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   03-AUG-2022, entry version 90.
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., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   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., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Hydrolyzes the cross-linked dimers tetrapentapeptide (D45)
CC       and tetratetrapeptide (D44). Removes the terminal D-alanine from
CC       muropeptides and disaccharide pentapeptide M5 with a C-terminal D-Ala-
CC       D-Ala dipeptide. Associated with recycling and remodeling of
CC       peptidoglycan (PG) (By similarity). {ECO:0000250}.
CC   -!- ACTIVITY REGULATION: Inhibited by cefmetazole.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the beta-lactamase family. {ECO:0000305}.
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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_SWKA01000005.1.
DR   AlphaFoldDB; P0AD71; -.
DR   SMR; P0AD71; -.
DR   STRING; 155864.EDL933_0433; -.
DR   MEROPS; S12.012; -.
DR   EnsemblBacteria; AAG54722; AAG54722; Z0472.
DR   EnsemblBacteria; BAB33849; BAB33849; ECs_0426.
DR   GeneID; 66671326; -.
DR   GeneID; 914528; -.
DR   KEGG; ece:Z0472; -.
DR   KEGG; ecs:ECs_0426; -.
DR   PATRIC; fig|386585.9.peg.521; -.
DR   eggNOG; COG1680; Bacteria.
DR   HOGENOM; CLU_020027_7_1_6; -.
DR   OMA; CEKDYFA; -.
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:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0008360; P:regulation of cell shape; ISS:UniProtKB.
DR   Gene3D; 3.40.710.10; -; 1.
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;
KW   Carboxypeptidase; Cell inner membrane; Cell membrane; Cell shape;
KW   Cell wall biogenesis/degradation; Hydrolase; Membrane; Protease;
KW   Reference proteome; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..385
FT                   /note="D-alanyl-D-alanine-carboxypeptidase/endopeptidase
FT                   AmpH"
FT                   /id="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