ID A0A0G0J7P7_9BACT Unreviewed; 344 AA.
AC A0A0G0J7P7;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=D-alanyl-D-alanine carboxypeptidase {ECO:0000313|EMBL:KKQ62927.1};
GN ORFNames=US82_C0004G0044 {ECO:0000313|EMBL:KKQ62927.1};
OS Parcubacteria group bacterium GW2011_GWC1_38_22.
OC Bacteria.
OX NCBI_TaxID=1618897 {ECO:0000313|EMBL:KKQ62927.1, ECO:0000313|Proteomes:UP000034773};
RN [1] {ECO:0000313|EMBL:KKQ62927.1, ECO:0000313|Proteomes:UP000034773}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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:KKQ62927.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LBUL01000004; KKQ62927.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0J7P7; -.
DR STRING; 1618897.US82_C0004G0044; -.
DR PATRIC; fig|1618897.3.peg.195; -.
DR Proteomes; UP000034773; 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 Carboxypeptidase {ECO:0000313|EMBL:KKQ62927.1};
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 Protease {ECO:0000313|EMBL:KKQ62927.1};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 85..324
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT ACT_SITE 113
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 116
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 180
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 292
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 344 AA; 37706 MW; 3E422347F94AD162 CRC64;
MGIGATILMI IAFPLNSLLL FHEGLSSGRF VQADGYGIET AVQGSVKGTE IQKIPEPIKL
KAQAVDNPKY KTVRNENVSN LVLPNAHAFA IIDADTGELL AGNHPTDERQ IASLTKMMTA
TLAMEKIKDL DEAVTIGEEE VYIEGTKVGC PRSGYCISQR LKIDEKISAR NLLQAMLMNS
ANDAAIALAK HMSGTQESFA EVMNLKAKQL GLSNTHFCTA SGLEIDGRES ECYSSAYDIG
RIAAYSMRYD YIWKVFRQPS NTKVASMDGN LVHTILNTDL ILNEVPDVIG GKTGFTPLAG
YSLLMGATDP TGKHRIIAVL LDDSHRWQDI RTAIDWTFKA YTWQ
//
