AMPH_ECOLI
ID AMPH_ECOLI Reviewed; 385 AA.
AC P0AD70; P46127; P75701; Q2MC49;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 111.
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 AmpH;
DE Flags: Precursor;
GN Name=ampH; Synonyms=yaiH; OrderedLocusNames=b0376, JW5052;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-78.
RC STRAIN=K12;
RX PubMed=1840583; DOI=10.1128/jb.173.12.3924-3929.1991;
RA del Castillo I., Gonzalez-Pastor J.E., San Millan J.L., Moreno F.;
RT "Nucleotide sequence of the Escherichia coli regulatory gene mprA and
RT construction and characterization of mprA-deficient mutants.";
RL J. Bacteriol. 173:3924-3929(1991).
RN [5]
RP IDENTIFICATION.
RX PubMed=7567469; DOI=10.1093/nar/23.17.3554;
RA Borodovsky M., McIninch J., Koonin E.V., Rudd K.E., Medigue C., Danchin A.;
RT "Detection of new genes in a bacterial genome using Markov models for three
RT gene classes.";
RL Nucleic Acids Res. 23:3554-3562(1995).
RN [6]
RP DISRUPTION PHENOTYPE, AND NOMENCLATURE.
RX PubMed=9324260; DOI=10.1128/jb.179.19.6112-6121.1997;
RA Henderson T.A., Young K.D., Denome S.A., Elf P.K.;
RT "AmpC and AmpH, proteins related to the class C beta-lactamases, bind
RT penicillin and contribute to the normal morphology of Escherichia coli.";
RL J. Bacteriol. 179:6112-6121(1997).
RN [7]
RP PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION AS A CARBOXYPEPTIDASE AND
RP ENDOPEPTIDASE, MASS SPECTROMETRY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBSTRATE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=22001512; DOI=10.1128/jb.05764-11;
RA Gonzalez-Leiza S.M., de Pedro M.A., Ayala J.A.;
RT "AmpH, a bifunctional DD-endopeptidase and DD-carboxypeptidase of
RT Escherichia coli.";
RL J. Bacteriol. 193:6887-6894(2011).
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). Also displays a low beta-lactamase activity.
CC {ECO:0000269|PubMed:22001512}.
CC -!- ACTIVITY REGULATION: Inhibited by cefmetazole.
CC {ECO:0000269|PubMed:22001512}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=102 uM for D45 (at 37 degrees Celsius and pH 7.3)
CC {ECO:0000269|PubMed:22001512};
CC KM=134 uM for D44 (at 37 degrees Celsius and pH 7.3)
CC {ECO:0000269|PubMed:22001512};
CC KM=225 uM for M5 (at 37 degrees Celsius and pH 7.5)
CC {ECO:0000269|PubMed:22001512};
CC Vmax=4.98 nmol/min/ug enzyme with M5 as substrate (at 37 degrees
CC Celsius and pH 7.5) {ECO:0000269|PubMed:22001512};
CC Vmax=162 nmol/min/ug enzyme with D44 as substrate (at 37 degrees
CC Celsius and pH 7.3) {ECO:0000269|PubMed:22001512};
CC Vmax=174 nmol/min/ug enzyme with D45 as substrate (at 37 degrees
CC Celsius and pH 7.3) {ECO:0000269|PubMed:22001512};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:22001512}.
CC -!- MASS SPECTROMETRY: Mass=41860; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:22001512};
CC -!- DISRUPTION PHENOTYPE: Disruption is viable and exhibits no overt growth
CC defects, but produces morphologically aberrant cells, particularly in
CC cell filaments induced by aztreonam. {ECO:0000269|PubMed:9324260}.
CC -!- SIMILARITY: Belongs to the beta-lactamase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB18099.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U73857; AAB18099.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC73479.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76157.1; -; Genomic_DNA.
DR EMBL; X54153; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; H64765; H64765.
DR RefSeq; NP_414910.1; NC_000913.3.
DR RefSeq; WP_000830741.1; NZ_SSZK01000009.1.
DR AlphaFoldDB; P0AD70; -.
DR SMR; P0AD70; -.
DR BioGRID; 4259482; 246.
DR BioGRID; 851243; 1.
DR DIP; DIP-47910N; -.
DR IntAct; P0AD70; 1.
DR STRING; 511145.b0376; -.
DR MEROPS; S12.012; -.
DR jPOST; P0AD70; -.
DR PaxDb; P0AD70; -.
DR PRIDE; P0AD70; -.
DR EnsemblBacteria; AAC73479; AAC73479; b0376.
DR EnsemblBacteria; BAE76157; BAE76157; BAE76157.
DR GeneID; 66671326; -.
DR GeneID; 946904; -.
DR KEGG; ecj:JW5052; -.
DR KEGG; eco:b0376; -.
DR PATRIC; fig|1411691.4.peg.1903; -.
DR EchoBASE; EB2708; -.
DR eggNOG; COG1680; Bacteria.
DR HOGENOM; CLU_020027_7_1_6; -.
DR InParanoid; P0AD70; -.
DR OMA; CEKDYFA; -.
DR PhylomeDB; P0AD70; -.
DR BioCyc; EcoCyc:EG12867-MON; -.
DR BioCyc; MetaCyc:EG12867-MON; -.
DR PRO; PR:P0AD70; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004180; F:carboxypeptidase activity; IDA:UniProtKB.
DR GO; GO:0004175; F:endopeptidase activity; IDA:UniProtKB.
DR GO; GO:0008658; F:penicillin binding; IDA:EcoCyc.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009253; P:peptidoglycan catabolic process; IMP:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0008360; P:regulation of cell shape; IMP: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 1: Evidence at protein level;
KW Carboxypeptidase; Cell inner membrane; Cell membrane; Cell shape;
KW Cell wall biogenesis/degradation; Direct protein sequencing; Hydrolase;
KW Membrane; Protease; Reference proteome; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:22001512"
FT CHAIN 22..385
FT /note="D-alanyl-D-alanine-carboxypeptidase/endopeptidase
FT AmpH"
FT /id="PRO_0000195474"
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
