ID A0A1E5GVJ6_9ENTE Unreviewed; 481 AA.
AC A0A1E5GVJ6;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=D-alanyl-D-alanine carboxypeptidase {ECO:0000313|EMBL:OEG16708.1};
GN ORFNames=BCR25_03675 {ECO:0000313|EMBL:OEG16708.1};
OS Enterococcus termitis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=332950 {ECO:0000313|EMBL:OEG16708.1, ECO:0000313|Proteomes:UP000095094};
RN [1] {ECO:0000313|EMBL:OEG16708.1, ECO:0000313|Proteomes:UP000095094}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 8895 {ECO:0000313|EMBL:OEG16708.1,
RC ECO:0000313|Proteomes:UP000095094};
RA Capua I., De Benedictis P., Joannis T., Lombin L.H., Cattoli G.;
RL Submitted (SEP-2016) 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}.
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:OEG16708.1}.
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DR EMBL; MIJY01000012; OEG16708.1; -; Genomic_DNA.
DR RefSeq; WP_069663105.1; NZ_MIJY01000012.1.
DR AlphaFoldDB; A0A1E5GVJ6; -.
DR PATRIC; fig|332950.4.peg.1521; -.
DR OrthoDB; 9791132at2; -.
DR Proteomes; UP000095094; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008800; F:beta-lactamase activity; IEA:InterPro.
DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:InterPro.
DR GO; GO:0030655; P:beta-lactam antibiotic catabolic process; 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 GO; GO:0046677; P:response to antibiotic; IEA:InterPro.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR Gene3D; 2.30.140.20; Penicillin-binding protein 4, C-terminal domain; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR000871; Beta-lactam_class-A.
DR InterPro; IPR015294; Pen-bd_prot4_C_dom.
DR InterPro; IPR037091; Pen-bd_prot4_C_dom_sf.
DR InterPro; IPR015956; Peniciliin-bd_prot_C_sf.
DR InterPro; IPR018044; Peptidase_S11.
DR InterPro; IPR001967; Peptidase_S11_N.
DR PANTHER; PTHR35333; BETA-LACTAMASE; 1.
DR PANTHER; PTHR35333:SF3; BETA-LACTAMASE2 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF09211; DUF1958; 1.
DR Pfam; PF00768; Peptidase_S11; 1.
DR PRINTS; PR00725; DADACBPTASE1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF69189; Penicillin-binding protein associated domain; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000313|EMBL:OEG16708.1};
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:OEG16708.1};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 420..441
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 462..480
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 52..299
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT DOMAIN 328..379
FT /note="Penicillin-binding protein 4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF09211"
FT ACT_SITE 79
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 82
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 143
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 270
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 481 AA; 53592 MW; 4B5BA2BE1B3AFB12 CRC64;
MPSLKKQLAT LTFFLLITCL FIGSLPQKTD AVDVEPDFTQ NPKYPIKNGY RPKASIVIDA
GSGQILWEDQ PDLPWSPASI AKVMTMYLVF EAMEQGKFTL DTTVKATEKY VNISQLYALS
NNNISLGVEY PVRDLLTMLA VPSSNVATLM LANLVSDNDE TGFIHLMNKK AADLGMKNTT
YFNSSGAQIS AFEGYYQAEG IDPNGDNKST ARDLAILAYN LVNKYPDALQ FTNQPVVTTM
KNTPYEETFD TYNYSLPGAK YGYDGVDGLK TGSSPTGGFN YIATAKKGEV RLIEVILGVG
DWSDQEGEYE RHIAGNAILD NTFSSYEYKK ILEKGTNTIN QKEITLDQDF YGLVKKGTTP
RFITENGTLS LANELGQVSP KIPVQSINYQ EKQQTAEKAA TKKQEKQKTS SFVGPKKTRT
YLFCGVLFTL SVLFFAFSRV FRKRISSIRR SNRKMATPTS RLFFILSILS FIGVIGVWFF
L
//
