ID A0A1A9HR85_9BURK Unreviewed; 302 AA.
AC A0A1A9HR85;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Peptidase S66 {ECO:0008006|Google:ProtNLM};
GN ORFNames=ABE85_21775 {ECO:0000313|EMBL:ANH69548.1};
OS Mitsuaria sp. 7.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Roseateles.
OX NCBI_TaxID=1658665 {ECO:0000313|EMBL:ANH69548.1, ECO:0000313|Proteomes:UP000078154};
RN [1] {ECO:0000313|EMBL:ANH69548.1, ECO:0000313|Proteomes:UP000078154}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=7 {ECO:0000313|EMBL:ANH69548.1,
RC ECO:0000313|Proteomes:UP000078154};
RA Bao W., Leung F.C.C., Jiang J.;
RT "Complete Genome Sequence of Mitsuaria sp. Strain 7, a Lignin-degrading
RT Bacterium Isolated from Forest Soil.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S66 family.
CC {ECO:0000256|ARBA:ARBA00010233}.
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DR EMBL; CP011514; ANH69548.1; -; Genomic_DNA.
DR RefSeq; WP_067279596.1; NZ_CP011514.1.
DR AlphaFoldDB; A0A1A9HR85; -.
DR STRING; 1658665.ABE85_21775; -.
DR KEGG; miu:ABE85_21775; -.
DR PATRIC; fig|1658665.3.peg.4453; -.
DR OrthoDB; 9807329at2; -.
DR Proteomes; UP000078154; Chromosome.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd07025; Peptidase_S66; 1.
DR Gene3D; 3.40.50.10740; Class I glutamine amidotransferase-like; 1.
DR Gene3D; 3.50.30.60; LD-carboxypeptidase A C-terminal domain-like; 1.
DR InterPro; IPR027461; Carboxypeptidase_A_C_sf.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR027478; LdcA_N.
DR InterPro; IPR040449; Peptidase_S66_N.
DR InterPro; IPR040921; Peptidase_S66C.
DR InterPro; IPR003507; S66_fam.
DR PANTHER; PTHR30237; MURAMOYLTETRAPEPTIDE CARBOXYPEPTIDASE; 1.
DR PANTHER; PTHR30237:SF2; MUREIN TETRAPEPTIDE CARBOXYPEPTIDASE; 1.
DR Pfam; PF02016; Peptidase_S66; 1.
DR Pfam; PF17676; Peptidase_S66C; 1.
DR PIRSF; PIRSF028757; LD-carboxypeptidase; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR SUPFAM; SSF141986; LD-carboxypeptidase A C-terminal domain-like; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000078154};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT DOMAIN 18..133
FT /note="LD-carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02016"
FT DOMAIN 185..293
FT /note="LD-carboxypeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17676"
FT ACT_SITE 115
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 216
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 278
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
SQ SEQUENCE 302 AA; 32126 MW; 3880A21558C65FC4 CRC64;
MADDTFLLPP LPERACLGVI APAGPPRDGT LDRVVPLIER LGFRAKLFPG CHGPAFLGHL
AADDGRRLAD LHEALDDPHV DAVIGLRGGY GCLRLLDRID RALLRRSRKP LIGYSDLTAL
HALRQQLGIA GWHAPMPASD WHKGDAGWAD AVALADRLRR GLRVGDSLGP ALAPHPLNRG
SAPVRGMLSG GNLAVLVALL GTPFMPDLRG AVLFLEDIGE DPYKIDRLLC QLRLAGALDE
IAGLLLGSFT DADPPDEVLA DYFGDLGIPV LAGWPSGHTT PHLPLPIGVA VTLDPGERTL
RA
//
