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Database: UniProt
Entry: A0A0G1QVS5_9BACT
LinkDB: A0A0G1QVS5_9BACT
Original site: A0A0G1QVS5_9BACT 
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
//
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