ID A0A0R2A9H8_9LACO Unreviewed; 410 AA.
AC A0A0R2A9H8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Aminopeptidase PepS {ECO:0000313|EMBL:KRM64024.1};
GN ORFNames=FC14_GL000034 {ECO:0000313|EMBL:KRM64024.1};
OS Ligilactobacillus agilis DSM 20509.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Ligilactobacillus.
OX NCBI_TaxID=1423718 {ECO:0000313|EMBL:KRM64024.1, ECO:0000313|Proteomes:UP000051008};
RN [1] {ECO:0000313|EMBL:KRM64024.1, ECO:0000313|Proteomes:UP000051008}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20509 {ECO:0000313|EMBL:KRM64024.1,
RC ECO:0000313|Proteomes:UP000051008};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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:KRM64024.1}.
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DR EMBL; AYYP01000044; KRM64024.1; -; Genomic_DNA.
DR RefSeq; WP_056976801.1; NZ_AYYP01000044.1.
DR AlphaFoldDB; A0A0R2A9H8; -.
DR PATRIC; fig|1423718.3.peg.36; -.
DR Proteomes; UP000051008; 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:KRM64024.1}; 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:UP000051008}.
SQ SEQUENCE 410 AA; 44981 MW; 7CCCBFA1FB000694 CRC64;
MTMTNFEEKL AKYAQLIIEV GVNVQKGQAV VLYISVTQQK LAHLLVEKAY QAGASEVIIK
WSDTFSNRQF LKYASAERLS NAPEYIVKEA EYIVAKKAAR ISVVSEDPGA YAGIDQKRIA
QNQKTMGQAL LSVRKATQNN DLSWTVVGAA DEAWAKKVFP NLAGQDAVSR LWEEIFKTCR
INEADPIAAW KAHDQQLRSK AEWLNQEQFS ALHYTSPLTD FTVGLPKNHI WEAASSLTPD
GISFMANMPT EEVFTAADCH RIDGYICSTK PLSYAGNILE DMKFTFKDGQ IVEATAKKGQ
AVLDHLLELP GARSLGEVSL VPDPSPISQS GITFFNTLFD ENASDHLALG AAYPTNVQGG
TNMTDEELLA HGVNVSQTHV DFMVGSSDMN IDGIKADGSL VPVFRNGDWA
//
