ID A0A089YYF8_9PSED Unreviewed; 411 AA.
AC A0A089YYF8;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Glutamate carboxypeptidase {ECO:0000313|EMBL:AIS19482.1};
GN ORFNames=LT40_19635 {ECO:0000313|EMBL:AIS19482.1};
OS Pseudomonas rhizosphaerae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=216142 {ECO:0000313|EMBL:AIS19482.1, ECO:0000313|Proteomes:UP000029499};
RN [1] {ECO:0000313|EMBL:AIS19482.1, ECO:0000313|Proteomes:UP000029499}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16299 {ECO:0000313|EMBL:AIS19482.1};
RX PubMed=25483321; DOI=10.1016/j.jbiotec.2014.11.031;
RA Kwak Y., Jung B.K., Shin J.H.;
RT "Complete genome sequence of Pseudomonas rhizosphaerae IH5T (=DSM 16299T),
RT a phosphate-solubilizing rhizobacterium for bacterial biofertilizer.";
RL J. Biotechnol. 193:137-138(2015).
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DR EMBL; CP009533; AIS19482.1; -; Genomic_DNA.
DR RefSeq; WP_043192782.1; NZ_CP009533.1.
DR AlphaFoldDB; A0A089YYF8; -.
DR STRING; 216142.LT40_19635; -.
DR KEGG; prh:LT40_19635; -.
DR eggNOG; COG0624; Bacteria.
DR HOGENOM; CLU_021802_7_0_6; -.
DR OrthoDB; 9776600at2; -.
DR Proteomes; UP000029499; Chromosome.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:1901564; P:organonitrogen compound metabolic process; IEA:UniProt.
DR CDD; cd03885; M20_CPDG2; 1.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
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:SF10; BLL3749 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.
PE 4: Predicted;
KW Carboxypeptidase {ECO:0000313|EMBL:AIS19482.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000313|EMBL:AIS19482.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000029499};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..411
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001852336"
FT DOMAIN 208..306
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT ACT_SITE 112
FT /evidence="ECO:0000256|PIRSR:PIRSR037238-1"
FT ACT_SITE 173
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR037238-1"
SQ SEQUENCE 411 AA; 43724 MW; 7A208AF2DBA67C1B CRC64;
MLVRPSRITA IAAACLFSLS THAAELPAAD LYKQAQAEQP SYLETVKELV SVDTGTGQEK
GLATISALLV KRLKELGATV QTTPATPSVG DNIVGTFKGT GSKNFLLMVH YDTVFGPGTA
AKRPFRTDQE RAYGPGVADA KGGVAMILHA LKLLKAQGFD GYGTLTVLFN PDEEMGSAGS
KKVIAELAAQ HDYVFSYEPP NKDAVTTATN GINGLVLEVK GRSSHAGSAP EEGRNALTEL
AHQLVQLKDL GDPDKGTTVN WTMAKAGEKR NIIPAIATAE ADMRYSDIEE TDRVLAQGQR
LIRKQLIDET QVSLRLEKGR PPLAKNSGSE QLAGVAQKAY AAIDKSIEPI AMRFGTDAGY
AYVPGSDKPA VLETMGVVGA GLHADDEYIE LNSIAPRLYL TLSMIRSLSA P
//
