ID A0A0D0R5T8_9GAMM Unreviewed; 347 AA.
AC A0A0D0R5T8;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=NODE_11, whole genome shotgun sequence {ECO:0000313|EMBL:KIQ97004.1};
DE EC=3.4.17.13 {ECO:0000313|EMBL:KIQ97004.1};
GN ORFNames=TI01_1460 {ECO:0000313|EMBL:KIQ97004.1};
OS Lysobacter sp. A03.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Lysobacter.
OX NCBI_TaxID=1199154 {ECO:0000313|EMBL:KIQ97004.1, ECO:0000313|Proteomes:UP000032077};
RN [1] {ECO:0000313|EMBL:KIQ97004.1, ECO:0000313|Proteomes:UP000032077}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A03 {ECO:0000313|EMBL:KIQ97004.1,
RC ECO:0000313|Proteomes:UP000032077};
RA Pereira J.Q., Ambrosini A., Sant'Anna F.H., Tadra-Sfeir M., Faoro H.,
RA Pedrosa F.O., de Souza E.M., Brandelli A., Passaglia L.M.;
RT "Genome sequence of Lysobacter sp. A03.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S66 family.
CC {ECO:0000256|ARBA:ARBA00010233}.
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:KIQ97004.1}.
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DR EMBL; JXSS01000064; KIQ97004.1; -; Genomic_DNA.
DR RefSeq; WP_043958593.1; NZ_JXSS01000064.1.
DR AlphaFoldDB; A0A0D0R5T8; -.
DR STRING; 1199154.TI01_1460; -.
DR PATRIC; fig|1199154.3.peg.271; -.
DR OrthoDB; 9807329at2; -.
DR Proteomes; UP000032077; Unassembled WGS sequence.
DR GO; GO:0106415; F:muramoyltetrapeptide carboxypeptidase activity; IEA:UniProtKB-EC.
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 ECO:0000313|EMBL:KIQ97004.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KIQ97004.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000032077};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..347
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002220244"
FT DOMAIN 45..162
FT /note="LD-carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02016"
FT DOMAIN 215..331
FT /note="LD-carboxypeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17676"
FT ACT_SITE 142
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 246
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 316
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
SQ SEQUENCE 347 AA; 37408 MW; ACEC02C651D356FE CRC64;
MHRRQFLAHA AGAAVILPFL RASKVFATPS SGKLLPVPLA KGDWVGLVSP SSALNDGFDL
QLAQEVMQAL GFKVKTGEHY AERRGHLAGT DAGRAGDINA MFSDPEVKAV IATRGGSGAA
RLLPLLDYKA IRRNPKALLG FSDITALHNA IHAQTGLVTF HGPNGSGSWN RFNVDQFERV
FFKRELMQYR NVQDPGDELV QRRNRTITIA GGTGRGELVG GNLSVLVALA GSPYLPDFTG
KILFIEDVSE APYRIDRMLT TLKLMGVLDA IAGVIFGDCS DCEPGNGYGS LTLSQILDDH
LKPLKIPAFQ GAMIGHIRQQ FIVPVGGLVE MDADAGTFRM LEPVFQS
//
