ID A0A0G0IHT1_9BACT Unreviewed; 337 AA.
AC A0A0G0IHT1;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Serine-type D-Ala-D-Ala carboxypeptidase {ECO:0000313|EMBL:KKQ54167.1};
GN ORFNames=US74_C0052G0006 {ECO:0000313|EMBL:KKQ54167.1};
OS Parcubacteria group bacterium GW2011_GWA2_38_13.
OC Bacteria.
OX NCBI_TaxID=1618811 {ECO:0000313|EMBL:KKQ54167.1, ECO:0000313|Proteomes:UP000034626};
RN [1] {ECO:0000313|EMBL:KKQ54167.1, ECO:0000313|Proteomes:UP000034626}
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:KKQ54167.1}.
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DR EMBL; LBUD01000052; KKQ54167.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0IHT1; -.
DR STRING; 1618811.US74_C0052G0006; -.
DR Proteomes; UP000034626; Unassembled WGS sequence.
DR GO; GO:0008800; F:beta-lactamase activity; IEA:InterPro.
DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:InterPro.
DR GO; GO:0030655; P:beta-lactam antibiotic catabolic process; 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 GO; GO:0046677; P:response to antibiotic; IEA:InterPro.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR000871; Beta-lactam_class-A.
DR InterPro; IPR018044; Peptidase_S11.
DR InterPro; IPR001967; Peptidase_S11_N.
DR PANTHER; PTHR35333; BETA-LACTAMASE; 1.
DR PANTHER; PTHR35333:SF3; BETA-LACTAMASE2 DOMAIN-CONTAINING PROTEIN; 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:KKQ54167.1};
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:KKQ54167.1};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 103..308
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT ACT_SITE 125
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 128
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 190
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 290
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 337 AA; 37484 MW; C34A318955746E1D CRC64;
MRTLGVGILT MDLEKIAIPW SGKSSDPAIL KHFSGYIVLQ VQSRGEAWYI NPNDGFRYYL
PNNEEGLNIL RSLGVGASNN ELRMIAMNAT QLYATFTFTA YAHVKLDAGK FSQAYYADNI
LPLASLTKLM TALVILDTKP DWEKKIILTQ EDIQYPKIYV DPDDVTSEVD FQEGDAITYQ
DLWNALLASS SNQAAGILAK NSGFTYKEFI KKMNDKAKSM GLKKTRFTDP SGLDTLNVGT
AKEMAIIARA AFNVSKIKTT TIKSFIIRAL RPDDTTRTIA VINRNQSILK FGPDAAKSGF
LYEAQRNVAY QEGSAVVVIL HARTLTEKNT LIKKLLK
//
