ID A0A0G3CMM8_9GAMM Unreviewed; 309 AA.
AC A0A0G3CMM8;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=D-alanyl-D-alanine endopeptidase {ECO:0000313|EMBL:AKJ41985.1};
GN Name=pbpG {ECO:0000313|EMBL:AKJ41985.1};
GN ORFNames=QQ39_07725 {ECO:0000313|EMBL:AKJ41985.1};
OS Pragia fontium.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Budviciaceae; Pragia.
OX NCBI_TaxID=82985 {ECO:0000313|EMBL:AKJ41985.1, ECO:0000313|Proteomes:UP000068021};
RN [1] {ECO:0000313|EMBL:AKJ41985.1, ECO:0000313|Proteomes:UP000068021}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=24613 {ECO:0000313|EMBL:AKJ41985.1,
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; AKJ41985.1; -; Genomic_DNA.
DR RefSeq; WP_047780724.1; NZ_UGTK01000001.1.
DR STRING; 82985.QQ39_07725; -.
DR KEGG; pfq:QQ39_07725; -.
DR PATRIC; fig|82985.3.peg.1614; -.
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: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:UP000068021};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
SQ SEQUENCE 309 AA; 34290 MW; CABD206C5905BFB8 CRC64;
MRTQIRFTLL SLAIFTSGFL AATTVSAKNT HGVSQSSPAK PELSSKSALV VDIQSRKVLY
SSNPDKVVPI ASLTKLMTAM VVLDAKQPLT QIIPVKINET KELRGVFSRV KVGSEITRKE
MLLLALMSSE NRAAASLAHN YPGGYRAFIK AMNAKAKSLG MKNTRYVEPT GLSEKNVSTA
RDLSRLVIAT KKYPMLSQLS TTEGKTVSFE NPRYTLEFHN TNHLIRNHDW KIQLTKTGYT
DEAGRCLTMR TTIGNREVAL VMLDAYGKYT HFADANRLRN WMESGQSLSI AEVSNKNTKK
QKAKSLRQG
//
