ID A0A0F0CGT5_9CLOT Unreviewed; 539 AA.
AC A0A0F0CGT5;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=D-alanyl-D-alanine carboxypeptidase DacB {ECO:0000313|EMBL:KJJ75540.1};
DE EC=3.4.16.4 {ECO:0000313|EMBL:KJJ75540.1};
GN Name=dacB_2 {ECO:0000313|EMBL:KJJ75540.1};
GN ORFNames=CLFS41_06370 {ECO:0000313|EMBL:KJJ75540.1};
OS Clostridium sp. FS41.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1609975 {ECO:0000313|EMBL:KJJ75540.1, ECO:0000313|Proteomes:UP000033604};
RN [1] {ECO:0000313|EMBL:KJJ75540.1, ECO:0000313|Proteomes:UP000033604}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FS41 {ECO:0000313|EMBL:KJJ75540.1,
RC ECO:0000313|Proteomes:UP000033604};
RA Poehlein A., Daniel R.;
RT "Genome sequencing of Clostridium sp. FS41.";
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
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:KJJ75540.1}.
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DR EMBL; JYHN01000025; KJJ75540.1; -; Genomic_DNA.
DR RefSeq; WP_045091436.1; NZ_JYHN01000025.1.
DR AlphaFoldDB; A0A0F0CGT5; -.
DR PATRIC; fig|1609975.3.peg.685; -.
DR Proteomes; UP000033604; Unassembled WGS sequence.
DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
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; 2.10.270.10; Cholin Binding; 1.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR018337; Cell_wall/Cho-bd_repeat.
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; PF01473; Choline_bind_1; 1.
DR Pfam; PF19085; Choline_bind_2; 1.
DR Pfam; PF19127; Choline_bind_3; 1.
DR Pfam; PF00768; Peptidase_S11; 1.
DR PRINTS; PR00725; DADACBPTASE1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF69360; Cell wall binding repeat; 1.
DR PROSITE; PS51170; CW; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000313|EMBL:KJJ75540.1};
KW Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KJJ75540.1};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW Protease {ECO:0000313|EMBL:KJJ75540.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000033604};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..539
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002437156"
FT DOMAIN 126..362
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT REPEAT 477..496
FT /note="Cell wall-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00591"
FT REGION 42..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 386..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 161
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 164
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 219
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 332
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 539 AA; 55518 MW; 3D6C67BF07D1DB80 CRC64;
MRSKQWKSFL CICTSCALLM STAVYANPVV IAPLEESQVA SVQSGGQSGS PASNQGPSGS
GDAGTVSSSG PAADNTAGQP SSGASPTEAG NGISPGAPGT GSQGNTGNNT TGNNVTGNIG
TVDTSAIQQP VVAAEGAVLM DAATGNVLFS KNGETKYYPA SITKLMTALL VAENCGLDDK
VTFSATATTN LESGAVSINM TEGDVMTVRQ CLYALLLKSA NEVGNALAEH VAGSNAQFAE
KMNAKAAALG CTNTHFTNPH GLNDSNHYTT PHDMALIARA AFQNDIVKTV ASTRTYSLPA
TIKNPSGLTV SIGHKMLNPS DSRYYEGVIG GKTGYTSKAG NTLVTAAEKD GVRLIAVVMK
AKSTHYTDTK SMFDYGFELA KAGALGSSDS SGTGPSSTGN AGNGTVGNSS TGTNNTATNN
TGTNSTGNSG PGTAAGQGWV QDATGWYYVK DNGSKAVNEW LTLDGVSYWI DSNSYMAKGW
RQINGIWYFL RSNGAMAKNQ WEKVDENGLW FYLGPDGAML TNTTTPDGHY VGSDGAWVE
//
