ID A3K339_9RHOB Unreviewed; 375 AA.
AC A3K339;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Putative carboxypeptidase {ECO:0000313|EMBL:EBA08598.1};
GN ORFNames=SSE37_17338 {ECO:0000313|EMBL:EBA08598.1};
OS Sagittula stellata E-37.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Sagittula.
OX NCBI_TaxID=388399 {ECO:0000313|EMBL:EBA08598.1, ECO:0000313|Proteomes:UP000005713};
RN [1] {ECO:0000313|EMBL:EBA08598.1, ECO:0000313|Proteomes:UP000005713}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E-37 {ECO:0000313|EMBL:EBA08598.1,
RC ECO:0000313|Proteomes:UP000005713};
RA Moran M.A., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (JUN-2006) 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:EBA08598.1}.
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DR EMBL; AAYA01000005; EBA08598.1; -; Genomic_DNA.
DR AlphaFoldDB; A3K339; -.
DR eggNOG; COG0624; Bacteria.
DR Proteomes; UP000005713; 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 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 Carboxypeptidase {ECO:0000313|EMBL:EBA08598.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000313|EMBL:EBA08598.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005713};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 171..260
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT ACT_SITE 77
FT /evidence="ECO:0000256|PIRSR:PIRSR037238-1"
FT ACT_SITE 135
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR037238-1"
SQ SEQUENCE 375 AA; 39337 MW; D425EB597DF126A0 CRC64;
MMTSEDILKE IMRWVELDTP TGSVATIAQL VDLIASELEP LGCEIERIPG RDGMGDHLIA
RFAGGNGPGV LVTSHIDTVC APGTVEIHRD GDRQYGPGIA DMKGGGYLAL CAMRNIVESG
TALPGPVTLI YNSDEEIGSP TSHAMIQAEA RKHGAALIPE PARGDEAITF RKGRAKYTLE
FQGRESHAGS AFADGRSAIL QMARTIGVLE AMTDLETETT VNVGRVRGGT EPNVVAGHAA
CDIDVRFADD ALGHAVEARL KGLGSDDPEV SITVSGEIEK PSLARTPETL AMFARASEIN
AGLGAPMVET RSGGGSDGNF TCAAGVPTLD GLGAIGNNWH SPQEHILVAP LARREALLRE
LILTYAGARP TGDNS
//