ID B0P6M0_9FIRM Unreviewed; 393 AA.
AC B0P6M0;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=Peptidase dimerization domain protein {ECO:0000313|EMBL:EDS12845.1};
GN ORFNames=ANACOL_00398 {ECO:0000313|EMBL:EDS12845.1};
OS Anaerotruncus colihominis DSM 17241.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Anaerotruncus.
OX NCBI_TaxID=445972 {ECO:0000313|EMBL:EDS12845.1, ECO:0000313|Proteomes:UP000003803};
RN [1] {ECO:0000313|EMBL:EDS12845.1, ECO:0000313|Proteomes:UP000003803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17241 {ECO:0000313|EMBL:EDS12845.1,
RC ECO:0000313|Proteomes:UP000003803};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Anaerotruncus colihominis(DSM 17241).";
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EDS12845.1, ECO:0000313|Proteomes:UP000003803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17241 {ECO:0000313|EMBL:EDS12845.1,
RC ECO:0000313|Proteomes:UP000003803};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
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:EDS12845.1}.
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DR EMBL; ABGD02000005; EDS12845.1; -; Genomic_DNA.
DR RefSeq; WP_006873807.1; NZ_DS544175.1.
DR AlphaFoldDB; B0P6M0; -.
DR STRING; 169435.ERS852551_00581; -.
DR GeneID; 72463075; -.
DR eggNOG; COG0624; Bacteria.
DR HOGENOM; CLU_021802_7_0_9; -.
DR Proteomes; UP000003803; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd03885; M20_CPDG2; 1.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR001261; ArgE/DapE_CS.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR017150; Pept_M20_glutamate_carboxypep.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR PANTHER; PTHR43808; ACETYLORNITHINE DEACETYLASE; 1.
DR PANTHER; PTHR43808:SF9; BLL0789 PROTEIN; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR PIRSF; PIRSF037238; Carboxypeptidase_G2; 1.
DR SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS00758; ARGE_DAPE_CPG2_1; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 186..285
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT ACT_SITE 89
FT /evidence="ECO:0000256|PIRSR:PIRSR037238-1"
FT ACT_SITE 149
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR037238-1"
SQ SEQUENCE 393 AA; 42886 MW; 3EA2E8F95EB5DBA6 CRC64;
MGKDLSAAYA YIDEIRDETI ALYKEFVNRE SWSKTPDKVR IFSDFLKGEM EKAGFECRYV
PVGVNADTLV GILGKDRPGK PILFCGHMDT VFPTGMHPEN PFKIEDGKAY GPGVLDMKGG
ILIALTTVKA LNKIGYADRP IKFCFSGDEE INHTGSQGAE VIEAEAKGCL CAFNMETGMI
DNYLCTGRKG CLRYTVEVDG VETHSGNDFQ GGRSAIAEMA YKIIDFHNMT DLSIGNTCNI
GTITGGTVPN AVPAHCEVVL DMRYTTLSGK EKLLAQLDEI CKRTHIDGTT TKYAFLNKLD
VFETTDEGMR FFNFVKDIAK EYGLPEVSGR PLGGGSDAAS TTMAGVPTIC SCGVRGQWNH
TMKEYAVVDS IFDRSKMYVA AVANADRFAE GAD
//
