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Database: UniProt
Entry: W4APB2_9BACL
LinkDB: W4APB2_9BACL
Original site: W4APB2_9BACL 
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
//
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