MPAA_ECO57
ID MPAA_ECO57 Reviewed; 242 AA.
AC P0ACV7; P51983; P77675;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 2.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Murein peptide amidase A {ECO:0000255|HAMAP-Rule:MF_02211};
DE EC=3.4.17.- {ECO:0000255|HAMAP-Rule:MF_02211};
DE AltName: Full=Gamma-D-Glu-Dap amidase {ECO:0000255|HAMAP-Rule:MF_02211};
DE AltName: Full=Zinc metallocarboxypeptidase MpaA {ECO:0000255|HAMAP-Rule:MF_02211};
GN Name=mpaA {ECO:0000255|HAMAP-Rule:MF_02211};
GN OrderedLocusNames=Z2448, ECs1905;
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).
RN [3] {ECO:0007744|PDB:5HXD}
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 1-237.
RX PubMed=27894248; DOI=10.2174/0929866523666161128153128;
RA Ma Y., Bai G., Cui Y., Zhao J., Yuan Z., Liu X.;
RT "Crystal structure of murein-tripeptide amidase MpaA from Escherichia coli
RT O157 at 2.6 Aa resolution.";
RL Protein Pept. Lett. 24:181-187(2017).
CC -!- FUNCTION: Involved in muropeptide degradation. Catalyzes the hydrolysis
CC of the gamma-D-glutamyl-diaminopimelic acid (gamma-D-Glu-Dap) amide
CC bond in the murein tripeptide L-alanyl-gamma-D-glutamyl-meso-
CC diaminopimelic acid, leading to the formation of L-Ala-gamma-D-Glu and
CC Dap. {ECO:0000255|HAMAP-Rule:MF_02211}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-alanyl-gamma-D-glutamyl-meso-diaminoheptanedioate = L-
CC alanyl-D-glutamate + meso-2,6-diaminoheptanedioate;
CC Xref=Rhea:RHEA:28398, ChEBI:CHEBI:15377, ChEBI:CHEBI:57791,
CC ChEBI:CHEBI:61395, ChEBI:CHEBI:61401; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_02211};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02211};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_02211};
CC -!- PATHWAY: Cell wall degradation; peptidoglycan degradation.
CC {ECO:0000255|HAMAP-Rule:MF_02211}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_02211}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02211}.
CC -!- SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000255|HAMAP-
CC Rule:MF_02211}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG56476.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB35328.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE005174; AAG56476.1; ALT_INIT; Genomic_DNA.
DR EMBL; BA000007; BAB35328.1; ALT_INIT; Genomic_DNA.
DR PIR; A99867; A99867.
DR PIR; H85751; H85751.
DR RefSeq; NP_309932.2; NC_002695.1.
DR RefSeq; WP_000219122.1; NZ_SWKA01000005.1.
DR PDB; 5HXD; X-ray; 2.60 A; A/B=1-237.
DR PDBsum; 5HXD; -.
DR AlphaFoldDB; P0ACV7; -.
DR SMR; P0ACV7; -.
DR STRING; 155864.EDL933_2353; -.
DR MEROPS; M14.034; -.
DR EnsemblBacteria; AAG56476; AAG56476; Z2448.
DR EnsemblBacteria; BAB35328; BAB35328; ECs_1905.
DR GeneID; 912455; -.
DR KEGG; ece:Z2448; -.
DR KEGG; ecs:ECs_1905; -.
DR PATRIC; fig|386585.9.peg.2010; -.
DR eggNOG; COG2866; Bacteria.
DR HOGENOM; CLU_102905_0_0_6; -.
DR OMA; ACIEDPH; -.
DR UniPathway; UPA00549; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004040; F:amidase activity; IEA:InterPro.
DR GO; GO:0061473; F:murein tripeptide carboxypeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016998; P:cell wall macromolecule catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009253; P:peptidoglycan catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR HAMAP; MF_02211; MpaA_carboxypeptidase; 1.
DR InterPro; IPR043691; MpaA.
DR InterPro; IPR000834; Peptidase_M14.
DR Pfam; PF00246; Peptidase_M14; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carboxypeptidase; Cell wall biogenesis/degradation;
KW Cytoplasm; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW Reference proteome; Zinc.
FT CHAIN 1..242
FT /note="Murein peptide amidase A"
FT /id="PRO_0000168895"
FT BINDING 49
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02211"
FT BINDING 52
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02211"
FT BINDING 157
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02211"
FT HELIX 7..9
FT /evidence="ECO:0007829|PDB:5HXD"
FT STRAND 18..22
FT /evidence="ECO:0007829|PDB:5HXD"
FT STRAND 28..32
FT /evidence="ECO:0007829|PDB:5HXD"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:5HXD"
FT HELIX 53..65
FT /evidence="ECO:0007829|PDB:5HXD"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:5HXD"
FT STRAND 73..77
FT /evidence="ECO:0007829|PDB:5HXD"
FT HELIX 81..85
FT /evidence="ECO:0007829|PDB:5HXD"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:5HXD"
FT STRAND 109..113
FT /evidence="ECO:0007829|PDB:5HXD"
FT STRAND 124..127
FT /evidence="ECO:0007829|PDB:5HXD"
FT HELIX 136..148
FT /evidence="ECO:0007829|PDB:5HXD"
FT STRAND 153..160
FT /evidence="ECO:0007829|PDB:5HXD"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:5HXD"
FT HELIX 170..178
FT /evidence="ECO:0007829|PDB:5HXD"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:5HXD"
FT HELIX 195..201
FT /evidence="ECO:0007829|PDB:5HXD"
FT STRAND 206..210
FT /evidence="ECO:0007829|PDB:5HXD"
FT HELIX 216..222
FT /evidence="ECO:0007829|PDB:5HXD"
FT HELIX 224..230
FT /evidence="ECO:0007829|PDB:5HXD"
SQ SEQUENCE 242 AA; 26558 MW; 6AC2984086E0A6C0 CRC64;
MTVTRPRAER GAFPPGTEHY GRSLLGAPLI WFPAPAASRE SGLILAGTHG DENSSVVTLS
CALRTLTPSL RRHHVVLCVN PDGCQLGLRA NANGVDLNRN FPAANWKEGE TVYRWNSAAE
ERDVVLLTGD KPGSEPETQA LCQLIHRIQP AWVVSFHDPL ACIEDPRHSE LGEWLAQAFE
LPLVTSVGYE TPGSFGSWCA DLNLHCITAE FPPISSDEAS EKYLFAMANL LRWHPKDAIR
PS
