ID A1HQW5_9FIRM Unreviewed; 399 AA.
AC A1HQW5;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE SubName: Full=Peptidase M20 {ECO:0000313|EMBL:EAX47673.1};
GN ORFNames=TcarDRAFT_1095 {ECO:0000313|EMBL:EAX47673.1};
OS Thermosinus carboxydivorans Nor1.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC Thermosinus.
OX NCBI_TaxID=401526 {ECO:0000313|EMBL:EAX47673.1, ECO:0000313|Proteomes:UP000005139};
RN [1] {ECO:0000313|EMBL:EAX47673.1, ECO:0000313|Proteomes:UP000005139}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nor1 {ECO:0000313|EMBL:EAX47673.1,
RC ECO:0000313|Proteomes:UP000005139};
RG US DOE Joint Genome Institute (JGI-ORNL);
RA Larimer F., Land M., Hauser L.;
RT "Annotation of the draft genome assembly of Thermosinus carboxydivorans
RT Nor1.";
RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EAX47673.1, ECO:0000313|Proteomes:UP000005139}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nor1 {ECO:0000313|EMBL:EAX47673.1,
RC ECO:0000313|Proteomes:UP000005139};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Bruce D., Pitluck S., Richardson P.;
RT "Sequencing of the draft genome and assembly of Thermosinus carboxydivorans
RT Nor1.";
RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000256|PIRSR:PIRSR001123-2};
CC Note=Binds 2 divalent metal cations per subunit.
CC {ECO:0000256|PIRSR:PIRSR001123-2};
CC -!- SIMILARITY: Belongs to the peptidase M42 family.
CC {ECO:0000256|PIRNR:PIRNR001123}.
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:EAX47673.1}.
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DR EMBL; AAWL01000008; EAX47673.1; -; Genomic_DNA.
DR RefSeq; WP_007289402.1; NZ_AAWL01000008.1.
DR AlphaFoldDB; A1HQW5; -.
DR eggNOG; COG0624; Bacteria.
DR OrthoDB; 9792335at2; -.
DR Proteomes; UP000005139; Unassembled WGS sequence.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 2.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR InterPro; IPR008007; Peptidase_M42.
DR PANTHER; PTHR43808; ACETYLORNITHINE DEACETYLASE; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR PIRSF; PIRSF001123; PepA_GA; 3.
DR SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR001123-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000005139}.
FT DOMAIN 177..278
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT BINDING 79
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
SQ SEQUENCE 399 AA; 43016 MW; F3BE574FDF6F3197 CRC64;
MDIARLTEVT AQNLEYAVKL AQKMVQTPSL SGQEKELAEL TRQTMEQLRF DEVYIDEVGN
VIGRIKGRGG GRSVMFNCHL DTVAAGDPAA WKYPPFAGVI ADGALWGLGA SDTKAAFACQ
IVAAAALKEA GMLPTGDIWV VGVVHEETSG FGSRYLAKKL APDVVILGEA SDNQIKIGHR
GRMQFDIYFK GKSTHASVPA RGVNPHFAAA RLLLQIERLK MQADPFFGES SVAPTLYVTD
QTSSNVTPGQ VVLSLDWRNI PGETEENIRR RLEQVVAECL IPGVTARIEL KMRDVGCYTG
YKGVAPAGEP SFATPPDDPI VLAVQQALAA VFNREVSIGV CGFATDGGHF RAEGSKVIIF
APSEERYCHT TEDSVSIEKM REAILGNMAL ALCLGAENC
//
