ID A0A1H0F2K9_9BACL Unreviewed; 397 AA.
AC A0A1H0F2K9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=D-alanyl-D-alanine carboxypeptidase {ECO:0000313|EMBL:SDN88779.1};
GN ORFNames=SAMN04487897_105272 {ECO:0000313|EMBL:SDN88779.1};
OS Paenibacillus sp. yr247.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1761880 {ECO:0000313|EMBL:SDN88779.1, ECO:0000313|Proteomes:UP000198936};
RN [1] {ECO:0000313|EMBL:SDN88779.1, ECO:0000313|Proteomes:UP000198936}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YR247 {ECO:0000313|EMBL:SDN88779.1,
RC ECO:0000313|Proteomes:UP000198936};
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; FNIF01000005; SDN88779.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H0F2K9; -.
DR STRING; 1761880.SAMN04487897_105272; -.
DR OrthoDB; 9791132at2; -.
DR Proteomes; UP000198936; 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; 2.30.140.30; -; 1.
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:SDN88779.1};
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:SDN88779.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000198936};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..397
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011638514"
FT DOMAIN 28..256
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT ACT_SITE 63
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 66
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 118
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 226
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 397 AA; 44052 MW; 125891DA34F1B368 CRC64;
MKKRVRFILC CSTLISLLVA PWSQVEAAPP GIHTNAVGAS LIDVESGRIL YSEKGDTPMR
IASLTKIMTA IVAIEQGNLN DKVKVSKNAF GKEGSSIYLK LGEEMRLHDM LYGLMMRSGN
DAATAIAEHI GGSVEGFVYL MNEKARMLGM DHSHFTNPSG LDEGEGHRSS PNDMAKLTAY
ALKNTIFQEI VSTKIKKVPN PNEAWDYSWL NKNKMLSLFE GADGVKTGYT KLAKRCLISS
ATRDGQQLAV VTLNDSDDWS DHARLLQYGF KYFPLHTIVK KGDAVESTPW VVGRTFSYPL
AQGEAEQLSK KVILVDPAST AYRLAERGTL QFSLQQKSIQ SVPIYDKTSP LLQTSSQSTF
SFKESKAYQE TLLSNYGYIC RMLVQQLFTV SRSEWAD
//
