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Database: UniProt
Entry: A0A0T9P118_9GAMM
LinkDB: A0A0T9P118_9GAMM
Original site: A0A0T9P118_9GAMM 
ID   A0A0T9P118_9GAMM        Unreviewed;       403 AA.
AC   A0A0T9P118;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 24.
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:CNH40307.1};
GN   ORFNames=ERS008529_01140 {ECO:0000313|EMBL:CNH40307.1};
OS   Yersinia pekkanenii.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=1288385 {ECO:0000313|EMBL:CNH40307.1, ECO:0000313|Proteomes:UP000045840};
RN   [1] {ECO:0000313|Proteomes:UP000045840}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A125KOH2 {ECO:0000313|Proteomes:UP000045840};
RG   Pathogen Informatics;
RL   Submitted (MAR-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}.
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DR   EMBL; CQAZ01000008; CNH40307.1; -; Genomic_DNA.
DR   RefSeq; WP_049611091.1; NZ_CWJL01000008.1.
DR   AlphaFoldDB; A0A0T9P118; -.
DR   STRING; 1288385.ERS137968_02051; -.
DR   OrthoDB; 9795979at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000045840; 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:CNH40307.1}; Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CNH40307.1};
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..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..403
FT                   /note="serine-type D-Ala-D-Ala carboxypeptidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006694224"
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;  44385 MW;  FC6A907EC3D17B79 CRC64;
     MKYVTTSRII KSLALGTVIV MSTASAANAD DVNLKTMIPG VPQIDAEAYV LIDYNSGKVL
     AEMNADARRN PASLTKMMTS YVIGQAIKAG KIGPEDMVTV GKDAWATGNP EFKGSSLMFL
     KPGDRVPVSK LTRGINLQSG NDACVAMADY VAGSQDSFVN LMNNYVKALG LQNTQFKTVH
     GLDAEGQYSS ARDMALIGQA LIRDVPDEYA IYKEKEFTFN NIRQMNRNGL LWDTSLNVDG
     IKTGHTEAAG YNLVASATDG QMRLISAVLG GHTYKGRETE SKKLLTWGFR FFETVAPLKV
     GKEFASEPVW FGDSDRVQLG VDKDVYLTIP RGRMKDLKAS YVLNTPEIHA PLAKNQVVGM
     INFQLDGKTI DQRPLVVMNE VKEGGFFSRM VDYIKLMFHR WFG
//
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