ID A0A1R4FST9_9MICO Unreviewed; 416 AA.
AC A0A1R4FST9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=D-alanyl-D-alanine carboxypeptidase {ECO:0000313|EMBL:SJM58812.1};
DE EC=3.4.16.4 {ECO:0000313|EMBL:SJM58812.1};
GN ORFNames=CZ674_06335 {ECO:0000313|EMBL:SJM58812.1};
OS Agrococcus casei LMG 22410.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Agrococcus.
OX NCBI_TaxID=1255656 {ECO:0000313|EMBL:SJM58812.1, ECO:0000313|Proteomes:UP000195787};
RN [1] {ECO:0000313|EMBL:SJM58812.1, ECO:0000313|Proteomes:UP000195787}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 22410 {ECO:0000313|EMBL:SJM58812.1,
RC ECO:0000313|Proteomes:UP000195787};
RA Peterson S.W.;
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S11 family.
CC {ECO:0000256|ARBA:ARBA00007164, ECO:0000256|RuleBase:RU004016}.
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DR EMBL; FUHU01000026; SJM58812.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R4FST9; -.
DR OrthoDB; 5241551at2; -.
DR Proteomes; UP000195787; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008800; F:beta-lactamase activity; IEA:InterPro.
DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0030655; P:beta-lactam antibiotic catabolic process; 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 GO; GO:0046677; P:response to antibiotic; IEA:InterPro.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR000871; Beta-lactam_class-A.
DR InterPro; IPR018044; Peptidase_S11.
DR InterPro; IPR001967; Peptidase_S11_N.
DR PANTHER; PTHR35333; BETA-LACTAMASE; 1.
DR PANTHER; PTHR35333:SF3; BETA-LACTAMASE2 DOMAIN-CONTAINING PROTEIN; 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:SJM58812.1};
KW Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:SJM58812.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW Protease {ECO:0000313|EMBL:SJM58812.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000195787};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 80..289
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT REGION 38..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 157
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 256
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 416 AA; 43368 MW; 78A1EBF7389979A1 CRC64;
MAESDRRGVH PAIAGTVVLV LFVLVLYAVA SMLASPPSVA AQPKDDITGV SEEGEPLALP
RGTDAGAVAI IGHDDAIEST GDDQPLPMAS IAKIVTALVL LEEHPMEPGS DGATITMGET
DLQYYWDMVA EQGSLTDVRA GAELSQRELM ERMLVISSGN AALSLANWGF GSQEAFVEAA
ASWISEQGLE SMTVVDPVGI SADSVATAGD MARLARIAYD NETLRELLGV ERIQVFGSWA
ANSNPLLGED GVTGGKTGSL FASGSNLMLF AEREVAGTQV PVVSVVVGVT GTASVSTASL
SLLDQAYSGF REQVVLPEGT VVGEYQADWS DRVITASTAE DLTAVTWKGI EVPAAVLLQE
VEPGTLSASP GNLTVSSFGT TTSVEVKTDG VIPPPDFLYR LLHPQMAISW VAGLFG
//
