DACC_ECOLI
ID DACC_ECOLI Reviewed; 400 AA.
AC P08506; P77287;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=D-alanyl-D-alanine carboxypeptidase DacC;
DE Short=DD-carboxypeptidase;
DE Short=DD-peptidase;
DE EC=3.4.16.4;
DE AltName: Full=Penicillin-binding protein 6;
DE Short=PBP-6;
DE Flags: Precursor;
GN Name=dacC; OrderedLocusNames=b0839, JW0823;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=3279397; DOI=10.1093/nar/16.4.1617;
RA Broome-Smith J.K., Ioannidis I., Edelman A., Spratt B.G.;
RT "Nucleotide sequences of the penicillin-binding protein 5 and 6 genes of
RT Escherichia coli.";
RL Nucleic Acids Res. 16:1617-1617(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP PROTEIN SEQUENCE OF 28-52.
RX PubMed=7042389; DOI=10.1016/0014-5793(82)80840-5;
RA Waxman D.J., Amanuma H., Strominger J.L.;
RT "Amino acid sequence homologies between Escherichia coli penicillin-binding
RT protein 5 and class A beta-lactamases.";
RL FEBS Lett. 139:159-163(1982).
RN [6]
RP SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=3330754; DOI=10.1111/j.1365-2958.1987.tb00522.x;
RA Jackson M.E., Pratt J.M.;
RT "An 18 amino acid amphiphilic helix forms the membrane-anchoring domain of
RT the Escherichia coli penicillin-binding protein 5.";
RL Mol. Microbiol. 1:23-28(1987).
CC -!- FUNCTION: Removes C-terminal D-alanyl residues from sugar-peptide cell
CC wall precursors.
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 -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:3330754};
CC Peripheral membrane protein {ECO:0000269|PubMed:3330754}; Periplasmic
CC side {ECO:0000269|PubMed:3330754}. Note=N-terminus lies in the
CC periplasmic space, targeted there by the C-terminal amphiphilic helix
CC (PMID:3330754).
CC -!- DOMAIN: The C-terminus forms an amphiphilic helix that targets the
CC protein to the periplasmic side of the inner cell membrane.
CC {ECO:0000269|PubMed:3330754}.
CC -!- SIMILARITY: Belongs to the peptidase S11 family. {ECO:0000305}.
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DR EMBL; X06480; CAA29775.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73926.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35542.1; -; Genomic_DNA.
DR PIR; G64821; G64821.
DR RefSeq; NP_415360.1; NC_000913.3.
DR RefSeq; WP_001300708.1; NZ_SSZK01000002.1.
DR PDB; 3IT9; X-ray; 2.10 A; A/B/C/D=28-378.
DR PDB; 3ITA; X-ray; 1.80 A; A/B/C/D=28-378.
DR PDB; 3ITB; X-ray; 1.80 A; A/B/C/D=28-378.
DR PDBsum; 3IT9; -.
DR PDBsum; 3ITA; -.
DR PDBsum; 3ITB; -.
DR AlphaFoldDB; P08506; -.
DR SMR; P08506; -.
DR BioGRID; 4262825; 228.
DR IntAct; P08506; 2.
DR MINT; P08506; -.
DR STRING; 511145.b0839; -.
DR ChEMBL; CHEMBL2354204; -.
DR DrugBank; DB01602; Bacampicillin.
DR DrugBank; DB00578; Carbenicillin.
DR DrugBank; DB09319; Carindacillin.
DR DrugBank; DB00274; Cefmetazole.
DR DrugBank; DB01329; Cefoperazone.
DR DrugBank; DB01331; Cefoxitin.
DR DrugBank; DB00430; Cefpiramide.
DR DrugBank; DB01332; Ceftizoxime.
DR DrugBank; DB09050; Ceftolozane.
DR DrugBank; DB01000; Cyclacillin.
DR DrugBank; DB00303; Ertapenem.
DR DrugCentral; P08506; -.
DR MEROPS; S11.003; -.
DR jPOST; P08506; -.
DR PaxDb; P08506; -.
DR PRIDE; P08506; -.
DR EnsemblBacteria; AAC73926; AAC73926; b0839.
DR EnsemblBacteria; BAA35542; BAA35542; BAA35542.
DR GeneID; 945455; -.
DR KEGG; ecj:JW0823; -.
DR KEGG; eco:b0839; -.
DR PATRIC; fig|1411691.4.peg.1439; -.
DR EchoBASE; EB0199; -.
DR eggNOG; COG1686; Bacteria.
DR HOGENOM; CLU_027070_8_1_6; -.
DR InParanoid; P08506; -.
DR OMA; TNEAKYC; -.
DR PhylomeDB; P08506; -.
DR BioCyc; EcoCyc:EG10203-MON; -.
DR BioCyc; MetaCyc:EG10203-MON; -.
DR UniPathway; UPA00219; -.
