ID   D3GX95_ECO44            Unreviewed;       403 AA.
AC   D3GX95;
DT   23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   23-MAR-2010, sequence version 1.
DT   01-OCT-2014, entry version 30.
DE   SubName: Full=Penicillin-binding protein 5 (D-alanyl-D-alanine carboxypeptidase) {ECO:0000313|EMBL:CBG33493.1};
DE            EC=3.4.16.4 {ECO:0000313|EMBL:CBG33493.1};
GN   Name=dacA {ECO:0000313|EMBL:CBG33493.1};
GN   OrderedLocusNames=EC042_0667 {ECO:0000313|EMBL:CBG33493.1};
OS   Escherichia coli O44:H18 (strain 042 / EAEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=216592 {ECO:0000313|EMBL:CBG33493.1, ECO:0000313|Proteomes:UP000001407};
RN   [1] {ECO:0000313|EMBL:CBG33493.1, ECO:0000313|Proteomes:UP000001407}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=042 / EAEC {ECO:0000313|Proteomes:UP000001407};
RX   PubMed=20098708; DOI=10.1371/journal.pone.0008801;
RA   Chaudhuri R.R., Sebaihia M., Hobman J.L., Webber M.A., Leyton D.L.,
RA   Goldberg M.D., Cunningham A.F., Scott-Tucker A., Ferguson P.R.,
RA   Thomas C.M., Frankel G., Tang C.M., Dudley E.G., Roberts I.S.,
RA   Rasko D.A., Pallen M.J., Parkhill J., Nataro J.P., Thomson N.R.,
RA   Henderson I.R.;
RT   "Complete genome sequence and comparative metabolic profiling of the
RT   prototypical enteroaggregative Escherichia coli strain 042.";
RL   PLoS ONE 5:E8801-E8801(2010).
CC   -!- SIMILARITY: Belongs to the peptidase S11 family.
CC       {ECO:0000256|RuleBase:RU004016}.
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DR   EMBL; FN554766; CBG33493.1; -; Genomic_DNA.
DR   RefSeq; YP_006094988.1; NC_017626.1.
DR   ProteinModelPortal; D3GX95; -.
DR   SMR; D3GX95; 32-386.
DR   GeneID; 12888190; -.
DR   KEGG; elo:EC042_0667; -.
DR   PATRIC; 36682660; VBIEscCol52250_0695.
DR   KO; K07258; -.
DR   OMA; YVIGQAV; -.
DR   BioCyc; ECOL216592:GCV7-666-MONOMER; -.
DR   GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
DR   Gene3D; 2.60.410.10; -; 1.
DR   Gene3D; 3.40.710.10; -; 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;
KW   Carboxypeptidase {ECO:0000313|EMBL:CBG33493.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001407};
KW   Hydrolase {ECO:0000313|EMBL:CBG33493.1}; Protease.
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
//