ID D4KBI3_9FIRM Unreviewed; 447 AA.
AC D4KBI3;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE SubName: Full=D-alanyl-D-alanine carboxypeptidase {ECO:0000313|EMBL:CBL02196.1};
GN ORFNames=FPR_19790 {ECO:0000313|EMBL:CBL02196.1};
OS Faecalibacterium prausnitzii SL3/3.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Faecalibacterium.
OX NCBI_TaxID=657322 {ECO:0000313|EMBL:CBL02196.1, ECO:0000313|Proteomes:UP000007059};
RN [1] {ECO:0000313|EMBL:CBL02196.1, ECO:0000313|Proteomes:UP000007059}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SL3/3 {ECO:0000313|EMBL:CBL02196.1,
RC ECO:0000313|Proteomes:UP000007059};
RG metaHIT consortium -- http://www.metahit.eu/;
RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT "The genome sequence of Faecalibacterium prausnitzii SL3/3.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBL02196.1, ECO:0000313|Proteomes:UP000007059}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SL3/3 {ECO:0000313|EMBL:CBL02196.1,
RC ECO:0000313|Proteomes:UP000007059};
RA Pajon A.;
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Removes C-terminal D-alanyl residues from sugar-peptide cell
CC wall precursors. {ECO:0000256|ARBA:ARBA00003217}.
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DR EMBL; FP929046; CBL02196.1; -; Genomic_DNA.
DR AlphaFoldDB; D4KBI3; -.
DR KEGG; fpa:FPR_19790; -.
DR PATRIC; fig|657322.3.peg.1883; -.
DR eggNOG; COG1686; Bacteria.
DR HOGENOM; CLU_027070_7_3_9; -.
DR Proteomes; UP000007059; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 2.60.410.10; D-Ala-D-Ala carboxypeptidase, C-terminal domain; 1.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR015956; Peniciliin-bd_prot_C_sf.
DR InterPro; IPR012907; Peptidase_S11_C.
DR InterPro; IPR037167; Peptidase_S11_C_sf.
DR InterPro; IPR001967; Peptidase_S11_N.
DR Pfam; PF07943; PBP5_C; 1.
DR Pfam; PF00768; Peptidase_S11; 1.
DR SMART; SM00936; PBP5_C; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF69189; Penicillin-binding protein associated domain; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Carboxypeptidase {ECO:0000313|EMBL:CBL02196.1};
KW Hydrolase {ECO:0000313|EMBL:CBL02196.1};
KW Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:CBL02196.1};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..447
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003060040"
FT TRANSMEM 409..431
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 297..392
FT /note="Peptidase S11 D-Ala-D-Ala carboxypeptidase A C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00936"
SQ SEQUENCE 447 AA; 49177 MW; 2E54206A0B1BA203 CRC64;
MKRIFALVLS FVFLLSCLVL PAGAMFDPSP VYQVQAASAY IVNTDTNIIV YDKDSTKQVS
AGGLTKYMTL AVLLTNYADQ LDNTFQMPFA ISDYVYNTNN ADMRSNETFT YREAMYAMLT
RNANEAAMGV AYTLSGGDLD GWVAQMNTLS QRIGTTASSW TDACGIDSGN TTCAVDMYLI
LRYLMSFDAF VEVSGAPSFT MPAKEKHRSS SVLVSQNAAL SKASGGSYYR SAMQGGMCSV
TAFKNDTGTQ SYVSWGNKDG ATYIFCVMDS PDSCDTFGYA NRRPALFETV KLMDWVFDSF
SIQAALDTDL TIAEIPVRYS SDTDTLQLYP NDSMMTLLPS TSDGTVTQKY FHLPDYVCAP
IQQGDVVGTV ELKLAGETIG VVDLIAGQDV ARNPLLFGVD KVKEFLTSLY LKVVLVLSLI
AGLIYGLWLL CSNWNRRKPT KKIHRRY
//
