ID D1VU71_9FIRM Unreviewed; 410 AA.
AC D1VU71;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE SubName: Full=Thermophilic metalloprotease (M29) {ECO:0000313|EMBL:EFA89919.1};
DE EC=3.4.11.- {ECO:0000313|EMBL:EFA89919.1};
GN Name=pepS {ECO:0000313|EMBL:EFA89919.1};
GN ORFNames=HMPREF0628_1114 {ECO:0000313|EMBL:EFA89919.1};
OS Peptoniphilus lacrimalis 315-B.
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC Peptoniphilus.
OX NCBI_TaxID=596330 {ECO:0000313|EMBL:EFA89919.1, ECO:0000313|Proteomes:UP000005711};
RN [1] {ECO:0000313|EMBL:EFA89919.1, ECO:0000313|Proteomes:UP000005711}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=315-B {ECO:0000313|EMBL:EFA89919.1,
RC ECO:0000313|Proteomes:UP000005711};
RA Durkin A.S., Madupu R., Torralba M., Methe B., Sutton G., Strausberg R.L.,
RA Nelson K.E.;
RT "Genome Sequence of Peptoniphilus lacrimalis 315-B.";
RL Submitted (DEC-2009) 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:EFA89919.1}.
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DR EMBL; ADDO01000055; EFA89919.1; -; Genomic_DNA.
DR RefSeq; WP_004825291.1; NZ_ADDO01000055.1.
DR AlphaFoldDB; D1VU71; -.
DR eggNOG; COG2309; Bacteria.
DR Proteomes; UP000005711; 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:EFA89919.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EFA89919.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000313|EMBL:EFA89919.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:EFA89919.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005711}.
SQ SEQUENCE 410 AA; 46525 MW; 40AFA8C68952BF61 CRC64;
MNLEKMFDKY ADLVIKCALK IKAGDILVIR SPIEASSLTE NLVKKAYEEG AKKVQVDYSD
ENITKLKYTY ESEKTLSQVP EFLIEKENYF INKKAKYLSI TGGNPELFKG IDSSKIKAAN
VANGIAFKDF SEKLMSNYTS WCVIGAATKA WATKVFPDLD EDEAKLKLWE EIFYTVRLFD
DDPVESMNKH IENLDKYAEF LNKNNFRYLH YKSKKGTDLI VELPKGYIFV GSEEKNSFGE
DFVANVPSEE VFSLPHKYGV NGIVYNTKPL NHNGVIVDKF YLKFKDGKVI DFDAEVGLDE
LKNILSSAKD SDRLGEIALV PYDSPISKRN ILFFNTLYDE NASCHFALGK AYPTCLKGGE
NIDEKDYDKY GINDSIVHVD FMVGDESTQI TGQRWDGTIV KIFEDGNFAI
//
