ID A0A1H3R177_9RHOB Unreviewed; 422 AA.
AC A0A1H3R177;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=D-alanyl-D-alanine carboxypeptidase {ECO:0000313|EMBL:SDZ19346.1};
GN ORFNames=SAMN05444004_107110 {ECO:0000313|EMBL:SDZ19346.1};
OS Jannaschia faecimaris.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Jannaschia.
OX NCBI_TaxID=1244108 {ECO:0000313|EMBL:SDZ19346.1, ECO:0000313|Proteomes:UP000198914};
RN [1] {ECO:0000313|EMBL:SDZ19346.1, ECO:0000313|Proteomes:UP000198914}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 100420 {ECO:0000313|EMBL:SDZ19346.1,
RC ECO:0000313|Proteomes:UP000198914};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FNPX01000007; SDZ19346.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H3R177; -.
DR STRING; 1244108.SAMN05444004_107110; -.
DR OrthoDB; 9795979at2; -.
DR Proteomes; UP000198914; 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:SDZ19346.1};
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:SDZ19346.1};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..422
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011627595"
FT DOMAIN 31..249
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT REGION 276..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 56
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 59
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 116
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 219
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 422 AA; 45377 MW; D75C8AEEFD667CD1 CRC64;
MNMIRTVLLG LATFCAIWLA AIPMAKAAPY AEMVIDARTG EVIRSRNADT RLHPASLTKM
MTLYIAFEAV RQGEITLDTE VRVSRNAANE VPSKLGLRSG QRIAFRYLIR AAAVKSANDA
ATAIGEAIAG SESAFAERMT RTARALGMTN TTFRNAHGLT ASGHLSTARD MTTLGRRLFY
DYPQYYNLFS RRTTDAGVTR VRNTNRRLLD AYRGADGIKT GYTSAAGFNL VSSAERGGVR
IIATVFGGRS TATRNERIAE LLDLGFANAP QHVTERRPSL PVYGGPTTTG PTAPAVSMRP
QMRGTPSGGT VYASASAPTV SVVQPEPRPE GEPARVVVTR ASTAGNEYGI ALSSQGSRSA
ADKLLLRTAL QELDTLDQAL RRVDRVRNGF APSFVGLSQR SAERACTRLR ARDVDCDVVI
GG
//
