ID A0A011NEN1_9PROT Unreviewed; 358 AA.
AC A0A011NEN1;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=D-alanyl-D-alanine endopeptidase {ECO:0000313|EMBL:EXI73621.1};
DE EC=3.4.21.- {ECO:0000313|EMBL:EXI73621.1};
GN Name=pbpG_1 {ECO:0000313|EMBL:EXI73621.1};
GN ORFNames=AW07_02579 {ECO:0000313|EMBL:EXI73621.1};
OS Candidatus Accumulibacter sp. SK-11.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Candidatus Accumulibacter.
OX NCBI_TaxID=1454000 {ECO:0000313|EMBL:EXI73621.1, ECO:0000313|Proteomes:UP000020226};
RN [1] {ECO:0000313|EMBL:EXI73621.1, ECO:0000313|Proteomes:UP000020226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK-11 {ECO:0000313|Proteomes:UP000020226};
RA Skennerton C.T., Barr J.J., Slater F.R., Bond P.L., Tyson G.W.;
RT "Expanding our view of genomic diversity in Candidatus Accumulibacter
RT clades.";
RL Submitted (FEB-2014) 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:EXI73621.1}.
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DR EMBL; JFAW01000014; EXI73621.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A011NEN1; -.
DR STRING; 1454000.AW07_02579; -.
DR PATRIC; fig|1454000.3.peg.2101; -.
DR Proteomes; UP000020226; 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, ECO:0000313|EMBL:EXI73621.1};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW Reference proteome {ECO:0000313|Proteomes:UP000020226};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 104..328
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..59
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 137
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 140
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 194
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 299
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 358 AA; 37993 MW; D56A52D9FF852206 CRC64;
MAQKARPAGT AVRSAVPRGK PAAVAEQRSI GTRAERKTSG VRTEQLARAG DKAKSRNEKG
KPSTVASIRG FAPQRAVASG GQAYQKKNLT RAVAGGADVW QETGQLAVHS GSALVIGQDA
GELLYEKNAN AVVPIASITK VMTAMVVLDS MPNLQAPISI GDEDVDYLRG SRSRLGVGTV
ITRETALLLA LMSSENRASH ALARHYPGGL QAFVAAMNRK AASLGMAHTR FDDPTGLSSN
NVSTAHDLAR MVAAAHRYPL IREFSTTPGV RAEVKGRELD FHNTNQLVSS PTWEIGLSKT
GYIQEAGKCL VMQARVADKP VVIVLLDSAG KQTRIGDANR IKRWMESASA AGRLPTPV
//
