ID A0A0Q2UU86_9RHOB Unreviewed; 432 AA.
AC A0A0Q2UU86;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=D-alanyl-D-alanine carboxypeptidase {ECO:0000313|EMBL:KQI67776.1};
GN ORFNames=AN189_13330 {ECO:0000313|EMBL:KQI67776.1};
OS Loktanella sp. 3ANDIMAR09.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Loktanella.
OX NCBI_TaxID=1225657 {ECO:0000313|EMBL:KQI67776.1, ECO:0000313|Proteomes:UP000051463};
RN [1] {ECO:0000313|EMBL:KQI67776.1, ECO:0000313|Proteomes:UP000051463}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3ANDIMAR09 {ECO:0000313|EMBL:KQI67776.1,
RC ECO:0000313|Proteomes:UP000051463};
RA Mas-Llado M., Nogales B., Bosch R.;
RT "Draft genome sequence of Loktanella sp. 3ANDIMAR09.";
RL Submitted (SEP-2015) 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:KQI67776.1}.
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DR EMBL; LJAK01000009; KQI67776.1; -; Genomic_DNA.
DR RefSeq; WP_056036935.1; NZ_LJAK01000009.1.
DR AlphaFoldDB; A0A0Q2UU86; -.
DR STRING; 1225657.AN189_13330; -.
DR PATRIC; fig|1225657.3.peg.2734; -.
DR OrthoDB; 9795979at2; -.
DR Proteomes; UP000051463; 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:SF34; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE DACC; 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:KQI67776.1};
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:KQI67776.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051463};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 13..230
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT ACT_SITE 38
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 41
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 98
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 201
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 432 AA; 46054 MW; D027293B7DF28933 CRC64;
MLSPVAAFAA PYAALVMDAR TGEVLHSRNA DTRLHPASLT KMMTLYIAFQ AIQRGEITLD
TEVRISSKAA SEPPSKLGLQ AGQTIKLRFL LRAAAVKSAN DAATAIGEAI SGSEEAFATR
MNRTAAAMGM TNTTFRNAHG LTENGHLSTA RDMSVLGRHV IYDFPQYYNL FSRRTADAGI
RQVSHTNTRF LNSYTGADGI KTGFTNAAGF NLTASAQRGQ ERIIATVFGG TSTAQRNARM
TELMDMGFNR APAVATLQRP DVPAATGTEQ VAMAGNARPT TQNGAGKTVR VTGRVSEALR
PAMRPAPEVP VALAVNTTSI EDALAEAIQV SSAPAAQPMA PAPEVVTRIS TSGGRHWGVN
VGRFNSRYEA EKVLIQVALN EMSTLEGAVR RVTQRSGGFD ANFMGLTREG ADLACRRLQA
RNQTCFMLGS EG
//
