ID A0A0G1QVS5_9BACT Unreviewed; 388 AA.
AC A0A0G1QVS5;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Serine-type D-Ala-D-Ala carboxypeptidase {ECO:0000313|EMBL:KKU21908.1};
GN ORFNames=UX33_C0019G0005 {ECO:0000313|EMBL:KKU21908.1};
OS Candidatus Azambacteria bacterium GW2011_GWC1_46_13.
OC Bacteria; Candidatus Azambacteria.
OX NCBI_TaxID=1618619 {ECO:0000313|EMBL:KKU21908.1, ECO:0000313|Proteomes:UP000034569};
RN [1] {ECO:0000313|EMBL:KKU21908.1, ECO:0000313|Proteomes:UP000034569}
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:KKU21908.1}.
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DR EMBL; LCLU01000019; KKU21908.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1QVS5; -.
DR PATRIC; fig|1618619.3.peg.394; -.
DR Proteomes; UP000034569; 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:KKU21908.1};
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:KKU21908.1};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 133..361
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT REGION 60..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..92
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 164
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 167
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 219
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 331
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 388 AA; 42556 MW; 32FA621DF8F7B7EC CRC64;
MTNALGAILA GLLLLVGILN DKGFFSADNS GSARIPFFKQ AAVKTDEKKQ NKPEIEVNNL
FSSLSGGLRP EESGSGKEEQ AAEPKKAEEG VQANKLPVEN EAKNEVSPTE KAALQTLKTI
NYLPVRNWNV PFAEISAKSV LSTDEKAEKV FYQKNSSERL PIASLTKLMT ALIVLDNYNL
EEKIKISKAA VQIEGEMGGL VVGETLTVHN LLYVMLIESS NDAAFAFAEK VGTDKFVELM
NKKAAVLDLK NTHFANPAGF DEKNNYSTAF DLARLASAAL NYPLVWEILR TKEIEIKSEA
VPDNPNQPIF PHRLINSNKL LDVVPEIVGG KTGYTDLAGG CMILVAQLEN FKVINIVLGA
DGGAPFLDRF KETEKLINWL KEAYLWKL
//