ID A0A1X4J1Z2_9RHOB Unreviewed; 394 AA.
AC A0A1X4J1Z2;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-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=BV911_01455 {ECO:0000313|EMBL:OSP56650.1};
OS Pseudoruegeria sp. SK021.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Pseudoruegeria.
OX NCBI_TaxID=1933035 {ECO:0000313|EMBL:OSP56650.1, ECO:0000313|Proteomes:UP000194129};
RN [1] {ECO:0000313|EMBL:OSP56650.1, ECO:0000313|Proteomes:UP000194129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK021 {ECO:0000313|EMBL:OSP56650.1,
RC ECO:0000313|Proteomes:UP000194129};
RA Pohlner M., Marshall I., Schreiber L., Cypionka H., Engelen B.;
RT "Draft genome sequence of Pseudoruegeria str. SK021, a representative of
RT the marine Rosebacter group, isolated from North Sea sediment.";
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
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:OSP56650.1}.
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DR EMBL; MTBG01000001; OSP56650.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X4J1Z2; -.
DR STRING; 1933035.BV911_01455; -.
DR OrthoDB; 9795979at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000194129; 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; 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.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000313|EMBL:OSP56650.1};
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:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000194129};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..394
FT /note="serine-type D-Ala-D-Ala carboxypeptidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012259362"
FT DOMAIN 278..368
FT /note="Peptidase S11 D-Ala-D-Ala carboxypeptidase A C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00936"
FT ACT_SITE 62
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 65
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 123
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 228
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 394 AA; 42935 MW; 3ECA2D16C7905713 CRC64;
MPTRNSNVRH LVTPLIASLV FAFPGMAQVG FETQAGAAYV VDVGTDTVLF EKNPDASLPP
ASMSKLMTLL MLFESLRDNP NVTLDTRFGV STKAREMGGS TMFLNERDRP TVEELIQGII
VQSGNDATVV VAEGLAGTED AFARMMNDRA KALGMENSTF ANASGWPDPN HRMSVKDLAF
VAEHLIRDFP EYYGYFSQAE YPFDGRAPQN RFNRNPLLKL GIGADGLKTG HTQEAGYGLV
GSAAQGNRRV IFVISGLPTA EARAEEAERV VSWAFRQFLE TKLAEEGDLI AEAPVWMGNL
QSVGLVVPKD VTFLNQAAFA NDYTTEVVYR SPLQAPIAKG DEIGQLVITR TGLPDSRIPL
VAERDVAQGG LIPRMRSATQ VLYNRLAGEA KDLF
//
