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Database: UniProt
Entry: G7UW64_PSEUP
LinkDB: G7UW64_PSEUP
Original site: G7UW64_PSEUP 
ID   G7UW64_PSEUP            Unreviewed;       572 AA.
AC   G7UW64;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   SubName: Full=Putative aminopeptidase {ECO:0000313|EMBL:AER57722.1};
GN   OrderedLocusNames=DSC_15390 {ECO:0000313|EMBL:AER57722.1};
OS   Pseudoxanthomonas spadix (strain BD-a59).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Pseudoxanthomonas.
OX   NCBI_TaxID=1045855 {ECO:0000313|EMBL:AER57722.1, ECO:0000313|Proteomes:UP000005870};
RN   [1] {ECO:0000313|EMBL:AER57722.1, ECO:0000313|Proteomes:UP000005870}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BD-a59 {ECO:0000313|EMBL:AER57722.1,
RC   ECO:0000313|Proteomes:UP000005870};
RX   PubMed=22207748; DOI=10.1128/JB.06436-11;
RA   Lee S.H., Jin H.M., Lee H.J., Kim J.M., Jeon C.O.;
RT   "Complete Genome Sequence of the BTEX-Degrading Bacterium Pseudoxanthomonas
RT   spadix BD-a59.";
RL   J. Bacteriol. 194:544-544(2012).
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DR   EMBL; CP003093; AER57722.1; -; Genomic_DNA.
DR   RefSeq; WP_014161894.1; NC_016147.2.
DR   AlphaFoldDB; G7UW64; -.
DR   STRING; 1045855.DSC_15390; -.
DR   KEGG; psd:DSC_15390; -.
DR   eggNOG; COG2234; Bacteria.
DR   HOGENOM; CLU_019932_2_1_6; -.
DR   OMA; VANINMD; -.
DR   OrthoDB; 9778250at2; -.
DR   Proteomes; UP000005870; Chromosome.
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   CDD; cd05660; M28_like_PA; 1.
DR   CDD; cd04821; PA_M28_1_2; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 2.
DR   InterPro; IPR045175; M28_fam.
DR   InterPro; IPR007484; Peptidase_M28.
DR   PANTHER; PTHR12147:SF51; ALKALINE PHOSPHATASE ISOZYME CONVERSION PROTEIN; 1.
DR   PANTHER; PTHR12147; METALLOPEPTIDASE M28 FAMILY MEMBER; 1.
DR   Pfam; PF04389; Peptidase_M28; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   Aminopeptidase {ECO:0000313|EMBL:AER57722.1};
KW   Hydrolase {ECO:0000313|EMBL:AER57722.1};
KW   Protease {ECO:0000313|EMBL:AER57722.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005870};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..572
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003504415"
FT   DOMAIN          318..533
FT                   /note="Peptidase M28"
FT                   /evidence="ECO:0000259|Pfam:PF04389"
FT   REGION          19..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   572 AA;  61551 MW;  80592869A0863598 CRC64;
     MSRTLLLGLA ALTALSACKK PDPAPAASTP PVQTAAAPDA PHAFSPQITA ADFAERVKTL
     SSDAFQGRAP GSPGEDMTVA YIAAQMQRIG LKPGNGDSWS QDVPMVETTA DPSTTLTVTQ
     ADGSTQTLSF GDQMVIGTRS GKPQVSIRDS ELVFVGYGVD APEQKWNDYG SAKRWEGKTV
     VMLVNDPGFH TDDAALFDGK KMTYYGRWTY KFEEAARKGA DAAIIIHDPL GASYGWDVVK
     NSWAGAQYDL PARDDPEPRL PAQGWITQDV ARALFAKAGL DLDQAYKDAS RRGFKPVPLK
     ARLSLDLNST IAEKQSRNVI GVLPGSEQPD QAVLYMAHWD HLGKHEGEDG DNIYNGAVDN
     ATGVAGILEV AEAFAHQDPK PKRSVVFLAV TLEESGLLGS KYYVAHPTFP LDRIAGVINL
     DAMSVAGKAR DVTVTGYGAS QLEDILKPLA EMQGRTLHAE SSPQSGFYFR SDHFNFAKAG
     VPALYTDGGD DLVEGGKAAG EAYAKDYGEH RYHSPADEYD PASWKLDGTV QDLELVYGVG
     KSLASDGQWP NWYEGNPFKA ARDRMMKAPA GK
//
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