ID A0A0A5HQS2_9BACI Unreviewed; 370 AA.
AC A0A0A5HQS2;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=D-alanyl-D-alanine carboxypeptidase {ECO:0000313|EMBL:KGX85962.1};
GN ORFNames=N784_06210 {ECO:0000313|EMBL:KGX85962.1};
OS Pontibacillus litoralis JSM 072002.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Pontibacillus.
OX NCBI_TaxID=1385512 {ECO:0000313|EMBL:KGX85962.1, ECO:0000313|Proteomes:UP000030401};
RN [1] {ECO:0000313|EMBL:KGX85962.1, ECO:0000313|Proteomes:UP000030401}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JSM 072002 {ECO:0000313|EMBL:KGX85962.1,
RC ECO:0000313|Proteomes:UP000030401};
RA Huang J., Wang G.;
RL Submitted (AUG-2013) 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:KGX85962.1}.
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DR EMBL; AVPG01000017; KGX85962.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A5HQS2; -.
DR STRING; 1385512.N784_06210; -.
DR eggNOG; COG1686; Bacteria.
DR OrthoDB; 9791132at2; -.
DR Proteomes; UP000030401; 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:KGX85962.1};
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:KGX85962.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030401};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 25..248
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT ACT_SITE 59
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 62
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 114
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 218
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 370 AA; 41554 MW; F9624203D1E14F5A CRC64;
MKQIISFTLI LALLIYVYPH KEKVYAKPSV SAQNAVLMEQ STGRVLFEKQ GHEKKKIASI
TKVMTAIIAI ESGKMKEEVT ISRRAVYEEG SSIYLEQGEK MKLKDLVYGL MLRSGNDAAT
AIAEHVGGSV EGFAVLMNEK ASWLGMTNTH FTNPHGLDEE EHYSTAYDMA LLTQYAMENE
TFRKISKTTL HKADSRTYAW GNKNKMLTKY YEHSTGGKTG YTKVAGRTLI STANKEGMEL
IVVTLNAPDD WNDHQYLFEW GYDNYDLRKL QQEGRVPMDF SESGEALGYI WDDVVFPLTN
EEANSVQKTT HIDKPDPLGV EASVLGKLSF NVNGEILTEV SIMADPKPIR SPFWKTSRTI
FERLMGGSNG
//
