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Database: UniProt
Entry: L0EUH5_LIBCB
LinkDB: L0EUH5_LIBCB
Original site: L0EUH5_LIBCB 
ID   L0EUH5_LIBCB            Unreviewed;       419 AA.
AC   L0EUH5;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   SubName: Full=Aminopeptidase S (Leu, Val, Phe, Tyr preference) {ECO:0000313|EMBL:AGA64016.1};
DE            EC=3.4.11.24 {ECO:0000313|EMBL:AGA64016.1};
GN   OrderedLocusNames=B488_00230 {ECO:0000313|EMBL:AGA64016.1};
OS   Liberibacter crescens (strain BT-1).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Liberibacter.
OX   NCBI_TaxID=1215343 {ECO:0000313|EMBL:AGA64016.1, ECO:0000313|Proteomes:UP000010799};
RN   [1] {ECO:0000313|EMBL:AGA64016.1, ECO:0000313|Proteomes:UP000010799}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BT-1 {ECO:0000313|EMBL:AGA64016.1,
RC   ECO:0000313|Proteomes:UP000010799};
RX   PubMed=23408754; DOI=10.4056/sigs.3326772;
RA   Leonard M.T., Fagen J.R., Davis-Richardson A.G., Davis M.J., Triplett E.W.;
RT   "Complete genome sequence of Liberibacter crescens BT-1.";
RL   Stand. Genomic Sci. 7:271-283(2012).
CC   -!- COFACTOR:
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC         Evidence={ECO:0000256|ARBA:ARBA00001941};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the peptidase M29 family.
CC       {ECO:0000256|ARBA:ARBA00008236}.
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DR   EMBL; CP003789; AGA64016.1; -; Genomic_DNA.
DR   RefSeq; WP_015272443.1; NC_019907.1.
DR   AlphaFoldDB; L0EUH5; -.
DR   STRING; 1215343.B488_00230; -.
DR   KEGG; lcc:B488_00230; -.
DR   PATRIC; fig|1215343.11.peg.25; -.
DR   eggNOG; COG2309; Bacteria.
DR   HOGENOM; CLU_054346_1_0_5; -.
DR   Proteomes; UP000010799; Chromosome.
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   Gene3D; 3.40.1830.10; Thermophilic metalloprotease (M29); 1.
DR   InterPro; IPR035097; M29_N-terminal.
DR   InterPro; IPR000787; Peptidase_M29.
DR   PANTHER; PTHR34448; AMINOPEPTIDASE; 1.
DR   PANTHER; PTHR34448:SF3; AMINOPEPTIDASE AMPS; 1.
DR   Pfam; PF02073; Peptidase_M29; 1.
DR   PRINTS; PR00919; THERMOPTASE.
DR   SUPFAM; SSF144052; Thermophilic metalloprotease-like; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW   ECO:0000313|EMBL:AGA64016.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:AGA64016.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010799}.
SQ   SEQUENCE   419 AA;  46092 MW;  23157284CD593FB8 CRC64;
     MNFSSHLSVP HIDMICLDKL AEIAVKVGLN IQDGQSVIIT APIESLPLTR LITKHAYLSG
     AGLVSIFYTD EETTLIRYQY SNHNGLSKAA DWLYKGMAQA YSAGTARLAI SGSNPVLLAD
     QDPDKIMRVD RAYFTSYKPA LEKISNFDIN WSIISYPSAS WARVVYPDDP EPIAIAKLAK
     AIFAISRANV DDPIEAWKKH NNFLHKRAKL LNDKHFSEIH FIGPGTFLKV GLVDGHLWQG
     GSSTAKNGVI CNTNIPTEEV FTTPHKLKVE GYVSSTKPLS YQGTLIDGIR VRFEEGRVVE
     AKALKNEAIF LKMLGSDSGA CRLGEVALVP NSSLVSKTGI LFYNTLFDEN ASSHIAFGQC
     YAKCFMNNSS LSSQQIEEQG GNTSIIHVDW MIGSNEIDVN GITKDGNSIP VMRKGEWVD
//
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