ID A0A1S2QJ56_9ACTN Unreviewed; 303 AA.
AC A0A1S2QJ56;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=D-alanyl-D-alanine carboxypeptidase {ECO:0000313|EMBL:OIK05703.1};
GN ORFNames=BIV23_10220 {ECO:0000313|EMBL:OIK05703.1};
OS Streptomyces monashensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1678012 {ECO:0000313|EMBL:OIK05703.1, ECO:0000313|Proteomes:UP000179642};
RN [1] {ECO:0000313|EMBL:OIK05703.1, ECO:0000313|Proteomes:UP000179642}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUSC 1 {ECO:0000313|EMBL:OIK05703.1,
RC ECO:0000313|Proteomes:UP000179642};
RA Lee L.-H., Ser H.-L., Law J.W.-F.;
RT "Genome sequence of Streptomyces sp. MUSC 1.";
RL Submitted (OCT-2016) 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:OIK05703.1}.
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DR EMBL; MLYO01000018; OIK05703.1; -; Genomic_DNA.
DR RefSeq; WP_071380483.1; NZ_MLYO01000018.1.
DR AlphaFoldDB; A0A1S2QJ56; -.
DR OrthoDB; 3530815at2; -.
DR Proteomes; UP000179642; 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: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:OIK05703.1};
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:OIK05703.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000179642};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..39
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 40..303
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010204180"
FT DOMAIN 38..280
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT ACT_SITE 74
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 77
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 135
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 252
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 303 AA; 31635 MW; 09213B1557B35982 CRC64;
MITGIHGTRR TRIRRGAAVA VTSGALLATG ALTAVPAQAV TAPSIVAAGG YVMNSANGAS
LYTKAADTKR STGSTTKIMT AKVVLAQSNL NLDKKVTIQK AYSDYVVKNN ASQAHLIVGD
KVTVRQLLYG LMLPSGCDAA YALADTYGSG STRDARVRNF IGKMNTAAKS LGLKNTSFDS
FDGIGNGNNF STPRDLTKIA SSAMKNATFR AIVKTKAYTA KTVTKTGSTR TMATWTNTNG
LLSSYSGTIG VKTGSGPEAK YCLVFAATRN GRTVIGTVLA STSIPQRESD AKKLLSYGFA
RLG
//
