MPAA_VIBC1
ID MPAA_VIBC1 Reviewed; 248 AA.
AC A7N805;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Murein peptide amidase A {ECO:0000255|HAMAP-Rule:MF_02211, ECO:0000303|PubMed:22970852};
DE EC=3.4.17.- {ECO:0000255|HAMAP-Rule:MF_02211, ECO:0000269|PubMed:22970852};
DE AltName: Full=Gamma-D-Glu-Dap amidase {ECO:0000255|HAMAP-Rule:MF_02211, ECO:0000305};
DE AltName: Full=Zinc metallocarboxypeptidase MpaA {ECO:0000255|HAMAP-Rule:MF_02211, ECO:0000303|PubMed:22970852};
GN Name=mpaA {ECO:0000255|HAMAP-Rule:MF_02211, ECO:0000303|PubMed:22970852};
GN OrderedLocusNames=VIBHAR_07057 {ECO:0000312|EMBL:ABU74930.1};
OS Vibrio campbellii (strain ATCC BAA-1116).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=2902295;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1116 / BB120;
RG The Vibrio harveyi Genome Sequencing Project;
RA Bassler B., Clifton S.W., Fulton L., Delehaunty K., Fronick C.,
RA Harrison M., Markivic C., Fulton R., Tin-Wollam A.-M., Shah N., Pepin K.,
RA Nash W., Thiruvilangam P., Bhonagiri V., Waters C., Tu K.C., Irgon J.,
RA Wilson R.K.;
RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0007744|PDB:4AXV}
RP X-RAY CRYSTALLOGRAPHY (2.17 ANGSTROMS) OF 14-248 IN COMPLEX WITH ZINC,
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, AND SUBUNIT.
RC STRAIN=ATCC BAA-1116 / BB120;
RX PubMed=22970852; DOI=10.1042/bj20121164;
RA Maqbool A., Herve M., Mengin-Lecreulx D., Wilkinson A.J., Thomas G.H.;
RT "MpaA is a murein-tripeptide-specific zinc carboxypeptidase that functions
RT as part of a catabolic pathway for peptidoglycan-derived peptides in gamma-
RT proteobacteria.";
RL Biochem. J. 448:329-341(2012).
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. Has weak activity with L-Ala-gamma-D-Glu-L-Lys, MurNAc-tripeptide
CC and gamma-D-Glu-meso-Dap. Cannot hydrolyze murein tetrapeptide.
CC {ECO:0000269|PubMed:22970852}.
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, ECO:0000269|PubMed:22970852};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02211,
CC ECO:0000269|PubMed:22970852};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_02211,
CC ECO:0000269|PubMed:22970852};
CC -!- PATHWAY: Cell wall degradation; peptidoglycan degradation.
CC {ECO:0000255|HAMAP-Rule:MF_02211, ECO:0000305|PubMed:22970852}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_02211,
CC ECO:0000269|PubMed:22970852}.
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, ECO:0000305}.
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DR EMBL; CP000790; ABU74930.1; -; Genomic_DNA.
DR PDB; 4AXV; X-ray; 2.17 A; A=14-248.
DR PDBsum; 4AXV; -.
DR AlphaFoldDB; A7N805; -.
DR SMR; A7N805; -.
DR EnsemblBacteria; ABU74930; ABU74930; VIBHAR_07057.
DR KEGG; vha:VIBHAR_07057; -.
DR PATRIC; fig|338187.36.peg.5881; -.
DR OMA; TWAGQER; -.
DR UniPathway; UPA00549; -.
DR Proteomes; UP000008152; Chromosome II.
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; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
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; IDA:UniProtKB.
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; Zinc.
FT CHAIN 1..248
FT /note="Murein peptide amidase A"
FT /id="PRO_0000446867"
FT BINDING 60
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02211,
FT ECO:0000269|PubMed:22970852, ECO:0007744|PDB:4AXV"
FT BINDING 63
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02211,
FT ECO:0000269|PubMed:22970852, ECO:0007744|PDB:4AXV"
FT BINDING 168
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02211,
FT ECO:0000269|PubMed:22970852, ECO:0007744|PDB:4AXV"
FT HELIX 18..20
FT /evidence="ECO:0007829|PDB:4AXV"
FT STRAND 29..33
FT /evidence="ECO:0007829|PDB:4AXV"
FT STRAND 39..43
FT /evidence="ECO:0007829|PDB:4AXV"
FT STRAND 54..57
FT /evidence="ECO:0007829|PDB:4AXV"
FT HELIX 65..76
FT /evidence="ECO:0007829|PDB:4AXV"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:4AXV"
FT STRAND 84..88
FT /evidence="ECO:0007829|PDB:4AXV"
FT HELIX 92..96
FT /evidence="ECO:0007829|PDB:4AXV"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:4AXV"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:4AXV"
FT STRAND 135..138
FT /evidence="ECO:0007829|PDB:4AXV"
FT HELIX 147..159
FT /evidence="ECO:0007829|PDB:4AXV"
FT STRAND 164..168
FT /evidence="ECO:0007829|PDB:4AXV"
FT STRAND 173..175
FT /evidence="ECO:0007829|PDB:4AXV"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:4AXV"
FT HELIX 181..190
FT /evidence="ECO:0007829|PDB:4AXV"
FT STRAND 198..202
FT /evidence="ECO:0007829|PDB:4AXV"
FT HELIX 206..212
FT /evidence="ECO:0007829|PDB:4AXV"
FT STRAND 217..221
FT /evidence="ECO:0007829|PDB:4AXV"
FT HELIX 227..242
FT /evidence="ECO:0007829|PDB:4AXV"
SQ SEQUENCE 248 AA; 27573 MW; 413BB948533F25CA CRC64;
MNRYYSNNQE ITVSLIPRTE RAAFLITPTS YGKSVLGAPL LYFPAQVESN SRGLILAGTH
GDETASIAGL SCALRSLPAE CLKHDVILSM NPDANQLGTR ANANQVDLNR AFPTQNWTEH
GTVYRWSSHT PVRDVKVKTG DKEQLEPEVD ALISLIELRR PKFVVSFHEP LAFVDDPAHS
DLAKWLGKQF NLPIVDDVDY ETPGSFGTWC NERQLPCITV ELPPISADLT IEKHLDAFIA
LLQHDPDL
