ID A0A1N7PLX0_9RHOB Unreviewed; 530 AA.
AC A0A1N7PLX0;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=D-alanyl-D-alanine carboxypeptidase {ECO:0000313|EMBL:SIT11643.1};
GN ORFNames=SAMN05421580_110121 {ECO:0000313|EMBL:SIT11643.1};
OS Rhodobacter aestuarii.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodobacter.
OX NCBI_TaxID=453582 {ECO:0000313|EMBL:SIT11643.1, ECO:0000313|Proteomes:UP000186221};
RN [1] {ECO:0000313|Proteomes:UP000186221}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19945 {ECO:0000313|Proteomes:UP000186221};
RA Varghese N., Submissions S.;
RL Submitted (JAN-2017) 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; FTOG01000010; SIT11643.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1N7PLX0; -.
DR STRING; 453582.SAMN05421580_110121; -.
DR OrthoDB; 9795979at2; -.
DR Proteomes; UP000186221; 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:SIT11643.1};
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:SIT11643.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000186221};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 11..228
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT REGION 257..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 36
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 39
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 96
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 199
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 530 AA; 55479 MW; AF5A7617860F26A2 CRC64;
MPVALWAAPF AAYVIDARSG EVLYAKNAET RLHPASLTKM MTLYIAFQEI EAGRLSLDTM
VTVSANAAGQ PPSRVGLKAG QKIALRYLIR AAAVKSANDA AAAIGDFIGG DEAKFAARMT
RTARALGMTK TTFKNANGLT REGHLSTAHD MTTLGRHLLF DFPQYYNLFS RRSADAGIAR
VYNTNRRFLD AYEGADGIKT GYTVAAGFNL VGSAKRGNKR IIATVFGGTS TASRNAKMAE
LLDLGFARAP NRARTVTPEP APMLLADAAP TSAPPALKRS PRPMERPAPA SPEIAAAIDT
DAIAAAVALA AAAPTPAPAP EPVQAAEPQE TVAATIQVAQ AQPNTLRPAP KPAHTAPVQL
ALAEDEPAGL VEVTAPQPET LAMLETDDSV LAQGDTDATA PIFIQTATAQ PETLAMSRSQ
ASRNDTVILA ALTPPAPMPQ ARREVVARAS SSGGRQWGVS LGKYNSQYAA EQVLLKTALM
ESTSLGEGLR KVASRPAGHE ALFVGLTRAD ADLACARLSA RAVDCTVIGP
//
