ID A0A0Q9YLV8_9GAMM Unreviewed; 399 AA.
AC A0A0Q9YLV8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 28-JAN-2026, entry version 34.
DE RecName: Full=serine-type D-Ala-D-Ala carboxypeptidase {ECO:0000256|ARBA:ARBA00012448};
DE EC=3.4.16.4 {ECO:0000256|ARBA:ARBA00012448};
GN Name=dacC {ECO:0000313|EMBL:KRG21733.1};
GN ORFNames=HT99x_003970 {ECO:0000313|EMBL:MCS5710574.1}, HT99x_00924
GN {ECO:0000313|EMBL:KRG21733.1};
OS Candidatus Berkiella aquae.
OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC Candidatus Berkiellales; Candidatus Berkiellaceae; Candidatus Berkiella.
OX NCBI_TaxID=295108 {ECO:0000313|EMBL:KRG21733.1};
RN [1] {ECO:0000313|EMBL:KRG21733.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HT99 {ECO:0000313|EMBL:KRG21733.1};
RA Mehari Y.T., Arivett B.A., Farone A.L., Gunderson J.H., Farone M.B.;
RT "Draft Genome Sequences of Two Novel Amoeba-resistant Intranuclear
RT Bacteria, Candidatus Berkiella cookevillensis and Candidatus Berkiella
RT aquae.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:MCS5710574.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HT99 {ECO:0000313|EMBL:MCS5710574.1};
RX PubMed=26893424;
RA Mehari Y.T., Arivett B.A., Farone A.L., Gunderson J.H., Farone M.B.;
RT "Draft Genome Sequences of Two Novel Amoeba-Resistant Intranuclear
RT Bacteria, 'Candidatus Berkiella cookevillensis' and 'Candidatus Berkiella
RT aquae'.";
RL Genome Announc. 4:e01732-e01715(2016).
RN [3] {ECO:0000313|EMBL:MCS5710574.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HT99 {ECO:0000313|EMBL:MCS5710574.1};
RA Kidane D.T., Mehari Y.T., Rice F.C., Arivett B.A., Farone A.L., Berk S.G.,
RA Farone M.B.;
RT "Genomic Description and Analysis of Intracellular Bacteria, Candidatus
RT Berkiella cookevillensis and Candidatus Berkiella aquae.";
RL Submitted (JUN-2021) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Removes C-terminal D-alanyl residues from sugar-peptide cell
CC wall precursors. {ECO:0000256|ARBA:ARBA00003217}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also
CC transpeptidation of peptidyl-alanyl moieties that are N-acyl
CC substituents of D-alanine.; EC=3.4.16.4;
CC Evidence={ECO:0000256|ARBA:ARBA00034000};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752}.
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:KRG21733.1}.
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DR EMBL; LKAJ01000003; KRG21733.1; -; Genomic_DNA.
DR EMBL; LKAJ02000001; MCS5710574.1; -; Genomic_DNA.
DR RefSeq; WP_075065563.1; NZ_LKAJ02000001.1.
DR AlphaFoldDB; A0A0Q9YLV8; -.
DR STRING; 295108.HT99x_00924; -.
DR PATRIC; fig|1590043.3.peg.929; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000051497; Unassembled WGS sequence.
DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR Gene3D; 2.60.410.10; D-Ala-D-Ala carboxypeptidase, C-terminal domain; 1.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR015956; Peniciliin-bd_prot_C_sf.
DR InterPro; IPR018044; Peptidase_S11.
DR InterPro; IPR012907; Peptidase_S11_C.
DR InterPro; IPR037167; Peptidase_S11_C_sf.
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; PF07943; PBP5_C; 1.
DR Pfam; PF00768; Peptidase_S11; 1.
DR PRINTS; PR00725; DADACBPTASE1.
DR SMART; SM00936; PBP5_C; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF69189; Penicillin-binding protein associated domain; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645,
KW ECO:0000313|EMBL:KRG21733.1}; Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KRG21733.1};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000051497};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..399
FT /note="serine-type D-Ala-D-Ala carboxypeptidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5043129692"
FT DOMAIN 279..369
FT /note="Peptidase S11 D-Ala-D-Ala carboxypeptidase A C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00936"
FT ACT_SITE 67
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 70
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 127
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 229
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 399 AA; 44598 MW; 39269ADCBBA53402 CRC64;
MRRLAFLWMS FLCLILLSRL GLAEQPAAIN HVPTPPEVDA EAYILVDYHS GKTLAEKESK
KRIDPASLTK MMSVFVIDHE IASDRLKLTD EVPISESAWK TEGSRMFVQA GKKIPVKDLI
NGIIIQSGND ATVALAEFVA GSESAFADLM NQYAQKIGMK DTHFANATGI PNPDHYTTAY
DLSLLAHALI KTFPETYKVY SEKWFTFNGI KQPNRNRLLW REPYIDGIKT GHSSTAGYCL
AASGQKDHMR LISVLVGAKT EAERTEQTLA LLRYGFRFFE THQLFQANTP LNEPRIWMGD
RKKLSLGITE DLFITIPQGQ YKNLDAKMNV DKRITAPITK GQNYGKLVVK INDELVTEVP
LIALEDVKAG TLWSRVSDYF SLGIHKALNS EETQVAAAS
//
