ID A0A078KRJ2_9FIRM Unreviewed; 365 AA.
AC A0A078KRJ2;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Peptidase S11 D-alanyl-D-alanine carboxypeptidase 1 {ECO:0000313|EMBL:CDZ25008.1};
GN ORFNames=CCDG5_1913 {ECO:0000313|EMBL:CDZ25008.1};
OS [Clostridium] cellulosi.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Oscillospiraceae incertae sedis.
OX NCBI_TaxID=29343 {ECO:0000313|EMBL:CDZ25008.1, ECO:0000313|Proteomes:UP000032431};
RN [1] {ECO:0000313|Proteomes:UP000032431}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DG5 {ECO:0000313|Proteomes:UP000032431};
RA Wibberg D.;
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S11 family.
CC {ECO:0000256|ARBA:ARBA00007164, ECO:0000256|RuleBase:RU004016}.
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DR EMBL; LM995447; CDZ25008.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A078KRJ2; -.
DR STRING; 29343.CCDG5_1913; -.
DR KEGG; ccel:CCDG5_1913; -.
DR PATRIC; fig|29343.3.peg.2006; -.
DR HOGENOM; CLU_027070_7_2_9; -.
DR OrthoDB; 9791132at2; -.
DR Proteomes; UP000032431; 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:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR018044; Peptidase_S11.
DR InterPro; IPR001967; Peptidase_S11_N.
DR PANTHER; PTHR21581; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE; 1.
DR PANTHER; PTHR21581:SF34; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE DACC; 1.
DR Pfam; PF00768; Peptidase_S11; 1.
DR PRINTS; PR00725; DADACBPTASE1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000313|EMBL:CDZ25008.1};
KW Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW Protease {ECO:0000313|EMBL:CDZ25008.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000032431};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..365
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039209214"
FT TRANSMEM 335..355
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 37..269
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT ACT_SITE 71
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 74
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 129
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 240
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 365 AA; 39393 MW; 34F5F3B4F851566C CRC64;
MKSKLVVTMA FSMLFTYITA SSGAALISKA ADPASDPSAP QITAEAAIVA DADTGYIYYN
KNMHQKMYPA SITKILTGLV AVENGHDSDI ITINGNIGEG MPSDAARIYL EDGEVITQEE
ALYTMFLASA NDSANALALH IGGTIEKFVN MMNERAKELG AVDSHFSNPS GLPDKNNVTS
AYDMAIITKK ALQEPALMKY FGAKSYTMPA TNKREPIAFS TLHKMMKNTI YKYEGTIAGK
TGWETMSGHT LVTAAKRNGR TLICVVLKSS NGNTVYKDTR ALLDYAFAKE IDTSSAQYLA
SPLKKVQAET TSNPIKNVPP PSSVKLNAGQ KDKDMAGPAI VLICSVCLFI LLISFGRKTI
AIRKR
//
