ID A0A0R1K1I9_9LACO Unreviewed; 436 AA.
AC A0A0R1K1I9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=D-alanyl-D-alanine carboxypeptidase {ECO:0000313|EMBL:KRK77357.1};
GN ORFNames=FD30_GL000106 {ECO:0000313|EMBL:KRK77357.1};
OS Levilactobacillus namurensis DSM 19117.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Levilactobacillus.
OX NCBI_TaxID=1423773 {ECO:0000313|EMBL:KRK77357.1, ECO:0000313|Proteomes:UP000051162};
RN [1] {ECO:0000313|EMBL:KRK77357.1, ECO:0000313|Proteomes:UP000051162}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19117 {ECO:0000313|EMBL:KRK77357.1,
RC ECO:0000313|Proteomes:UP000051162};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(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:KRK77357.1}.
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DR EMBL; AZDT01000007; KRK77357.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R1K1I9; -.
DR STRING; 1423773.FD30_GL000106; -.
DR PATRIC; fig|1423773.3.peg.109; -.
DR OrthoDB; 9791132at2; -.
DR Proteomes; UP000051162; 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.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000313|EMBL:KRK77357.1};
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:KRK77357.1};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..43
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 44..436
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006406376"
FT DOMAIN 47..297
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT ACT_SITE 80
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 83
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 144
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 267
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 436 AA; 47312 MW; AAC0C86ADCCDDEF4 CRC64;
MKDGHFYIER KTLLVKSLKR WLVRLSVGLL VVTGTLPATT AQAASSKISK VPARAAYVMD
AQSGQVLYQQ NANHQYPIAS LTKLLTVYLT VKAINDGKIN WDDQVPIDSD LIRLSHNSVF
SSLRMKSSDK FTVRQLVEAA MVASSNSAAS ALGDYVAGSN AAFIQLMNQQ SQAWGINAHF
ISSSGLDNSD LDKYNYRLPG TGAKEENLVS AKAISIVAQH LLQADPQITK ISSQTQARVN
GTQIFNENGS LKGQANYDKD THIDGLKTGY TENANLCFTA TFTVDGERMI ATILGGNTTF
TAMNKLVKQV QKQYQLQPVH LTNRSVKLAN GTTVQAVPDT SQVGSWTTQG QDGGQITTSF
KPTLTPAALQ AGRVQANDQV ATLTVRDPQT GVTQEVAYRT QTPVTLFSSH QTFSRPTKVA
PAIQRLTLQT AVFALR
//
