ID A0A0Q6VQ85_9BURK Unreviewed; 291 AA.
AC A0A0Q6VQ85;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Peptidase S11 {ECO:0000313|EMBL:KQV80709.1};
GN ORFNames=ASD15_12315 {ECO:0000313|EMBL:KQV80709.1};
OS Massilia sp. Root351.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=1736522 {ECO:0000313|EMBL:KQV80709.1, ECO:0000313|Proteomes:UP000051876};
RN [1] {ECO:0000313|EMBL:KQV80709.1, ECO:0000313|Proteomes:UP000051876}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root351 {ECO:0000313|EMBL:KQV80709.1,
RC ECO:0000313|Proteomes:UP000051876};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQV80709.1, ECO:0000313|Proteomes:UP000051876}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root351 {ECO:0000313|EMBL:KQV80709.1,
RC ECO:0000313|Proteomes:UP000051876};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
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:KQV80709.1}.
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DR EMBL; LMDJ01000031; KQV80709.1; -; Genomic_DNA.
DR RefSeq; WP_057156950.1; NZ_LMDJ01000031.1.
DR AlphaFoldDB; A0A0Q6VQ85; -.
DR OrthoDB; 5688590at2; -.
DR Proteomes; UP000051876; 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 Reference proteome {ECO:0000313|Proteomes:UP000051876};
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_5006294905"
FT DOMAIN 21..243
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT REGION 266..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 51
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 54
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 108
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 213
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 291 AA; 31279 MW; 963032E919E66FDD CRC64;
MIKKTVAALL MSLSAAAMAM PLGSQSVLVV EDDTGKILVE KNANAVVPIA SLTKLMTAMV
VLDAKQDMNE EIEIDKEDVD TLKHSTSRVP VGAAIPRGDV LQLALMSSDN RAAASLGRTY
PGGTPAFKAA VNAKIRALGL TQTVIEEPTG LSPNNKSTAS ELVKMAAAAS KYEAIRRMTT
DKNEIINIKG RKVEYHNTNR LVGAKGWDIG MSKTGYTEEA GRCLIMRITS AGKNATLVLL
NAKANSARLM DAFNIRRFIS GAEEEAKPRV MRASSRKKAP ATKNPRRRRA S
//
