ID I4VTP4_9GAMM Unreviewed; 335 AA.
AC I4VTP4;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=L,D-carboxypeptidase A {ECO:0000313|EMBL:EIL90585.1};
DE EC=3.4.17.13 {ECO:0000313|EMBL:EIL90585.1};
GN Name=ldcA {ECO:0000313|EMBL:EIL90585.1};
GN ORFNames=UU5_15043 {ECO:0000313|EMBL:EIL90585.1};
OS Rhodanobacter sp. 115.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Rhodanobacter.
OX NCBI_TaxID=1162282 {ECO:0000313|EMBL:EIL90585.1, ECO:0000313|Proteomes:UP000004557};
RN [1] {ECO:0000313|EMBL:EIL90585.1, ECO:0000313|Proteomes:UP000004557}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=115 {ECO:0000313|EMBL:EIL90585.1,
RC ECO:0000313|Proteomes:UP000004557};
RX PubMed=22843592; DOI=10.1128/JB.00871-12;
RA Kostka J.E., Green S.J., Rishishwar L., Prakash O., Katz L.S.,
RA Marino-Ramirez L., Jordan I.K., Munk C., Ivanova N., Mikhailova N.,
RA Watson D.B., Brown S.D., Palumbo A.V., Brooks S.C.;
RT "Genome sequences for six rhodanobacter strains, isolated from soils and
RT the terrestrial subsurface, with variable denitrification capabilities.";
RL J. Bacteriol. 194:4461-4462(2012).
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:EIL90585.1}.
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DR EMBL; AJXS01000358; EIL90585.1; -; Genomic_DNA.
DR RefSeq; WP_008214456.1; NZ_AJXS01000358.1.
DR AlphaFoldDB; I4VTP4; -.
DR MEROPS; S66.002; -.
DR PATRIC; fig|1162282.3.peg.2839; -.
DR OrthoDB; 9807329at2; -.
DR Proteomes; UP000004557; 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:EIL90585.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EIL90585.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT DOMAIN 6..128
FT /note="LD-carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02016"
FT DOMAIN 172..293
FT /note="LD-carboxypeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17676"
FT REGION 311..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 108
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 208
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 335 AA; 35319 MW; 8EA101DF8F9A063A CRC64;
MPAIQIQLIA PSGYPHDRAA LARGVERLRG AGCALSGLDV LERSELRFAG SDAERLADIN
HLADLSTLPD LVLTTRGGYG ASRLLPHLRY DALRERLAET PIPLVGHSDF TALQLALHAK
SGLCTFSGPL LADLGTDAHD DDFSWRHFWS TLTSSSTTLA WADAGVADVD ASGPLWGGNL
AVLCSLLGTP YFPGAKGGGI DGGILFVEDV GEPPFRIERL LYQLHLSGVL GRQQALVLGG
FSHCRPGPND NGYDLAAAFA QIERVAGIPV VHGLPHGHGA RQLTLPFGAP ARLRVEGGSA
RLDFHGYPHL PLGSSPAVPG RQGREQGQAG STPNP
//