ID R7RS40_9CLOT Unreviewed; 403 AA.
AC R7RS40;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=D-alanyl-D-alanine carboxypeptidase {ECO:0000313|EMBL:CDF58093.1};
DE EC=3.4.16.4 {ECO:0000313|EMBL:CDF58093.1};
GN ORFNames=TCEL_02007 {ECO:0000313|EMBL:CDF58093.1};
OS Thermobrachium celere DSM 8682.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Thermobrachium.
OX NCBI_TaxID=941824 {ECO:0000313|EMBL:CDF58093.1, ECO:0000313|Proteomes:UP000014923};
RN [1] {ECO:0000313|EMBL:CDF58093.1, ECO:0000313|Proteomes:UP000014923}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8682 {ECO:0000313|EMBL:CDF58093.1,
RC ECO:0000313|Proteomes:UP000014923};
RA Ciranna A., Larjo A., Kivisto A., Santala V., Roos C., Karp M.;
RT "Draft genome sequence of the hydrogen-ethanol-producing anaerobic
RT alkalithermophilic Caloramator celere.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S11 family.
CC {ECO:0000256|ARBA:ARBA00007164, ECO:0000256|RuleBase:RU004016}.
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:CDF58093.1}.
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DR EMBL; CAVN010000093; CDF58093.1; -; Genomic_DNA.
DR AlphaFoldDB; R7RS40; -.
DR MEROPS; S11.005; -.
DR eggNOG; COG1686; Bacteria.
DR HOGENOM; CLU_027070_8_1_9; -.
DR OrthoDB; 1701915at2; -.
DR Proteomes; UP000014923; Unassembled WGS sequence.
DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
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:SF11; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE DACA; 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:CDF58093.1};
KW Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CDF58093.1};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW Protease {ECO:0000313|EMBL:CDF58093.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000014923};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 37..267
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT ACT_SITE 67
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 70
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 127
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 232
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 403 AA; 46670 MW; C3DDA4722990076E CRC64;
MLKLERGAVM KRLIVLICLS LILIIDNKIV FAQDLLNLRC KSAVLIDAES GKVLYEKNKD
ERLPIASITK LMTFYTFVEE LGEEYINGYL TYNIDNSKYK KDEPILDIKA GERIKTGDLI
TAMLVFSANN APDMLVNEYE RVKKENFIEK MNQTAKKLGL NDTYYVNPSG LTKENKYNIS
TAYDQARLSY YILKKHKDIL RYTSKKYFDY NGKRYYSTNK LLGNYHGLDG LKTGYTKEAG
YCLISTLDAS KYSGNSKPLR FITVVLGCSS DAERFVETRK LLDYAKNNFE NYVLDSEKTF
EVKNTDYVGD LIKLKPSGDV YILKNKHESP ELSIKLNDKL NRKIRKNDVI GRLFIKTSIG
TKEVDLISVN DYTRKSLFFR LFQHIKNLFK NMGWFGWIEL KKI
//
