ID R5QXY5_9FIRM Unreviewed; 278 AA.
AC R5QXY5;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Peptidase U61 LD-carboxypeptidase A {ECO:0000313|EMBL:CCZ33313.1};
GN ORFNames=BN747_02002 {ECO:0000313|EMBL:CCZ33313.1};
OS Firmicutes bacterium CAG:646.
OC Bacteria; Bacillota.
OX NCBI_TaxID=1262995 {ECO:0000313|EMBL:CCZ33313.1, ECO:0000313|Proteomes:UP000018386};
RN [1] {ECO:0000313|EMBL:CCZ33313.1, ECO:0000313|Proteomes:UP000018386}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:646 {ECO:0000313|Proteomes:UP000018386};
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:CCZ33313.1}.
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DR EMBL; CAZW010000059; CCZ33313.1; -; Genomic_DNA.
DR AlphaFoldDB; R5QXY5; -.
DR STRING; 1262995.BN747_02002; -.
DR Proteomes; UP000018386; Unassembled WGS sequence.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
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:CCZ33313.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000313|EMBL:CCZ33313.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000018386}.
FT DOMAIN 8..123
FT /note="LD-carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02016"
FT DOMAIN 164..275
FT /note="LD-carboxypeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17676"
FT ACT_SITE 106
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 195
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 263
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
SQ SEQUENCE 278 AA; 31183 MW; 9705E283CA7A52C1 CRC64;
MFKEKDTVCI VSCSDGMLPE NQGKIEELKK VFYQMGLQVL ESPYLYRKDA LAVSPARRGE
YLMSCYENEQ VKAIFDVSGG NLANQILEFL DFETIKKSGV QFWGYSDLTV VLNALYTKAG
KSSWLYQVRN LVGRDGEDQR RRFQGEREQF LPDDWKLLAG SRMEGILVGG NIRCFLKLAG
TQYFPDLEGK LLFLESFGGS EGVIASLLTQ LKQMGAFDKI GGLLLGTFTE LNEKEGREKI
EELVLSLRGE RKFPVARTSQ VGHGADSRGL PIGSIYKV
//
