ID M8DK50_9BACI Unreviewed; 442 AA.
AC M8DK50;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 30.
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=H919_13685 {ECO:0000313|EMBL:EMT44760.1};
OS Anoxybacillus flavithermus AK1.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Anoxybacillus.
OX NCBI_TaxID=1297581 {ECO:0000313|EMBL:EMT44760.1, ECO:0000313|Proteomes:UP000012085};
RN [1] {ECO:0000313|EMBL:EMT44760.1, ECO:0000313|Proteomes:UP000012085}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK1 {ECO:0000313|EMBL:EMT44760.1,
RC ECO:0000313|Proteomes:UP000012085};
RA Rajan I., PoliReddy D., Sugumar T., Rathinam K., Alqarawi S., Khalil A.B.,
RA Sivakumar N.;
RT "Assembly of a new bacterial strain Anoxybacillus flavithermus AK1.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EMT44760.1, ECO:0000313|Proteomes:UP000012085}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK1 {ECO:0000313|EMBL:EMT44760.1,
RC ECO:0000313|Proteomes:UP000012085};
RX PubMed=26044438;
RA Khalil A., Sivakumar N., Qarawi S.;
RT "Genome Sequence of Anoxybacillus flavithermus Strain AK1, a Thermophile
RT Isolated from a Hot Spring in Saudi Arabia.";
RL Genome Announc. 3:e00604-15(2015).
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:EMT44760.1}.
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DR EMBL; APCD01000044; EMT44760.1; -; Genomic_DNA.
DR AlphaFoldDB; M8DK50; -.
DR PATRIC; fig|1297581.3.peg.2746; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000012085; 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:SF11; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE DACA; 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 ECO:0000313|EMBL:EMT44760.1}; 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}.
FT DOMAIN 308..412
FT /note="Peptidase S11 D-Ala-D-Ala carboxypeptidase A C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00936"
FT ACT_SITE 64
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 67
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 128
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 253
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 442 AA; 49645 MW; 9B50B27A38425D95 CRC64;
MKTWYKRFII SIVAMFLFMG TLPQNIKAEE DVLNIEADAA ILVEAETGKI LYQKNIDAVL
GIASMTKMMT EYLLLEAIHE GRVKWDQEYA VSEYVYQISQ KRDLSNVPLR RDGKYTVREL
YEAMAIYSAN GATVAIAEIV GGSETNFVKM MNEKAKQLGL KDYKFVNATG LNNKDLGGLH
PAGSGDNEEN VMSARDVATL AYHLYHQFPE ILDTASIPRK FFREGTDDQI KMDNWNWMLP
GLVAAYEGVD GIKTGYTEFA GYCFTGTAER NGMRFITVVM NAKTNGKGTH MSRFQETRKM
LDYAFSNYTV QQLYPKGYIT KKHETVAVKK GKEKQVAVAT KKPLSLVMKR GEEKKYKPVV
VIEKETLTAP VKKGQKVGYM YVKYEGTDYG YLTKEGEKAV QVDIVTKQAV EKANGFVLAM
RAIGELFGDI WNGAANAIKG LF
//
