ID A0A099WFR6_9LIST Unreviewed; 305 AA.
AC A0A099WFR6;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=D-alanyl-D-alanine carboxypeptidase {ECO:0000313|EMBL:KGL44584.1};
GN ORFNames=EP57_01085 {ECO:0000313|EMBL:KGL44584.1};
OS Listeria booriae.
OC Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=1552123 {ECO:0000313|EMBL:KGL44584.1, ECO:0000313|Proteomes:UP000029844};
RN [1] {ECO:0000313|EMBL:KGL44584.1, ECO:0000313|Proteomes:UP000029844}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL A5-0281 {ECO:0000313|EMBL:KGL44584.1,
RC ECO:0000313|Proteomes:UP000029844};
RA den Bakker H.C.;
RT "Novel Listeriaceae from food processing environments.";
RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
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:KGL44584.1}.
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DR EMBL; JNFA01000002; KGL44584.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A099WFR6; -.
DR STRING; 1552123.EP57_01085; -.
DR MEROPS; S11.001; -.
DR eggNOG; COG1686; Bacteria.
DR Proteomes; UP000029844; 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:SF11; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE DACA; 1.
DR Pfam; PF00768; Peptidase_S11; 1.
DR PRINTS; PR00725; DADACBPTASE1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000313|EMBL:KGL44584.1};
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:KGL44584.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000029844};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..305
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038542718"
FT DOMAIN 54..286
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT ACT_SITE 90
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 93
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 150
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 256
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 305 AA; 32909 MW; 9BC9315B06F2747B CRC64;
MKIKHSCLIA VLAASSLSLA ACNNNEDQAT ATKQKVTATA ETAEKKVEQT VDTTPSPDLN
ISAESAALYN MDDTKPLYEK SPEIVTPIAS ITKLMTTYLV LQAIHNKTLS WDETLQLEPL
DDKAAVSLYM VTNKKTWTVK DLYAAMLVMS ANDAAEALGK RLDKTDFPGK MNKTAKKLGL
SSKSNFVSAS GLDSGGEENV STSKDLYLLA SSLITKYPEV LDMTSKASYK TSNGYTVQST
DALLANKEID GLDGLKTGFT DGAGYCFVGT AKQNGKRLIS IVLKTSTIDA RFQDTKTLMA
YGFKN
//