DR EvolutionaryTrace; P08506; -.
DR PRO; PR:P08506; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoliWiki.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0004180; F:carboxypeptidase activity; IDA:EcoCyc.
DR GO; GO:0008658; F:penicillin binding; IDA:EcoCyc.
DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; ISM:EcoCyc.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IDA:EcoCyc.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IMP:EcoCyc.
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_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 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 1: Evidence at protein level;
KW 3D-structure; Carboxypeptidase; Cell inner membrane; Cell membrane;
KW Cell shape; Cell wall biogenesis/degradation; Direct protein sequencing;
KW Hydrolase; Membrane; Peptidoglycan synthesis; Protease; Reference proteome;
KW Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000269|PubMed:7042389"
FT CHAIN 28..400
FT /note="D-alanyl-D-alanine carboxypeptidase DacC"
FT /id="PRO_0000027233"
FT REGION 383..400
FT /note="Required for inner membrane binding"
FT ACT_SITE 66
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 69
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 132
FT /evidence="ECO:0000250"
FT BINDING 235
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CONFLICT 231
FT /note="V -> E (in Ref. 1; CAA29775)"
FT /evidence="ECO:0000305"
FT STRAND 39..46
FT /evidence="ECO:0007829|PDB:3ITA"
FT TURN 47..49
FT /evidence="ECO:0007829|PDB:3ITA"
FT STRAND 52..57
FT /evidence="ECO:0007829|PDB:3ITA"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:3ITA"
FT HELIX 68..81
FT /evidence="ECO:0007829|PDB:3ITA"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:3ITA"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:3ITA"
FT TURN 99..101
FT /evidence="ECO:0007829|PDB:3ITA"
FT HELIX 103..105
FT /evidence="ECO:0007829|PDB:3ITA"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:3ITA"
FT HELIX 121..129
FT /evidence="ECO:0007829|PDB:3ITA"
FT HELIX 134..145
FT /evidence="ECO:0007829|PDB:3ITA"
FT HELIX 148..161
FT /evidence="ECO:0007829|PDB:3ITA"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:3ITB"
FT HELIX 184..197
FT /evidence="ECO:0007829|PDB:3ITA"
FT HELIX 199..202
FT /evidence="ECO:0007829|PDB:3ITA"
FT HELIX 203..206
FT /evidence="ECO:0007829|PDB:3ITA"
FT STRAND 209..212
FT /evidence="ECO:0007829|PDB:3ITA"
FT STRAND 215..218
FT /evidence="ECO:0007829|PDB:3ITA"
FT HELIX 222..225
FT /evidence="ECO:0007829|PDB:3ITA"
FT STRAND 230..239
FT /evidence="ECO:0007829|PDB:3ITA"
FT TURN 240..242
FT /evidence="ECO:0007829|PDB:3ITA"
FT STRAND 243..252
FT /evidence="ECO:0007829|PDB:3ITA"
FT STRAND 255..266
FT /evidence="ECO:0007829|PDB:3ITA"
FT HELIX 267..284
FT /evidence="ECO:0007829|PDB:3ITA"
FT STRAND 285..288
FT /evidence="ECO:0007829|PDB:3ITA"
FT STRAND 297..313
FT /evidence="ECO:0007829|PDB:3ITA"
FT HELIX 315..317
FT /evidence="ECO:0007829|PDB:3ITA"
FT STRAND 320..323
FT /evidence="ECO:0007829|PDB:3ITA"
FT HELIX 327..329
FT /evidence="ECO:0007829|PDB:3ITA"
FT STRAND 330..343
FT /evidence="ECO:0007829|PDB:3ITA"
FT STRAND 350..358
FT /evidence="ECO:0007829|PDB:3ITA"
FT STRAND 361..370
FT /evidence="ECO:0007829|PDB:3ITA"
SQ SEQUENCE 400 AA; 43609 MW; 4D7F3BDCEA64C775 CRC64;
MTQYSSLLRG LAAGSAFLFL FAPTAFAAEQ TVEAPSVDAR AWILMDYASG KVLAEGNADE
KLDPASLTKI MTSYVVGQAL KADKIKLTDM VTVGKDAWAT GNPALRGSSV MFLKPGDQVS
VADLNKGVII QSGNDACIAL ADYVAGSQES FIGLMNGYAK KLGLTNTTFQ TVHGLDAPGQ
FSTARDMALL GKALIHDVPE EYAIHKEKEF TFNKIRQPNR NRLLWSSNLN VDGMKTGTTA
GAGYNLVASA TQGDMRLISV VLGAKTDRIR FNESEKLLTW GFRFFETVTP IKPDATFVTQ
RVWFGDKSEV NLGAGEAGSV TIPRGQLKNL KASYTLTEPQ LTAPLKKGQV VGTIDFQLNG
KSIEQRPLIV MENVEEGGFF GRVWDFVMMK FHQWFGSWFS
