBI_TaxID=33888 {ECO:0000313|EMBL:AND17228.1, ECO:0000313|Proteomes:UP000077071};
RN [1] {ECO:0000313|EMBL:AND17228.1, ECO:0000313|Proteomes:UP000077071}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCPPB 1953 {ECO:0000313|EMBL:AND17228.1,
RC ECO:0000313|Proteomes:UP000077071};
RA Park J., Lee H.-H., Lee S.-W., Seo Y.-S.;
RT "Complete genome sequence of Rathayibacter tritici NCPPB 1953.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP015515; AND17228.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A160KV62; -.
DR STRING; 33888.A6122_2104; -.
DR KEGG; rtn:A6122_2104; -.
DR PATRIC; fig|33888.3.peg.2341; -.
DR OrthoDB; 345880at2; -.
DR Proteomes; UP000077071; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008235; F:metalloexopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.50.30.30; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR045175; M28_fam.
DR InterPro; IPR046450; PA_dom_sf.
DR InterPro; IPR003137; PA_domain.
DR InterPro; IPR007484; Peptidase_M28.
DR PANTHER; PTHR12147; METALLOPEPTIDASE M28 FAMILY MEMBER; 1.
DR PANTHER; PTHR12147:SF55; PEPTIDE HYDROLASE; 1.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
DR SUPFAM; SSF52025; PA domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 4: Predicted;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022438};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022438};
KW Reference proteome {ECO:0000313|Proteomes:UP000077071};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..561
FT /note="Peptidase M28"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039473857"
FT TRANSMEM 530..553
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 116..204
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 227..442
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
FT REGION 455..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..494
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 503..519
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 561 AA; 56348 MW; E050855C4971F55D CRC64;
MIGAGALVAG LAFAPAANAV EPVAFAATVT VDGIMTHLEA LQAIADANGG TRAIGTPGYE
LSGEYVEAVL ASAGYTTTRQ DFTTSTQTID AFTLTTGTGA VGTPMEFTPS TPEGGVTGEL
IAPVDPLGCS ADAWTGLDAT GKVALVSRGS CSFLEKSIAA GAAGASAILI YDNAPSDALN
GTFGAQDEAA VPGVGLTQAE GQALLAALPA SVSVLIEQTT TEVATFNIVT ETPGGDHDNV
VMLGAHLDSV PAGPGINDNG SGSATLLETA VQLAAAGETT NAVRFAWWGA EEVGLVGSYT
YVDSLSEEDA STIATYMNFD MVASPNYVIS VYDANESTYE APVEVPAGSI ATEKAFTDYF
DSIDQPWIDT AFDGRSDYDG FISVGIPSSG VFTGADDVKT EEEVALFGGT AGITHDPNYH
SAADDIDNIN QEALGITSKA IAFVTASFAA DTSAIDAEKN PTTPTPEPSA TPTAGPPVPP
IAEPTVPPTT APTTAPTNAP TNAPTPGSTP APVAPHPGGR PPLASTGADI GLPLGLGALL
VAGGIGGLLL AALRRQRAER G
//
