(data stored in ACNUC7421 zone)

SWISSPROT: AMPH_ECO57

ID   AMPH_ECO57              Reviewed;         385 AA.
AC   P0AD71; P46127; P75701;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   05-JUL-2017, entry version 71.
DE   RecName: Full=D-alanyl-D-alanine-carboxypeptidase/endopeptidase AmpH;
DE            EC=3.4.-.-;
DE   AltName: Full=DD-alanine-endopeptidase;
DE   AltName: Full=DD-carboxypeptidase;
DE   AltName: Full=Penicillin-binding protein;
DE            Short=PBP;
DE   Flags: Precursor;
GN   Name=ampH; OrderedLocusNames=Z0472, ECs0426;
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: Hydrolyzes the cross-linked dimers tetrapentapeptide
CC       (D45) and tetratetrapeptide (D44). Removes the terminal D-alanine
CC       from muropeptides and disaccharide pentapeptide M5 with a C-
CC       terminal D-Ala-D-Ala dipeptide. Associated with recycling and
CC       remodeling of peptidoglycan (PG) (By similarity). {ECO:0000250}.
CC   -!- ENZYME REGULATION: Inhibited by cefmetazole.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the beta-lactamase family. {ECO:0000305}.
DR   EMBL; AE005174; AAG54722.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB33849.1; -; Genomic_DNA.
DR   PIR; B90682; B90682.
DR   PIR; F85532; F85532.
DR   RefSeq; NP_308453.1; NC_002695.1.
DR   RefSeq; WP_000830741.1; NZ_MWVM01000022.1.
DR   ProteinModelPortal; P0AD71; -.
DR   SMR; P0AD71; -.
DR   STRING; 155864.Z0472; -.
DR   EnsemblBacteria; AAG54722; AAG54722; Z0472.
DR   EnsemblBacteria; BAB33849; BAB33849; BAB33849.
DR   GeneID; 914528; -.
DR   KEGG; ece:Z0472; -.
DR   KEGG; ecs:ECs0426; -.
DR   PATRIC; fig|386585.9.peg.521; -.
DR   eggNOG; ENOG4107R6D; Bacteria.
DR   eggNOG; COG1680; LUCA.
DR   HOGENOM; HOG000117477; -.
DR   KO; K18988; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004180; F:carboxypeptidase activity; ISS:UniProtKB.
DR   GO; GO:0004175; F:endopeptidase activity; ISS:UniProtKB.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009253; P:peptidoglycan catabolic process; ISS:UniProtKB.
DR   GO; GO:0008360; P:regulation of cell shape; ISS:UniProtKB.
DR   InterPro; IPR001466; Beta-lactam-related.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   Pfam; PF00144; Beta-lactamase; 1.
DR   SUPFAM; SSF56601; SSF56601; 1.
PE   3: Inferred from homology;
DR   PRODOM; P0AD71.
DR   SWISS-2DPAGE; P0AD71.
KW   Carboxypeptidase; Cell inner membrane; Cell membrane; Cell shape;
KW   Cell wall biogenesis/degradation; Complete proteome; Hydrolase;
KW   Membrane; Protease; Signal.
FT   SIGNAL        1     21       {ECO:0000255}.
FT   CHAIN        22    385       D-alanyl-D-alanine-
FT                                carboxypeptidase/endopeptidase AmpH.
FT                                /FTId=PRO_0000195475.
SQ   SEQUENCE   385 AA;  41849 MW;  2D249CBA78022947 CRC64;
     MKRSLLFSAV LCAASLTSVH AAQPITEPEF ASDIVDRYAD HIFYGSGATG MALVVIDGNQ
     RVFRSYGETR PGNNVRPQLD SVVRIASLTK LMTSEMLVKL LDQGTVKLND PLSKYAPPGA
     RVPTYNGTPI TLVNLATHTS ALPREQPGGA AHRPVFVWPT REQRWKYLST AKLKAAPGSQ
     AAYSNLAFDL LADALANASG KPYTQLFEEQ ITRPLGMKDT TYTPSPDQCR RLMVAERGAS
     PCNNTLAAIG SGGVYSTPGD MMRWMQQYLS SDFYQRSNQA DRMQTLIYQR AQFTKVIGMD
     VPGKADALGL GWVYMAPKEG RPGIIQKTGG GGGFITYMAM IPQKNIGAFV VVTRSPLTRF
     KNMSDGINDL VTELSGNKPL VIPAS
//

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