ID B7R7N3_9THEO Unreviewed; 377 AA.
AC B7R7N3;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 03-MAY-2023, entry version 57.
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 ORFNames=CDSM653_01233 {ECO:0000313|EMBL:KKC29748.1};
OS Caldanaerobacter subterraneus subsp. pacificus DSM 12653.
OC Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Caldanaerobacter.
OX NCBI_TaxID=391606 {ECO:0000313|EMBL:KKC29748.1, ECO:0000313|Proteomes:UP000010146};
RN [1] {ECO:0000313|EMBL:KKC29748.1, ECO:0000313|Proteomes:UP000010146}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12653 {ECO:0000313|EMBL:KKC29748.1,
RC ECO:0000313|Proteomes:UP000010146};
RA Gonzalez J., Sokolova T., Ferriera S., Johnson J., Kravitz S., Beeson K.,
RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KKC29748.1, ECO:0000313|Proteomes:UP000010146}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12653 {ECO:0000313|EMBL:KKC29748.1,
RC ECO:0000313|Proteomes:UP000010146};
RX PubMed=26446804; DOI=10.1186/s12864-015-1955-9;
RA Sant'Anna F.H., Lebedinsky A.V., Sokolova T.G., Robb F.T., Gonzalez J.M.;
RT "Analysis of three genomes within the thermophilic bacterial species
RT Caldanaerobacter subterraneus with a focus on carbon monoxide dehydrogenase
RT evolution and hydrolase diversity.";
RL BMC Genomics 16:757-757(2015).
RN [3] {ECO:0000313|Proteomes:UP000010146}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12653 {ECO:0000313|Proteomes:UP000010146};
RA Sant'Anna F.H., Lebedinsky A., Sokolova T., Robb F.T., Gonzalez J.M.;
RT "Genome analysis of three genomes within the thermophilic hydrogenogenic
RT bacterial species Caldanaerobacter subterraneus.";
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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:KKC29748.1}.
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DR EMBL; ABXP02000071; KKC29748.1; -; Genomic_DNA.
DR RefSeq; WP_009610241.1; NZ_ABXP02000071.1.
DR AlphaFoldDB; B7R7N3; -.
DR MEROPS; S11.005; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000010146; 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-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:SF6; TRAFFICKING PROTEIN PARTICLE COMPLEX SUBUNIT 12; 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.
DR PROSITE; PS50890; PUA; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645,
KW ECO:0000313|EMBL:KKC29748.1}; 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 Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..377
FT /note="serine-type D-Ala-D-Ala carboxypeptidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009949166"
FT DOMAIN 268..358
FT /note="Peptidase S11 D-Ala-D-Ala carboxypeptidase A C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00936"
FT ACT_SITE 55
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 58
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 115
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 218
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 377 AA; 41681 MW; 380EA7490F990EF7 CRC64;
MSKKFLALLI STFLLFNTAY ADVMNLKAKS AILMEAETGE ILYEKDIHKP LPPASVTKVM
TLLLAIEAID SGKIKVTDKV VTSKHAFDMG GTQIYLEVGE EMTVDDLMKA IAMNSANDAS
VALAEYIAGT EENFVEMMNK RAKELGAKNT TFKNATGLPE EGHLTTVYDI AMISRELVKH
PSIFKYLTNK IDSLRNGKFS LINTNKLLWR YQGVDGIKTG STSEALYCMA ATAKRGDTRL
IAVVFGAPDS ETRFNETAKL LDYGFANFET VKVASKGEVL GKIKVLKGNK EMVEGISLKD
EYVVVKKGEG KNIKKEVELK NFLTAPVSKN NPLGVLKILQ EGKLIKTVDI YPATDVKKAN
FFENFNKVIN YWIKKGS
//