ID R6KP90_9CLOT Unreviewed; 290 AA.
AC R6KP90;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Peptidase U61 LD-carboxypeptidase A {ECO:0000313|EMBL:CDB75335.1};
GN ORFNames=BN573_01508 {ECO:0000313|EMBL:CDB75335.1};
OS Clostridium sp. CAG:265.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1262787 {ECO:0000313|EMBL:CDB75335.1, ECO:0000313|Proteomes:UP000018277};
RN [1] {ECO:0000313|EMBL:CDB75335.1, ECO:0000313|Proteomes:UP000018277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:265 {ECO:0000313|Proteomes:UP000018277};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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:CDB75335.1}.
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DR EMBL; CBEC010000060; CDB75335.1; -; Genomic_DNA.
DR AlphaFoldDB; R6KP90; -.
DR Proteomes; UP000018277; Unassembled WGS sequence.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR CDD; cd07062; Peptidase_S66_mccF_like; 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:SF5; CARBOXYPEPTIDASE YOCD-RELATED; 1.
DR PANTHER; PTHR30237; MURAMOYLTETRAPEPTIDE 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:0000313|EMBL:CDB75335.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000313|EMBL:CDB75335.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000018277}.
FT DOMAIN 11..129
FT /note="LD-carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02016"
FT DOMAIN 170..282
FT /note="LD-carboxypeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17676"
FT ACT_SITE 110
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 201
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 268
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
SQ SEQUENCE 290 AA; 32757 MW; 58AE3387292D8CA0 CRC64;
MNSLLKTNDY IGLVANSNGI DIANKDKIDT LIACLKELGL NPLLSSIFYK KQGPFNGTGQ
ERADVLNTYF NDPNIKAIFD LSGGDLSNET LDYIDFQTIS DNPKPFFGYS DLSTLLNAIN
TKSHIATYHY QLRHLIGRNS LEQKEYFLNS FMKSNMPKFK YEFIRGSQME GIVIGGNIRC
FLKLMGTKYQ PDFNNKILFL ESLSGDCAKM ATFLRQYKQI GAFDNLNGII LGTFTEMEKE
KYKPTIEEMI ISLVDSSIPI AKSLELGHGE DCKCIIIGNH YSLKKQKLEV
//
