ID A0A0G0PUF3_9BACT Unreviewed; 362 AA.
AC A0A0G0PUF3;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Serine-type D-Ala-D-Ala carboxypeptidase {ECO:0000313|EMBL:KKR31794.1};
GN ORFNames=UT63_C0060G0002 {ECO:0000313|EMBL:KKR31794.1};
OS Candidatus Gottesmanbacteria bacterium GW2011_GWC2_39_8.
OC Bacteria; Candidatus Gottesmanbacteria.
OX NCBI_TaxID=1618450 {ECO:0000313|EMBL:KKR31794.1, ECO:0000313|Proteomes:UP000034539};
RN [1] {ECO:0000313|EMBL:KKR31794.1, ECO:0000313|Proteomes:UP000034539}
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:KKR31794.1}.
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DR EMBL; LBXN01000060; KKR31794.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0PUF3; -.
DR Proteomes; UP000034539; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:SF32; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE DACB; 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:KKR31794.1};
KW Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW Protease {ECO:0000313|EMBL:KKR31794.1};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..42
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 88..318
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT ACT_SITE 123
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 126
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 178
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 288
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 362 AA; 40772 MW; 0969772519D70A1E CRC64;
MKTSEYKFSV NVDKESFFHL NWRIFFISIG VGFLVALFQL IFSYTNFVSP LTSVQRTEIF
PSLYPNLEKT RNNFVLHKKK SLVSEAYAAA APYTQAVSYA VIDYDNGEIL ESKDLSGKRA
IASLTKLMTA VVAMDLASPD EVYTASYKTA NIQPTKIGLI PGQKMTLREL MEGLLMTSAN
DTAEMIKEGI DQKYGEEVFI KAMNVKAKFL GLKNSNFDNP QGFDSSNNYS SVEDLSILTH
YALENYPLIA EIVKKDYDFL PQNQLHKQYD LYNWNGLLGV YPEVLGVKIG NTKDAGMTMI
ALSKRGNKKI LAVLLGAPGI LERDLWTSQL LDLGFKETKG LAVVNVTEQQ LLDKYSTWKY
WN
//
