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Database: UniProt
Entry: I4VTP4_9GAMM
LinkDB: I4VTP4_9GAMM
Original site: I4VTP4_9GAMM 
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
//
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