ID A0A1C6TZI8_9ACTN Unreviewed; 428 AA.
AC A0A1C6TZI8;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=D-alanyl-D-alanine carboxypeptidase (Penicillin-binding protein 5/6) {ECO:0000313|EMBL:SCL47252.1};
GN ORFNames=GA0070603_0339 {ECO:0000313|EMBL:SCL47252.1};
OS Micromonospora chersina.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=47854 {ECO:0000313|EMBL:SCL47252.1, ECO:0000313|Proteomes:UP000198605};
RN [1] {ECO:0000313|EMBL:SCL47252.1, ECO:0000313|Proteomes:UP000198605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44151 {ECO:0000313|EMBL:SCL47252.1,
RC ECO:0000313|Proteomes:UP000198605};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-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; FMIB01000002; SCL47252.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C6TZI8; -.
DR STRING; 47854.GA0070603_0339; -.
DR OrthoDB; 3663940at2; -.
DR Proteomes; UP000198605; 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:SF33; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE DACB1; 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:SCL47252.1};
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:SCL47252.1};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..428
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008747222"
FT DOMAIN 84..316
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT REGION 27..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..61
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 118
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 121
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 175
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 286
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 428 AA; 42519 MW; 2D5FA6A4BE48E8F2 CRC64;
MRTWGPSAVL AAALLVPASM LSTPATAGTR APVRRLPAGA PPCPNVPAPA TRPPQPPPAA
DPAARAVGGA ALATAGLALP PAAPAPPAVT ATSWVVADLD TGAVLGGCGP HEYGVPASVQ
KLLLAATMLP RLDPGREVTV TAEDLAIEPG SSAVGLVAGG RYRIETIWLG LLLKSGNEAA
NALARLGGGP DGTAGGIRAM NTEARRLGAL QTHAVTPSGL DGPDQFTSAY DLALIARACF
ADPAFRRYAA TRTAQVPAQP ALRAKAFGIS NDNMLLDHYP GAIGGKTGFT DLARHTYVGA
AERGGRRLVV TVLGAEATTQ RGWQQGAALL DWGFGLPRDA AVGRLVRPGE LDRAAASPTG
AASALAGGAG LGGAGAATTG SWPGTGPSVA VGAVLVAGGA VLLARRRRHA ALAALPPGAT
SRGAPEDG
//
