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
//