ID A0A0Q4XR26_9BURK Unreviewed; 414 AA.
AC A0A0Q4XR26;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Carboxypeptidase {ECO:0000313|EMBL:KQP14420.1};
GN ORFNames=ASF43_15435 {ECO:0000313|EMBL:KQP14420.1};
OS Pseudorhodoferax sp. Leaf267.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae.
OX NCBI_TaxID=1736316 {ECO:0000313|EMBL:KQP14420.1, ECO:0000313|Proteomes:UP000051560};
RN [1] {ECO:0000313|EMBL:KQP14420.1, ECO:0000313|Proteomes:UP000051560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf267 {ECO:0000313|EMBL:KQP14420.1,
RC ECO:0000313|Proteomes:UP000051560};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQP14420.1, ECO:0000313|Proteomes:UP000051560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf267 {ECO:0000313|EMBL:KQP14420.1,
RC ECO:0000313|Proteomes:UP000051560};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQP14420.1}.
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DR EMBL; LMMV01000022; KQP14420.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q4XR26; -.
DR STRING; 1736316.ASF43_15435; -.
DR Proteomes; UP000051560; 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: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.
DR PROSITE; PS00758; ARGE_DAPE_CPG2_1; 1.
DR PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1.
PE 4: Predicted;
KW Carboxypeptidase {ECO:0000313|EMBL:KQP14420.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000313|EMBL:KQP14420.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051560};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..414
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006239933"
FT DOMAIN 211..310
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT ACT_SITE 113
FT /evidence="ECO:0000256|PIRSR:PIRSR037238-1"
FT ACT_SITE 174
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR037238-1"
SQ SEQUENCE 414 AA; 43570 MW; F9E087C7BE255D9F CRC64;
MRAAFGRALL AGLLLAAGSP HALAQPRDEA LFQAATDERP ALVKTLEQLV NIETGTGDAE
GMAEAGRFLE QQLQAHGLTV TRHKAAGLAI GDNLVASMKG RGGKNLLLMA HMDTVYPRGM
LAKAPFRVEG DKAFGPGIAD DKGGVAVILH TLKLLKARNF QDFGTLTVLF NTDEEKGSLG
SRDLIQAEAA KADVVLSYEP TAAGKESFAL GTSGIAYVIA NIKGKASHAG AAPELGVNAL
VEAADLVRRT LDLDDKARGL RFNWTIAKAG AVNNVIPDSA TLNADMRYVR NADFDATVAT
LKERAQQKKL PAAEVDIVVN RGRPAFDAGP AGKLLVDKAV AIYKEAGADI GVTERTGGGT
DAAYAALSGK PVIESMGLPG FGYHSNDAEY VDIGAVPRRL YLSVRMVMDL ARGR
//
