ID A0A081NU11_9BACL Unreviewed; 411 AA.
AC A0A081NU11;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Peptidase M29 {ECO:0000313|EMBL:KEQ21934.1};
GN ORFNames=ET33_30145 {ECO:0000313|EMBL:KEQ21934.1};
OS Paenibacillus tyrfis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1501230 {ECO:0000313|EMBL:KEQ21934.1, ECO:0000313|Proteomes:UP000028123};
RN [1] {ECO:0000313|EMBL:KEQ21934.1, ECO:0000313|Proteomes:UP000028123}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSt1 {ECO:0000313|EMBL:KEQ21934.1,
RC ECO:0000313|Proteomes:UP000028123};
RA Aw Y.K., Ong K.S., Gan H.M., Lee S.M.;
RT "Draft genome sequence of Paenibacillus sp. MSt1.";
RL Submitted (JUN-2014) 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:KEQ21934.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JNVM01000051; KEQ21934.1; -; Genomic_DNA.
DR RefSeq; WP_036692968.1; NZ_JNVM01000051.1.
DR AlphaFoldDB; A0A081NU11; -.
DR MEROPS; M29.002; -.
DR eggNOG; COG2309; Bacteria.
DR OrthoDB; 9803993at2; -.
DR Proteomes; UP000028123; 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:UP000028123}.
SQ SEQUENCE 411 AA; 46046 MW; D3251AB1D5FDE6C5 CRC64;
MEAFDRSLEK YAELVVRVGA NVQPGQVLHI ESPLEAAPFT RKVVQKAYEA GAKYVQVQWD
DEEVTRNRFL YAPDESFDYY PQWMPAMMEQ LAENGGALIN IKVPDPELYK GIDSDKVTRA
TKAAAVARET FQSYVRNKKF SWCLVKAPTR AWAAKVFPEL PEEERVRVMW DTIFKMNRVD
ADDPVAAWKE HIGRLKQVKE KLNEKKYKKL HYRAPGTDLS VELPEGHIWH GGGTTDDQGV
YFVANMPTEE VYTMPLRTGV NGTVTSTKPL NLNGRLVDKF ALTFEGGKVV SYTAEVGLEY
LDALLKTDEG AKYLGEVALV PHHSPISNLN RVFYNTGIDE NASCHFAVGS AYPFTIENGT
KMTKEELLAK GANVSLTHVD FMVGSAELDI DGELPDGTRE PVFRQGNWAV G
//
