ID I2BAV3_SHIBC Unreviewed; 406 AA.
AC I2BAV3; K6VBZ0;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=serine-type D-Ala-D-Ala carboxypeptidase {ECO:0000256|ARBA:ARBA00012448};
DE EC=3.4.16.4 {ECO:0000256|ARBA:ARBA00012448};
GN Name=dacC {ECO:0000313|EMBL:AFJ47657.1};
GN OrderedLocusNames=EBL_c25710 {ECO:0000313|EMBL:AFJ47657.1};
OS Shimwellia blattae (strain ATCC 29907 / DSM 4481 / JCM 1650 / NBRC 105725 /
OS CDC 9005-74) (Escherichia blattae).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shimwellia.
OX NCBI_TaxID=630626 {ECO:0000313|EMBL:AFJ47657.1, ECO:0000313|Proteomes:UP000001955};
RN [1] {ECO:0000313|EMBL:AFJ47657.1, ECO:0000313|Proteomes:UP000001955}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29907 / DSM 4481 / JCM 1650 / NBRC 105725 / CDC 9005-74
RC {ECO:0000313|Proteomes:UP000001955};
RX PubMed=22843577; DOI=10.1128/JB.00829-12;
RA Brzuszkiewicz E., Waschkowitz T., Wiezer A., Daniel R.;
RT "Complete genome sequence of the B12-producing Shimwellia blattae strain
RT DSM 4481, isolated from a cockroach.";
RL J. Bacteriol. 194:4436-4436(2012).
CC -!- FUNCTION: Removes C-terminal D-alanyl residues from sugar-peptide cell
CC wall precursors. {ECO:0000256|ARBA:ARBA00003217}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also
CC transpeptidation of peptidyl-alanyl moieties that are N-acyl
CC substituents of D-alanine.; EC=3.4.16.4;
CC Evidence={ECO:0000256|ARBA:ARBA00034000};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752}.
CC -!- SIMILARITY: Belongs to the peptidase S11 family.
CC {ECO:0000256|ARBA:ARBA00007164, ECO:0000256|RuleBase:RU004016}.
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DR EMBL; CP001560; AFJ47657.1; -; Genomic_DNA.
DR RefSeq; WP_002439446.1; NZ_BAHA01000003.1.
DR AlphaFoldDB; I2BAV3; -.
DR STRING; 630626.EBL_c25710; -.
DR MEROPS; S11.003; -.
DR KEGG; ebt:EBL_c25710; -.
DR PATRIC; fig|630626.3.peg.2497; -.
DR eggNOG; COG1686; Bacteria.
DR HOGENOM; CLU_027070_8_1_6; -.
DR OrthoDB; 9795979at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000001955; Chromosome.
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-UniPathway.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR Gene3D; 2.60.410.10; D-Ala-D-Ala carboxypeptidase, C-terminal domain; 1.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR015956; Peniciliin-bd_prot_C_sf.
DR InterPro; IPR018044; Peptidase_S11.
DR InterPro; IPR012907; Peptidase_S11_C.
DR InterPro; IPR037167; Peptidase_S11_C_sf.
DR InterPro; IPR001967; Peptidase_S11_N.
DR PANTHER; PTHR21581; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE; 1.
DR PANTHER; PTHR21581:SF34; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE DACC; 1.
DR Pfam; PF07943; PBP5_C; 1.
DR Pfam; PF00768; Peptidase_S11; 1.
DR PRINTS; PR00725; DADACBPTASE1.
DR SMART; SM00936; PBP5_C; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF69189; Penicillin-binding protein associated domain; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
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:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000001955};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..406
FT /note="serine-type D-Ala-D-Ala carboxypeptidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003656084"
FT DOMAIN 291..382
FT /note="Peptidase S11 D-Ala-D-Ala carboxypeptidase A C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00936"
FT ACT_SITE 72
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 75
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 138
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 241
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 406 AA; 44038 MW; 04C1377A33E02DF1 CRC64;
MAFMKNTLSS SWRKWVAGTT LLLLMAPVVH GADAPGAPGA PPLDAKAWIL MDYASGKVLA
QGNADEKLDP ASLTKLMTSY VVGHALKAGK IKLTDMVTVG QDAWATGNPA LRGSSVMFLK
PGDRVSVEDL NKGVIIQSGN DACIALADYV AGSQDSFISL MNGYAQKLGL QNTVFKTVHG
LDAPGQFSTA RDMALLGQAL IRDVPDEYAV HKEKEFTFNK IRQPNRNRLL WNSHLTVDGM
KTGTTAGAGY NLVASATQGD MRLISVVLGT RTDGIRFRES EKLLTWGFRF WETVTPIKPD
ATFVTQKVWY GDTGEAKLGA GSQGSITIPR GQMKNLKASY TLTEPQLTAP LKKGQVVGTI
DFQLNGKSIE QRPLIVMEAV EEGGFFSRII DFVMMKLHGW FGSLFS
//
