(data stored in ACNUC7421 zone)

SWISSPROT: DACA_ECO57

ID   DACA_ECO57              Reviewed;         403 AA.
AC   P0AEB4; P04287; P77106;
DT   20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-1987, sequence version 1.
DT   05-JUL-2017, entry version 89.
DE   RecName: Full=D-alanyl-D-alanine carboxypeptidase DacA;
DE            Short=DD-carboxypeptidase;
DE            Short=DD-peptidase;
DE            EC=3.4.16.4;
DE   AltName: Full=Penicillin-binding protein 5;
DE            Short=PBP-5;
DE   Flags: Precursor;
GN   Name=dacA; OrderedLocusNames=Z0777, ECs0670;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Removes C-terminal D-alanyl residues from sugar-peptide
CC       cell wall precursors. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: Preferential cleavage: (Ac)(2)-L-Lys-D-Ala-|-
CC       D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are
CC       N-acyl substituents of D-alanine.
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}. Note=N-terminal lies in
CC       the periplasmic space. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S11 family. {ECO:0000305}.
DR   EMBL; AE005174; AAG54966.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB34093.1; -; Genomic_DNA.
DR   PIR; B85563; B85563.
DR   PIR; F90712; F90712.
DR   RefSeq; NP_308697.1; NC_002695.1.
DR   RefSeq; WP_001092082.1; NZ_MWVM01000011.1.
DR   ProteinModelPortal; P0AEB4; -.
DR   SMR; P0AEB4; -.
DR   STRING; 155864.Z0777; -.
DR   PRIDE; P0AEB4; -.
DR   EnsemblBacteria; AAG54966; AAG54966; Z0777.
DR   EnsemblBacteria; BAB34093; BAB34093; BAB34093.
DR   GeneID; 917030; -.
DR   KEGG; ece:Z0777; -.
DR   KEGG; ecs:ECs0670; -.
DR   PATRIC; fig|386585.9.peg.781; -.
DR   eggNOG; ENOG4105DZ1; Bacteria.
DR   eggNOG; COG1686; LUCA.
DR   HOGENOM; HOG000086623; -.
DR   KO; K07258; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.410.10; -; 1.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR015956; Peniciliin-bd_prot-assoc.
DR   InterPro; IPR018044; Peptidase_S11.
DR   InterPro; IPR012907; Peptidase_S11_C.
DR   InterPro; IPR001967; Peptidase_S11_N.
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; SSF56601; 1.
DR   SUPFAM; SSF69189; SSF69189; 1.
PE   3: Inferred from homology;
DR   PRODOM; P0AEB4.
DR   SWISS-2DPAGE; P0AEB4.
KW   Carboxypeptidase; Cell inner membrane; Cell membrane; Cell shape;
KW   Cell wall biogenesis/degradation; Complete proteome; Hydrolase;
KW   Membrane; Peptidoglycan synthesis; Protease; Signal.
FT   SIGNAL        1     29       {ECO:0000250}.
FT   CHAIN        30    403       D-alanyl-D-alanine carboxypeptidase DacA.
FT                                /FTId=PRO_0000043391.
FT   ACT_SITE     73     73       Acyl-ester intermediate. {ECO:0000250}.
FT   ACT_SITE     76     76       Proton acceptor. {ECO:0000250}.
FT   ACT_SITE    139    139       {ECO:0000250}.
FT   BINDING     242    242       Substrate. {ECO:0000250}.
FT   CONFLICT     94     94       E -> D (in Ref. 2; BAB34093).
FT                                {ECO:0000305}.
SQ   SEQUENCE   403 AA;  44444 MW;  7FAAB8E98452FF22 CRC64;
     MNTIFSARIM KRLALTTALC TAFISAAHAD DLNIKTMIPG VPQIDAESYI LIDYNSGKVL
     AEQNADVRRD PASLTKMMTS YVIGQAMKAG KFKETDLVTI GNDAWATGNP VFKGSSLMFL
     KPGMQVPVSQ LIRGINLQSG NDACVAMADF AAGSQDAFVG LMNSYVNALG LKNTHFQTVH
     GLDADGQYSS ARDMALIGQA LIRDVPNEYS IYKEKEFTFN GIRQLNRNGL LWDNSLNVDG
     IKTGHTDKAG YNLVASATEG QMRLISAVMG GRTFKGREAE SKKLLTWGFR FFETVNPLKV
     GKEFASEPVW FGDSDRASLG VDKDVYLTIP RGRMKDLKAS YVLNSSELHA PLQKNQVVGT
     INFQLDGKTI EQRPLVVLQE IPEGNFFGKI IDYIKLMFHH WFG
//

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