ID A0A0G3CJ19_9GAMM Unreviewed; 308 AA.
AC A0A0G3CJ19;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=D-alanyl-D-alanine endopeptidase {ECO:0000313|EMBL:AKJ41984.1};
GN Name=pbpG {ECO:0000313|EMBL:AKJ41984.1};
GN ORFNames=QQ39_07720 {ECO:0000313|EMBL:AKJ41984.1};
OS Pragia fontium.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Budviciaceae; Pragia.
OX NCBI_TaxID=82985 {ECO:0000313|EMBL:AKJ41984.1, ECO:0000313|Proteomes:UP000068021};
RN [1] {ECO:0000313|EMBL:AKJ41984.1, ECO:0000313|Proteomes:UP000068021}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=24613 {ECO:0000313|EMBL:AKJ41984.1,
RC ECO:0000313|Proteomes:UP000068021};
RX PubMed=26159528;
RA Snopkova K., Sedlar K., Bosak J., Chaloupkova E., Provaznik I., Smajs D.;
RT "Complete Genome Sequence of Pragia fontium 24613, an Environmental
RT Bacterium from the Family Enterobacteriaceae.";
RL Genome Announc. 3:e00740-15(2015).
CC -!- SIMILARITY: Belongs to the peptidase S11 family.
CC {ECO:0000256|ARBA:ARBA00007164, ECO:0000256|RuleBase:RU004016}.
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DR EMBL; CP010423; AKJ41984.1; -; Genomic_DNA.
DR RefSeq; WP_047780723.1; NZ_CP010423.1.
DR AlphaFoldDB; A0A0G3CJ19; -.
DR STRING; 82985.QQ39_07720; -.
DR KEGG; pfq:QQ39_07720; -.
DR PATRIC; fig|82985.3.peg.1613; -.
DR OrthoDB; 5688590at2; -.
DR Proteomes; UP000068021; 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 PANTHER; PTHR21581; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE; 1.
DR PANTHER; PTHR21581:SF26; D-ALANYL-D-ALANINE ENDOPEPTIDASE; 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:UP000068021};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..308
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002552600"
FT DOMAIN 35..266
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT ACT_SITE 72
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 75
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 129
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 236
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 308 AA; 33999 MW; 8191A457BEF6EBCA CRC64;
MRTKIRYSLL SLFILSASTF SVSAVQAAGA PTIAQKSTAQ PEIASGSALV IDMKNNKVIY
STNPDKVVPI ASITKLMTAM VVLDKKLSLT EIIPVTINQT KELEGVYSRV KVGSEVSRGD
MMLLALMSSE NRAAAALAHS YPGGYNAFIK AMNDKAKALG MTHTHYVEPT GLSEQNVSTA
NDLTRLLFAS KQYPLLSQLS TTQEKTISFQ KPNYTLEFRN TNYLVKKDDW NIQLTKTGFT
NQAGHCLAMR TTINHREVTL VVLDAFGKYT HFADANRLRK WMETGEAPPV PQAAKNYRKQ
KALQTTLN
//