ID A0A0T7RQA6_SALET Unreviewed; 403 AA.
AC A0A0T7RQA6;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 49.
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=dacA {ECO:0000313|EMBL:SUE48332.1};
GN ORFNames=B7N00_10520 {ECO:0000313|EMBL:EDG5017384.1}, B7N01_02515
GN {ECO:0000313|EMBL:EDG4993304.1}, B7N35_00510
GN {ECO:0000313|EMBL:EDG5124518.1}, B7N72_04205
GN {ECO:0000313|EMBL:EDG5369315.1}, B7N78_03535
GN {ECO:0000313|EMBL:EDG5278854.1}, B7N80_15395
GN {ECO:0000313|EMBL:EDG5289762.1}, B7N84_06765
GN {ECO:0000313|EMBL:EDG5266043.1}, DRU31_02540
GN {ECO:0000313|EMBL:EBS2451217.1}, E0916_05365
GN {ECO:0000313|EMBL:ECF1445395.1}, EJV93_06210
GN {ECO:0000313|EMBL:ECA2720807.1}, ERS008202_02065
GN {ECO:0000313|EMBL:CNU16641.1}, ERS008207_00527
GN {ECO:0000313|EMBL:CNT66640.1}, EWC73_15355
GN {ECO:0000313|EMBL:ECE8537564.1}, G0B02_00615
GN {ECO:0000313|EMBL:HAC6377647.1}, G0D18_16005
GN {ECO:0000313|EMBL:HAC6682125.1}, G2206_07310
GN {ECO:0000313|EMBL:HAE0434579.1}, NCTC5754_03281
GN {ECO:0000313|EMBL:SUE48332.1};
OS Salmonella enterica subsp. enterica serovar Bovismorbificans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=58097 {ECO:0000313|EMBL:SUE48332.1, ECO:0000313|Proteomes:UP000254190};
RN [1] {ECO:0000313|Proteomes:UP000039541, ECO:0000313|Proteomes:UP000042394}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3476 {ECO:0000313|EMBL:CNU16641.1,
RC ECO:0000313|Proteomes:UP000039541}, and D4891
RC {ECO:0000313|EMBL:CNT66640.1, ECO:0000313|Proteomes:UP000042394};
RG Pathogen Informatics;
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:HAC6377647.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BCW_3301 {ECO:0000313|EMBL:HAC6377647.1}, M123
RC {ECO:0000313|EMBL:HAC6682125.1}, and MS140073
RC {ECO:0000313|EMBL:HAE0434579.1};
RX PubMed=30286803;
RA Souvorov A., Agarwala R., Lipman D.J.;
RT "SKESA: strategic k-mer extension for scrupulous assemblies.";
RL Genome Biol. 19:153-153(2018).
RN [3] {ECO:0000313|EMBL:SUE48332.1, ECO:0000313|Proteomes:UP000254190}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC5754 {ECO:0000313|EMBL:SUE48332.1,
RC ECO:0000313|Proteomes:UP000254190};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:HAE0434579.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BCW_3301 {ECO:0000313|EMBL:HAC6377647.1}, M123
RC {ECO:0000313|EMBL:HAC6682125.1}, and MS140073
RC {ECO:0000313|EMBL:HAE0434579.1};
RG NCBI Pathogen Detection Project;
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:ECF1445395.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=136768 {ECO:0000313|EMBL:EDG4993304.1}, 138330
RC {ECO:0000313|EMBL:EDG5289762.1}, 143652
RC {ECO:0000313|EMBL:EDG5369315.1}, 273631
RC {ECO:0000313|EMBL:EDG5017384.1}, 330535
RC {ECO:0000313|EMBL:EDG5266043.1}, 333944
RC {ECO:0000313|EMBL:EDG5278854.1}, 337042
RC {ECO:0000313|EMBL:EDG5124518.1}, 387147
RC {ECO:0000313|EMBL:EBS2451217.1}, 470200
RC {ECO:0000313|EMBL:ECE8537564.1}, 598023
RC {ECO:0000313|EMBL:ECA2720807.1}, and 692616
RC {ECO:0000313|EMBL:ECF1445395.1};
RA Ashton P.M., Dallman T., Nair S., De Pinna E., Peters T., Grant K.;
RL Submitted (MAR-2019) 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}.
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DR EMBL; CQPD01000003; CNT66640.1; -; Genomic_DNA.
DR EMBL; CQPC01000023; CNU16641.1; -; Genomic_DNA.
DR EMBL; AAGUWJ010000002; EBS2451217.1; -; Genomic_DNA.
DR EMBL; AAHTVM010000003; ECA2720807.1; -; Genomic_DNA.
DR EMBL; AAIJHK010000014; ECE8537564.1; -; Genomic_DNA.
DR EMBL; AAIKGE010000003; ECF1445395.1; -; Genomic_DNA.
DR EMBL; AAMEJW010000002; EDG4993304.1; -; Genomic_DNA.
DR EMBL; AAMEJY010000005; EDG5017384.1; -; Genomic_DNA.
DR EMBL; AAMEKY010000001; EDG5124518.1; -; Genomic_DNA.
DR EMBL; AAMEMC010000003; EDG5266043.1; -; Genomic_DNA.
DR EMBL; AAMEMH010000002; EDG5278854.1; -; Genomic_DNA.
DR EMBL; AAMEML010000017; EDG5289762.1; -; Genomic_DNA.
DR EMBL; AAMEMP010000003; EDG5369315.1; -; Genomic_DNA.
DR EMBL; DAAMEZ010000001; HAC6377647.1; -; Genomic_DNA.
DR EMBL; DAAMHM010000012; HAC6682125.1; -; Genomic_DNA.
DR EMBL; DAAQQK010000006; HAE0434579.1; -; Genomic_DNA.
DR EMBL; UGVQ01000002; SUE48332.1; -; Genomic_DNA.
DR RefSeq; WP_000858711.1; NZ_WFIN01000003.1.
DR AlphaFoldDB; A0A0T7RQA6; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000039541; Unassembled WGS sequence.
DR Proteomes; UP000042394; Unassembled WGS sequence.
DR Proteomes; UP000254190; Unassembled WGS sequence.
DR Proteomes; UP000839929; 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:SF27; 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:SUE48332.1}; Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:SUE48332.1};
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..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..403
FT /note="serine-type D-Ala-D-Ala carboxypeptidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015044934"
FT DOMAIN 292..383
FT /note="Peptidase S11 D-Ala-D-Ala carboxypeptidase A C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00936"
FT ACT_SITE 73
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 76
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 139
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 242
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 403 AA; 44457 MW; 396FA1626ECF2CB8 CRC64;
MKTTFSARFM QRMALTTALC AAFISTAHAD DLNIKTMIPG VPQIDAESYI LIDYNSGKVL
AEQNADERRD PASLTKMMTS YVIGQAMKAG KFKETDLVTV GNDAWATGNP VFKGSSLMFL
KPGMQVPVSQ LIRGINLQSG NDACVAMADF AAGSQDAFVG LMNSYVNALG LKNTHFQTVH
GLDADGQYSS ARDMALIGQA LIRDVPNEYA VYKEKEFTFN GIRQLNRNGL LWDNSLNVDG
IKTGHTSKAG YNLVASATEG QMRLISAVMG GRTYKGRETE SKKLLTWGFR FFETVNPLKA
GKEFASEPAW FGNTDRASLG VDKDVYLTIP RGRMKDLKAS YVLNTAELHA PLQKNQVVGT
INFQLDGKTI EQRPLVVLQE IPEGNFFGKI IDYIKLMFHH WFG
//
