ID A0A2V1MXZ1_9LACO Unreviewed; 411 AA.
AC A0A2V1MXZ1;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE SubName: Full=Aminopeptidase {ECO:0000313|EMBL:PWF99910.1};
GN ORFNames=DCM90_02865 {ECO:0000313|EMBL:PWF99910.1};
OS Levilactobacillus bambusae.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Levilactobacillus.
OX NCBI_TaxID=2024736 {ECO:0000313|EMBL:PWF99910.1, ECO:0000313|Proteomes:UP000245080};
RN [1] {ECO:0000313|EMBL:PWF99910.1, ECO:0000313|Proteomes:UP000245080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BS-W1 {ECO:0000313|EMBL:PWF99910.1,
RC ECO:0000313|Proteomes:UP000245080};
RA Wang L.-T.;
RT "Lactobacillus bambusae sp. nov., isolated from a traditional fermented Ma-
RT bamboo shoots of Taiwan.";
RL Int. J. Syst. Evol. Microbiol. 0:0-0(2018).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PWF99910.1}.
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DR EMBL; QCXQ01000002; PWF99910.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V1MXZ1; -.
DR OrthoDB; 9803993at2; -.
DR Proteomes; UP000245080; Unassembled WGS sequence.
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:PWF99910.1}; 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:UP000245080}.
SQ SEQUENCE 411 AA; 45110 MW; C6274F9E8F3AFF14 CRC64;
MNDSNFERDL KKYAYLIVET GANVQPGQTV VVAIAVDQQP LAHLIMEAAY ERGANEVIID
WKDDLTTKNY LLHTTEKSLA TAPRYLEVQA KDRAADRVTR ISVVSSAPDA YAEVAADRIS
AYQAARGRAL APVRKATQNN DLSWVVVAAA GRKWAQEVFS DLTDQAAVSA LWQEIFKTTR
IDQPDPEAAW DQHVKALGLK ADWLNHQQFD ALHYVAPHTD LTVGLPQHHL WEAAGSYDAA
HHFFIPNMPT EEVFTAPDRL RVNGTVRSTR PLSYAGTLIN QLQLTFKNGK IVEATAAEGE
HVLQQLIETD AGSQYLGEAA LVPDNSPISQ SGIVFLNTLF DENAADHLAI GAAYPTNIRN
GSTFTDSELL NAGLNISQVH VDFMIGSSKM AVDGLDKKGQ VTPIMRNGNW V
//
