ID R1HCM6_9GAMM Unreviewed; 400 AA.
AC R1HCM6;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=G113_05208 {ECO:0000313|EMBL:EOD56149.1};
OS Aeromonas molluscorum 848.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Aeromonas.
OX NCBI_TaxID=1268236 {ECO:0000313|EMBL:EOD56149.1, ECO:0000313|Proteomes:UP000013526};
RN [1] {ECO:0000313|EMBL:EOD56149.1, ECO:0000313|Proteomes:UP000013526}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=848 {ECO:0000313|EMBL:EOD56149.1,
RC ECO:0000313|Proteomes:UP000013526};
RX PubMed=23788549;
RA Spataro N., Farfan M., Albarral V., Sanglas A., Loren J.G., Fuste M.C.,
RA Bosch E.;
RT "Draft Genome Sequence of Aeromonas molluscorum Strain 848TT, Isolated from
RT Bivalve Molluscs.";
RL Genome Announc. 1:E00382-13(2013).
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:EOD56149.1}.
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DR EMBL; AQGQ01000019; EOD56149.1; -; Genomic_DNA.
DR RefSeq; WP_005894660.1; NZ_AQGQ01000019.1.
DR AlphaFoldDB; R1HCM6; -.
DR PATRIC; fig|1268236.3.peg.1038; -.
DR OrthoDB; 9795979at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000013526; 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 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 Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..400
FT /note="serine-type D-Ala-D-Ala carboxypeptidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004361030"
FT DOMAIN 290..380
FT /note="Peptidase S11 D-Ala-D-Ala carboxypeptidase A C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00936"
FT ACT_SITE 73
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 76
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 136
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 239
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 400 AA; 43643 MW; 2DA3033DB0763242 CRC64;
MSKFSHSVIL AALISATAQA NTPTPDALPT PNSMPVVVPA APTISAKAHI LIDYASGQIL
AEENAEERLP PASLTKMMTS YIIGQELLKG NIKRTDMVTI SQNAWSKNYS DSSKMFIEVG
KQVSVDDLNK GIIIQSGNDA CVAMAEFLAG STDSFASLMN TWSAKLGMND SHFMNPHGLD
AEGHYSTAHD MARLGQALIR DLPEEYKIYS QKSFVFNGIT QHNRNRLLWD QSLQVDGIKT
GHVSQVGYNL VSSATNNEGM RLIAVVFGAS SEASRAAESK KLLTYGFRFF QSSTPYKAGT
ELVSQKIWMG DKPEVKLGVD QDVSVVVTRG QASNLKADFQ LDSELKAPLA KGQKVGTVFL
KQGDKEIKQV PLVALEDVQE GGLMSRLWDY VVLLVTSWFK
//
