ID A0A177ZW88_9BACI Unreviewed; 414 AA.
AC A0A177ZW88;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Peptidase M29 {ECO:0000313|EMBL:OAK71973.1};
GN ORFNames=ABB05_10080 {ECO:0000313|EMBL:OAK71973.1};
OS Lederbergia galactosidilytica.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lederbergia.
OX NCBI_TaxID=217031 {ECO:0000313|EMBL:OAK71973.1, ECO:0000313|Proteomes:UP000077881};
RN [1] {ECO:0000313|EMBL:OAK71973.1, ECO:0000313|Proteomes:UP000077881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G25-74 {ECO:0000313|EMBL:OAK71973.1,
RC ECO:0000313|Proteomes:UP000077881};
RA Zheng Z., Sun M.;
RT "Comparison of genome.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
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:OAK71973.1}.
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DR EMBL; LDJR01000044; OAK71973.1; -; Genomic_DNA.
DR RefSeq; WP_057989058.1; NZ_LDJR01000044.1.
DR AlphaFoldDB; A0A177ZW88; -.
DR PATRIC; fig|217031.6.peg.2139; -.
DR OrthoDB; 9803993at2; -.
DR Proteomes; UP000077881; 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 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:UP000077881}.
SQ SEQUENCE 414 AA; 45717 MW; 9293A71057E6C05D CRC64;
MALPNFEENL QKYAQLLVAK GINVQPGDWV KMTITVDQAP LARLITKEAY QLGAEKVIIK
WSDDEISKLH YLHQPVEVLT DIPDYEIQES EDHVLNHRVS RLSIVSSDPG LLNEVDPTKV
ATYQNVAGKA FQAQRIATQN DDLKWTVAAA AGAGWAAHVF PELSTSEEQV DALWDQIFKT
CRVYEDDPVA AWDEHKKLLN EKAAILNEIQ FDALHYKAPG TDLTLGLPKN HIWASAESYN
PKGEDFIANM PTEEVFTAPD THRMEGVVRS TKPLSYAGTL IEGIEVHFKD GKIVDISAEK
GDEAIKKLVQ DNDGATGLGE VALVPDPSPI SQSNIIFFNT LFDENASNHL AIGSAYPTTI
QGGTKMSQEE LLEHGMNTST VHVDFMIGSD KMDIDGIKQD GTVVPIFRNG DWAI
//
