ID A0A143HDV5_9BACL Unreviewed; 410 AA.
AC A0A143HDV5;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Peptidase M29 {ECO:0000313|EMBL:AMW99927.1};
GN ORFNames=ATY39_11140 {ECO:0000313|EMBL:AMW99927.1};
OS Rummeliibacillus stabekisii.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Rummeliibacillus.
OX NCBI_TaxID=241244 {ECO:0000313|EMBL:AMW99927.1, ECO:0000313|Proteomes:UP000076021};
RN [1] {ECO:0000313|EMBL:AMW99927.1, ECO:0000313|Proteomes:UP000076021}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PP9 {ECO:0000313|EMBL:AMW99927.1,
RC ECO:0000313|Proteomes:UP000076021};
RX PubMed=27231360;
RA da Mota F.F., Vollu R.E., Jurelevicius D., Seldin L.;
RT "Whole-Genome Sequence of Rummeliibacillus stabekisii Strain PP9 Isolated
RT from Antarctic Soil.";
RL Genome Announc. 4:0-0(2016).
RN [2] {ECO:0000313|Proteomes:UP000076021}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PP9 {ECO:0000313|Proteomes:UP000076021};
RA Ploux O.;
RL Submitted (MAR-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 ---------------------------------------------------------------------------
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; CP014806; AMW99927.1; -; Genomic_DNA.
DR RefSeq; WP_066789756.1; NZ_CP014806.1.
DR AlphaFoldDB; A0A143HDV5; -.
DR STRING; 241244.ATY39_11140; -.
DR KEGG; rst:ATY39_11140; -.
DR OrthoDB; 9803993at2; -.
DR Proteomes; UP000076021; Chromosome.
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:UP000076021}.
SQ SEQUENCE 410 AA; 45750 MW; D90B6CEE68853D9B CRC64;
MKTFQEKLDS YAELAVKVGV NLQPSQYLFI QASIDQAEFV RLVVKKAYEA EAKEVFVHYS
DDLLTRMHYD MAPEDAFGFF APWQAEEKNW LADHGAAFMT IKSQSPDLLK GVDPKKIALQ
QKAAGQALQH FRQASQSNKI SWNIIGTPSK EWAAKVFPDL EEDKQVPALW EAIFKTVRAD
LDNPLEAWEA HDEVLHEKVK YLNGKKYQKL HYTAPGTDLT IELPKGHVWS GGGSKNQNGK
PFMANIPTEE VFTAPHKDGV NGYITCTKPL SYAGTIIDHF TLTFENGRIV DVKAEEGEDV
LKNLVETDEG SHYLGEVALV PHDSPISNSG LLFYNTLFDE NASNHLAIGS AYAFCIENGT
TMTAAELEKQ GINQSIMHVD FMVGSKDMDI EGITEDGHSE AVFRNGNWAF
//
