ID A0A1B8UXZ2_9BACL Unreviewed; 410 AA.
AC A0A1B8UXZ2;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=Peptidase M29 {ECO:0000313|EMBL:OBY81132.1};
GN ORFNames=BBG47_02295 {ECO:0000313|EMBL:OBY81132.1};
OS Paenibacillus sp. KS1.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1849249 {ECO:0000313|EMBL:OBY81132.1, ECO:0000313|Proteomes:UP000092663};
RN [1] {ECO:0000313|EMBL:OBY81132.1, ECO:0000313|Proteomes:UP000092663}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KS1 {ECO:0000313|EMBL:OBY81132.1,
RC ECO:0000313|Proteomes:UP000092663};
RA Lata P., Govindarajan S., Qi F., Li J.-L., Sahoo M.K.;
RT "Deep sequencing identified Paenibacillus in Kanamycin resistant culture
RT isolate from epiphyte Tillandsia usneoides (Spanish moss) in central
RT Florida, USA.";
RL Submitted (JUN-2016) 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:OBY81132.1}.
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DR EMBL; MAIS01000004; OBY81132.1; -; Genomic_DNA.
DR RefSeq; WP_065290358.1; NZ_MAIS01000004.1.
DR AlphaFoldDB; A0A1B8UXZ2; -.
DR OrthoDB; 9803993at2; -.
DR Proteomes; UP000092663; 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:UP000092663}.
SQ SEQUENCE 410 AA; 45601 MW; 4E842650EE55CA5A CRC64;
MVNFEQQLEK YAELIVKVGV NVQKDQDVFV NSSIEVAPLA RLVARKAYEA GARNVHIDWS
DEATTRLKFE NASDDVFTQF PEWEALKRNT FVDKGAAFIS IVSSSPDLLK GVDPQRIGNN
QKASGQALEH FRRCVQANKV SWTVVAASSR DWAAKVFPGV AVEEAVEKLW EAIFQSIRLN
SDNPVQAWTE HNETLHKKVE VLNSKHFHKL HYTAPGTDLT IELPEKHLWV GAGSVNEKDV
PFMANMPTEE VFTVPHKLGV NGYVSSTKPL SYGGNLIDNF KITFENGRIV KVEAEQGQEI
LQQLVDTDEG SHFLGEVALV PHQSPISESN ILFYNTLFDE NASNHLAIGS GYAFNVEGGT
KMSQEELEES GVNRSITHVD FMVGSADMDI DGIQKDGTTE PIFRKGNWAI
//
