ID B5CPF5_9FIRM Unreviewed; 256 AA.
AC B5CPF5;
DT 14-OCT-2008, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2008, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE SubName: Full=Serine-type D-Ala-D-Ala carboxypeptidase {ECO:0000313|EMBL:EDY32747.1};
DE EC=3.4.16.4 {ECO:0000313|EMBL:EDY32747.1};
GN ORFNames=RUMLAC_01348 {ECO:0000313|EMBL:EDY32747.1};
OS [Ruminococcus] lactaris ATCC 29176.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Mediterraneibacter.
OX NCBI_TaxID=471875 {ECO:0000313|EMBL:EDY32747.1, ECO:0000313|Proteomes:UP000003254};
RN [1] {ECO:0000313|EMBL:EDY32747.1, ECO:0000313|Proteomes:UP000003254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29176 {ECO:0000313|EMBL:EDY32747.1,
RC ECO:0000313|Proteomes:UP000003254};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Ruminococcus lactaris ATCC 29176.";
RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EDY32747.1, ECO:0000313|Proteomes:UP000003254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29176 {ECO:0000313|EMBL:EDY32747.1,
RC ECO:0000313|Proteomes:UP000003254};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
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:EDY32747.1}.
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DR EMBL; ABOU02000033; EDY32747.1; -; Genomic_DNA.
DR AlphaFoldDB; B5CPF5; -.
DR eggNOG; COG1876; Bacteria.
DR HOGENOM; CLU_054193_3_0_9; -.
DR Proteomes; UP000003254; Unassembled WGS sequence.
DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd14852; LD-carboxypeptidase; 1.
DR Gene3D; 3.30.1380.10; -; 1.
DR InterPro; IPR009045; Hedgehog_sig/DD-Pept_Zn-bd_sf.
DR InterPro; IPR003709; Pept_M15B.
DR PANTHER; PTHR34385; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE; 1.
DR PANTHER; PTHR34385:SF1; PEPTIDOGLYCAN L-ALANYL-D-GLUTAMATE ENDOPEPTIDASE CWLK; 1.
DR Pfam; PF02557; VanY; 1.
DR SUPFAM; SSF55166; Hedgehog/DD-peptidase; 1.
PE 4: Predicted;
KW Carboxypeptidase {ECO:0000313|EMBL:EDY32747.1};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000313|EMBL:EDY32747.1};
KW Protease {ECO:0000313|EMBL:EDY32747.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000003254};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..256
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039668435"
FT DOMAIN 100..236
FT /note="Peptidase M15B"
FT /evidence="ECO:0000259|Pfam:PF02557"
FT COILED 20..54
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 256 AA; 29042 MW; D3CAE20417F88A13 CRC64;
MLCAAVGLIV LMGIAVAGQM ESTEQQNQKL LSENQKLTEE NERLEKDLNN WKIAKEIKEA
PAVRLKEDSE NWMLALVNEE YPLAKDYTPA SLTKLDEKCS VDTRIYGELE QMIADARQAG
LNLYVTSAYR SYDRQREVFD TTMKDWISKG YSPLDAYDET KKSVAVPGTS EHATGLAVDI
ISGQYTGLDD KQGDTAEQEW LMAHCQEYGF ILRFPKDKSN VTGIVYEPWH YRYVGKEAAK
KITEQGITLE EYLQAD
//
