ID Q09AR6_STIAD Unreviewed; 391 AA.
AC Q09AR6;
DT 31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 92.
DE SubName: Full=Carboxypeptidase G2 {ECO:0000313|EMBL:EAU68777.1};
DE SubName: Full=Peptidase M20 {ECO:0000313|EMBL:ADO74854.1};
GN OrderedLocusNames=STAUR_7098 {ECO:0000313|EMBL:ADO74854.1};
GN ORFNames=STIAU_8511 {ECO:0000313|EMBL:EAU68777.1};
OS Stigmatella aurantiaca (strain DW4/3-1).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Archangiaceae; Stigmatella.
OX NCBI_TaxID=378806 {ECO:0000313|EMBL:EAU68777.1, ECO:0000313|Proteomes:UP000032702};
RN [1] {ECO:0000313|EMBL:EAU68777.1, ECO:0000313|Proteomes:UP000032702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DW4/3-1 {ECO:0000313|EMBL:EAU68777.1,
RC ECO:0000313|Proteomes:UP000032702};
RA Nierman W.C.;
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADO74854.1, ECO:0000313|Proteomes:UP000001351}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DW4/3-1 {ECO:0000313|EMBL:ADO74854.1,
RC ECO:0000313|Proteomes:UP000001351};
RX PubMed=21037205; DOI=10.1093/molbev/msq292;
RA Huntley S., Hamann N., Wegener-Feldbrugge S., Treuner-Lange A., Kube M.,
RA Reinhardt R., Klages S., Muller R., Ronning C.M., Nierman W.C.,
RA Sogaard-Andersen L.;
RT "Comparative genomic analysis of fruiting body formation in Myxococcales.";
RL Mol. Biol. Evol. 28:1083-1097(2011).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
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DR EMBL; CP002271; ADO74854.1; -; Genomic_DNA.
DR EMBL; AAMD01000012; EAU68777.1; -; Genomic_DNA.
DR RefSeq; WP_002611521.1; NZ_AAMD01000012.1.
DR STRING; 378806.STAUR_7098; -.
DR KEGG; sur:STAUR_7098; -.
DR PATRIC; fig|378806.16.peg.8155; -.
DR eggNOG; COG0624; Bacteria.
DR HOGENOM; CLU_021802_7_1_7; -.
DR OrthoDB; 9809784at2; -.
DR Proteomes; UP000001351; Chromosome.
DR Proteomes; UP000032702; Unassembled WGS sequence.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 Carboxypeptidase {ECO:0000313|EMBL:EAU68777.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000313|EMBL:EAU68777.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 185..282
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 391 AA; 40886 MW; CE9A80898E29638B CRC64;
MREMGEAAAH WLEDRAGEMD EALGALVQVN SYTENPEGGR KLGGLLRECF AVPGLSAEVV
LSARFADHLV FRSAGRPGAR PVALVGHLDT VYPPGRFEGY RKDGPLRRGP GVLDMKGGLV
VMAWALRALA ASGGLQALPP LRLVVVSDEE VGSPEGQGVV REAIGGASAC LVFEAGREGD
AIITQRKGTG AVKVVAHGKA AHAGNAYAEG ANALWALARF VDGAQQLTDI PRGLTVNVGR
VVGGQGKNTI PDRAEADVDL RFCTREEGED LVRRLQHLAT QASQGIPGTR LELVGGVARD
PLERTEASAA LMAAYGRCAH ASGLGHAESP RVGGGSDAST AFGLGIPSID GLGPRGKGFH
TVEEYIELET LRAKAQALAR FLASWESSPP F
//