ID A0A1H7PGX9_9BURK Unreviewed; 291 AA.
AC A0A1H7PGX9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=D-alanyl-D-alanine endopeptidase (Penicillin-binding protein 7) {ECO:0000313|EMBL:SEL35041.1};
GN ORFNames=SAMN05216319_1591 {ECO:0000313|EMBL:SEL35041.1};
OS Duganella sp. CF402.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Duganella.
OX NCBI_TaxID=1855289 {ECO:0000313|EMBL:SEL35041.1, ECO:0000313|Proteomes:UP000198529};
RN [1] {ECO:0000313|Proteomes:UP000198529}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF402 {ECO:0000313|Proteomes:UP000198529};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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; FOBG01000001; SEL35041.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H7PGX9; -.
DR STRING; 1855289.SAMN05216319_1591; -.
DR Proteomes; UP000198529; Unassembled WGS sequence.
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:SF6; TRAFFICKING PROTEIN PARTICLE COMPLEX SUBUNIT 12; 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..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..291
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011691664"
FT DOMAIN 23..244
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT REGION 268..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..291
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 52
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 55
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 109
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 214
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 291 AA; 31089 MW; 38E6BAAAC5809598 CRC64;
MLKKIIAALL TSFTAASFAA VPLGSQSVLV VEDATGKVLL EKNANAQVPI ASLTKLMTAM
VVLDAKQDMD EKIAIDRSDV DTLKHSASRV PVGAELSRGD ALQLALMSSD NRAAASLGRT
YPGGIEAFRV AVKNKIRALG LTQTVIEEPT GLSPHNMSTA TELAKIAAAA SAYPDIRRIT
TDTKDVINIK GRKVEYHNTN RLVGAKGWDV GLSKTGYTEE AGRCLIMRFK SAGKNATLVL
LNAKANSARL MDAVNIRRFI AGPDEKPKVM KASVSGKKKA AKTSKRTRRA M
//
