ID B7GHV9_ANOFW Unreviewed; 410 AA.
AC B7GHV9;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Leucyl aminopeptidase (Aminopeptidase T) {ECO:0000313|EMBL:ACJ33531.1};
GN Name=ampS {ECO:0000313|EMBL:ACJ33531.1};
GN OrderedLocusNames=Aflv_1155 {ECO:0000313|EMBL:ACJ33531.1};
OS Anoxybacillus flavithermus (strain DSM 21510 / WK1).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Anoxybacillus.
OX NCBI_TaxID=491915 {ECO:0000313|EMBL:ACJ33531.1, ECO:0000313|Proteomes:UP000000742};
RN [1] {ECO:0000313|EMBL:ACJ33531.1, ECO:0000313|Proteomes:UP000000742}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21510 / WK1 {ECO:0000313|Proteomes:UP000000742};
RX PubMed=19014707; DOI=10.1186/gb-2008-9-11-r161;
RA Saw J.H., Mountain B.W., Feng L., Omelchenko M.V., Hou S., Saito J.A.,
RA Stott M.B., Li D., Zhao G., Wu J., Galperin M.Y., Koonin E.V.,
RA Makarova K.S., Wolf Y.I., Rigden D.J., Dunfield P.F., Wang L., Alam M.;
RT "Encapsulated in silica: genome, proteome and physiology of the
RT thermophilic bacterium Anoxybacillus flavithermus WK1.";
RL Genome Biol. 9:R161.1-R161.16(2008).
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; CP000922; ACJ33531.1; -; Genomic_DNA.
DR RefSeq; WP_012574783.1; NC_011567.1.
DR AlphaFoldDB; B7GHV9; -.
DR STRING; 491915.Aflv_1155; -.
DR MEROPS; M29.002; -.
DR GeneID; 7037412; -.
DR KEGG; afl:Aflv_1155; -.
DR PATRIC; fig|491915.6.peg.1178; -.
DR eggNOG; COG2309; Bacteria.
DR HOGENOM; CLU_054346_1_0_9; -.
DR Proteomes; UP000000742; 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:ACJ33531.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000000742}.
SQ SEQUENCE 410 AA; 45556 MW; 2D653E09909D5045 CRC64;
MLEKQLQKYA ELAVRVGVNI QPGQTLFINA PLPSAPLVRE IAKKAYEAGA KHVHVEWSDE
EITYIKFKHA PEEALHEYPS WLAKGREEVA EKGGAFLSIY APNPDLLKDI DPARVAAATK
AASMALQHYR SRLMADHNCW SLIAVPTPAW AKKVFPHMNE DEAIAKLWDV IFQVTRVDQD
DPIAAWKTHN EKLARIVDYL NNKQYKQLIY DGPGTNLTVE LPDGHVWAGG AAKNTDGIVF
NPNMPTEEVF TMPHKDGTNG VVRNTKPLNY GGNIIDGFTL TFKDGKVVDF TAEVGYDTLK
HLLDTDEGAR RLGEIALVPH RSPISQSNLV FYNTLFDENA ASHLALGKAY PTNIEGGTNM
RTEELLARGA NDSLVHEDFM IGSHELNVDG VTKDGVREPI MRNGEWVISI
//
