ID   H1PM34_9FIRM            Unreviewed;       312 AA.
AC   H1PM34;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=LD-carboxypeptidase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=HMPREF0380_01242 {ECO:0000313|EMBL:EHO84164.1};
OS   Eubacterium infirmum F0142.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales;
OC   Eubacteriales Family XIII. Incertae Sedis.
OX   NCBI_TaxID=883109 {ECO:0000313|EMBL:EHO84164.1, ECO:0000313|Proteomes:UP000004504};
RN   [1] {ECO:0000313|EMBL:EHO84164.1, ECO:0000313|Proteomes:UP000004504}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0142 {ECO:0000313|EMBL:EHO84164.1,
RC   ECO:0000313|Proteomes:UP000004504};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Ganesan A.,
RA   Baranova O.V., Blanton J.M., Tanner A.C., Dewhirst F.E., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Chapman S.B., Gearin G., Goldberg J., Griggs A.,
RA   Gujja S., Hansen M., Heiman D., Howarth C., Larimer J., Lui A.,
RA   MacDonald P.J.P., McCowen C., Montmayeur A., Murphy C., Neiman D.,
RA   Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P., Stolte C.,
RA   Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Eubacterium infirmum F0142.";
RL   Submitted (DEC-2011) 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; AGWI01000020; EHO84164.1; -; Genomic_DNA.
DR   AlphaFoldDB; H1PM34; -.
DR   STRING; 883109.HMPREF0380_01242; -.
DR   MEROPS; S66.001; -.
DR   PATRIC; fig|883109.3.peg.1235; -.
DR   eggNOG; COG1619; Bacteria.
DR   HOGENOM; CLU_034346_3_1_9; -.
DR   Proteomes; UP000004504; Unassembled WGS sequence.
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:UP000004504};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT   DOMAIN          19..136
FT                   /note="LD-carboxypeptidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02016"
FT   DOMAIN          185..299
FT                   /note="LD-carboxypeptidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17676"
FT   ACT_SITE        116
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT   ACT_SITE        215
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT   ACT_SITE        284
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
SQ   SEQUENCE   312 AA;  34540 MW;  D9C52224C35F4695 CRC64;
     MKNFEKMLYP RQLRKGDTVG IICPSSAIPS DKIERVKSCV ENMGYKTKLA DNLDKVFAGY
     MAGDGDERAK WVNKMFADPE VDAIFCVRGG DGSSRLMPYL DYEIIKANPK IFVGYSDVTN
     IHMALNQICG MVSFHGPMIS SNMLDGLTDE ESASFFDTIN AESDFDYQNP KGYEIKKLKG
     GKAIGNLVGG NLSLLSASIG TPFEVESEDN ILFIEEVCEP MSKIEKWIFH LRNAGKLDKC
     RGIVLGQFTK VENAEEPSYD ENEVTLAALR NLDIPVVCNV QSGHGKPMMT LPLGTLCTLD
     ADEGRISFKV ER
//