ID A0A108C9L0_9BURK Unreviewed; 357 AA.
AC A0A108C9L0;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=D-alanyl-D-alanine endopeptidase {ECO:0000313|EMBL:KWK70501.1};
GN ORFNames=WM16_21175 {ECO:0000313|EMBL:KWK70501.1};
OS Burkholderia ubonensis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=101571 {ECO:0000313|EMBL:KWK70501.1, ECO:0000313|Proteomes:UP000065504};
RN [1] {ECO:0000313|EMBL:KWK70501.1, ECO:0000313|Proteomes:UP000065504}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSMB782WGS {ECO:0000313|EMBL:KWK70501.1,
RC ECO:0000313|Proteomes:UP000065504};
RA Sahl J., Keim P., Wagner D.;
RT "Expanding the genomic diversity of Burkholderia species for the
RT development of highly accurate diagnostics.";
RL Submitted (NOV-2015) 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:KWK70501.1}.
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DR EMBL; LPLU01000106; KWK70501.1; -; Genomic_DNA.
DR RefSeq; WP_060236435.1; NZ_LPLU01000106.1.
DR AlphaFoldDB; A0A108C9L0; -.
DR Proteomes; UP000065504; Unassembled WGS sequence.
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 InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR000871; Beta-lactam_class-A.
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; PF00768; Peptidase_S11; 1.
DR PRINTS; PR00725; DADACBPTASE1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE 3: Inferred from homology;
KW Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..357
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007129617"
FT DOMAIN 112..336
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT REGION 36..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..93
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 144
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 147
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 201
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 306
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 357 AA; 39338 MW; 178BB6CA94114A98 CRC64;
MTGIIVRAPR ARTFLLIIAS LLLCAFMSNA SAHRAAHRPA QGHATPAKLK KPPTHRKLGR
HHRPRARHHA VKHHAAPAPQ QHRRAKRAAS ARPRPTTKPR LLASCGYSPR AANALHSRAA
YVLDVRTGTP LLARNARTVR PIASISKLMT AVVARDADRP LDGMLRVSSH DRDTIKFTHS
RLSVGSTLSR RDMYRIALMS SENRAAAALS RDYPGGRPAF VAAMNREARR LGMRRTRFRE
PTGLSPRNVS TAEELALLVD AAARDPLIRR FSTAKSGTVH PGDGKLLYVN SDPLVRYGQW
PIQLQKTGFI NEAGHGVVMR ALVRGRPQTI VLLGSPTRDG VTSDALRIRR WLACSLM
//
