ID W4APB2_9BACL Unreviewed; 395 AA.
AC W4APB2;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=D-alanyl-D-alanine carboxypeptidase {ECO:0000313|EMBL:ETT33323.1};
GN ORFNames=C161_19932 {ECO:0000313|EMBL:ETT33323.1};
OS Paenibacillus sp. FSL R5-192.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1226754 {ECO:0000313|EMBL:ETT33323.1, ECO:0000313|Proteomes:UP000019041};
RN [1] {ECO:0000313|EMBL:ETT33323.1, ECO:0000313|Proteomes:UP000019041}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL R5-192 {ECO:0000313|EMBL:ETT33323.1,
RC ECO:0000313|Proteomes:UP000019041};
RX PubMed=24422886; DOI=10.1186/1471-2164-15-26;
RA Moreno Switt A.I., Andrus A.D., Ranieri M.L., Orsi R.H., Ivy R.,
RA den Bakker H.C., Martin N.H., Wiedmann M., Boor K.J.;
RT "Genomic comparison of sporeforming bacilli isolated from milk.";
RL BMC Genomics 15:26-26(2014).
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:ETT33323.1}.
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DR EMBL; ASPR01000042; ETT33323.1; -; Genomic_DNA.
DR RefSeq; WP_036672259.1; NZ_ASPR01000042.1.
DR AlphaFoldDB; W4APB2; -.
DR PATRIC; fig|1226754.4.peg.4044; -.
DR Proteomes; UP000019041; 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:SF32; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE DACB; 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:ETT33323.1};
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:ETT33323.1};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..395
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004837730"
FT DOMAIN 29..255
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT ACT_SITE 64
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 67
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 119
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 226
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 395 AA; 43214 MW; B3AD71B9B0E3BA6B CRC64;
MRKITKVIAC MLIPVFLLSS LGATQAQATI QGPSTHAQSA ALIDVTSGRI LYSKDGDKEL
RIASLTKIMT AIVAIEHSRL DDKVKVSPTA FAKEGSSLYL KLGEEMTLEN MLYGLMLRSG
NDAASAIAEH VGGSEEGFVL LMNKKAEQIG LTHSHFMNPH GLDAEGHYST ANDLARLTAY
ALHNPVFKRI VATEDKSAPN PNESWEYSWH NKNKMLRMYE GADGVKTGYT KKAFRCLVSS
ATRNGQQLAA VTLNDGNDWN DHARMLDFGF EYFPLVEVAK QEQPVQNTDV VTGRGFWYPL
AKSEQGSLTK KLILHENRGQ SETEGKEQST DPSFGLAGRI DMQLDGKLVG SIPVYRKGSY
IPPEPKTEDA TLGGIGDVSS WAAAWRAVLS HLLSP
//