ID M4XFS9_9PSED Unreviewed; 310 AA.
AC M4XFS9;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=D-alanyl-D-alanine endopeptidase {ECO:0000313|EMBL:AGI24195.1};
GN Name=pbpG {ECO:0000313|EMBL:AGI24195.1};
GN ORFNames=H681_11625 {ECO:0000313|EMBL:AGI24195.1};
OS Pseudomonas sp. ATCC 13867.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1294143 {ECO:0000313|EMBL:AGI24195.1, ECO:0000313|Proteomes:UP000012082};
RN [1] {ECO:0000313|EMBL:AGI24195.1, ECO:0000313|Proteomes:UP000012082}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13867 {ECO:0000313|EMBL:AGI24195.1,
RC ECO:0000313|Proteomes:UP000012082};
RX PubMed=23723394;
RA Ainala S.K., Somasundar A., Park S.;
RT "Complete genome sequence of Pseudomonas denitrificans ATCC 13867.";
RL Genome Announc. 1:E00257-E00213(2013).
CC -!- SIMILARITY: Belongs to the peptidase S11 family.
CC {ECO:0000256|ARBA:ARBA00007164, ECO:0000256|RuleBase:RU004016}.
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DR EMBL; CP004143; AGI24195.1; -; Genomic_DNA.
DR RefSeq; WP_015477053.1; NC_020829.1.
DR AlphaFoldDB; M4XFS9; -.
DR STRING; 1294143.H681_11625; -.
DR MEROPS; S11.002; -.
DR KEGG; pdr:H681_11625; -.
DR PATRIC; fig|1294143.3.peg.2349; -.
DR eggNOG; COG1686; Bacteria.
DR HOGENOM; CLU_027070_0_3_6; -.
DR OrthoDB; 5688590at2; -.
DR Proteomes; UP000012082; Chromosome.
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 InterPro; IPR006311; TAT_signal.
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.
DR PROSITE; PS51318; TAT; 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..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..310
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004061039"
FT DOMAIN 33..262
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT ACT_SITE 68
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 71
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 125
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 232
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 310 AA; 33310 MW; A338E0B8CC0C3614 CRC64;
MTSRRSILSL LFACAAVVCT SNSLAATPAK ATQPNQLVLA SGSALVVDLQ TNKVIYSSNP
GLVVPIASVT KLMTAMVTLD AKLPMNEMIT VDISETAEMK GVFSRVHLGS QISREKMLLL
ALMSSENRAA ASLAHHYPGG SKAFVAAMNA KARSLGMNHT HYVEPTGLSI HNTSNAQDLI
RLAKAAYTYP QIRRMSTTAT SDARFSKPGY SLSFFNTNPL VRNGKWDIRL TKTGFTNDAG
HCLVMVTMMN GRPVALALLD AFGKRTHVAD ASRIRRWVET GKASPVPAVA LQYKAQRSQA
RAANVAATTE
//
