ID A0A2A4FW31_9SPHN Unreviewed; 392 AA.
AC A0A2A4FW31;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
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 ORFNames=COO09_10415 {ECO:0000313|EMBL:PCE42404.1};
OS Rhizorhabdus dicambivorans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Rhizorhabdus.
OX NCBI_TaxID=1850238 {ECO:0000313|EMBL:PCE42404.1, ECO:0000313|Proteomes:UP000218934};
RN [1] {ECO:0000313|EMBL:PCE42404.1, ECO:0000313|Proteomes:UP000218934}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ndbn-20m {ECO:0000313|EMBL:PCE42404.1,
RC ECO:0000313|Proteomes:UP000218934};
RA Na L.;
RT "The Catabolism of 3,6-Dichlorosalicylic acid is Initiated by the
RT Cytochrome P450 Monooxygenase DsmABC in Rhizorhabdus dicambivorans
RT Ndbn-20.";
RL Submitted (SEP-2017) 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:PCE42404.1}.
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DR EMBL; NWUF01000008; PCE42404.1; -; Genomic_DNA.
DR RefSeq; WP_066963507.1; NZ_NWUF01000008.1.
DR AlphaFoldDB; A0A2A4FW31; -.
DR KEGG; rdi:CMV14_13365; -.
DR OrthoDB; 9795979at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000218934; 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:SF34; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE DACC; 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:PCE42404.1}; 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:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000218934};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..392
FT /note="serine-type D-Ala-D-Ala carboxypeptidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012607505"
FT DOMAIN 284..374
FT /note="Peptidase S11 D-Ala-D-Ala carboxypeptidase A C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00936"
FT ACT_SITE 58
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 61
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 123
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 234
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 392 AA; 42107 MW; E1D60C3AFCCBAAB6 CRC64;
MKRSKIALFS GLLLGLAIPA EAAAPPFDTP APVAFLKDLS SGAILYAKNP DVRMPPASMA
KMMTVYVAFD LIKKGELKLD AMATVRPETW KRWHGPAAGS TMFLSPGEQV SVANLLFGIV
TLSGNDACVV LAEHISGTEQ AFIALMNRRA KEMGLTNSHF GTSNGWPDGG VTYVTARDLT
TLAEKTITEH PKLYKTFYSR PNFTWGKTMG SGQAITQANR DPLLGRVDGA DGLKTGHTEE
AGYGFTGSAE QNGRRLVMVL SGLTSFNQRI EQSVSFMNWG FRAWQAKPIV PKGRKVQTAE
VQLGDVSEVG LVAPKDLTVT IPAGLGSDLK TKVVYQGPIK APFKKGDHIA DLVVTGPDMA
PQKLPLVADA DVGTAGFFDR MMAGLRWLFG FG
//
