ID A0A427KBN4_9GAMM Unreviewed; 235 AA.
AC A0A427KBN4;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE RecName: Full=Murein peptide amidase A {ECO:0000256|HAMAP-Rule:MF_02211};
DE EC=3.4.17.- {ECO:0000256|HAMAP-Rule:MF_02211};
DE AltName: Full=Gamma-D-Glu-Dap amidase {ECO:0000256|HAMAP-Rule:MF_02211};
DE AltName: Full=Zinc metallocarboxypeptidase MpaA {ECO:0000256|HAMAP-Rule:MF_02211};
GN Name=mpaA {ECO:0000256|HAMAP-Rule:MF_02211,
GN ECO:0000313|EMBL:RRZ95645.1};
GN ORFNames=EGK14_03560 {ECO:0000313|EMBL:RRZ95645.1};
OS Erwinia sp. 198.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=2022746 {ECO:0000313|EMBL:RRZ95645.1, ECO:0000313|Proteomes:UP000273595};
RN [1] {ECO:0000313|EMBL:RRZ95645.1, ECO:0000313|Proteomes:UP000273595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=198 {ECO:0000313|EMBL:RRZ95645.1,
RC ECO:0000313|Proteomes:UP000273595};
RA D'Souza A.W., Potter R.F., Wallace M., Shupe A., Patel S., Sun S., Gul D.,
RA Kwon J.H., Andleeb S., Burnham C.-A.D., Dantas G.;
RT "Transmission dynamics of multidrug resistant bacteria on intensive care
RT unit surfaces.";
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|HAMAP-
CC Rule:MF_02211};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_02211};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_02211};
CC -!- PATHWAY: Cell wall degradation; peptidoglycan degradation.
CC {ECO:0000256|HAMAP-Rule:MF_02211}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_02211}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02211}.
CC -!- SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000256|HAMAP-
CC Rule:MF_02211}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RRZ95645.1}.
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DR EMBL; RHUM01000002; RRZ95645.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A427KBN4; -.
DR OrthoDB; 9779324at2; -.
DR UniPathway; UPA00549; -.
DR Proteomes; UP000273595; Unassembled WGS sequence.
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 CDD; cd06904; M14_MpaA-like; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR HAMAP; MF_02211; MpaA_carboxypeptidase; 1.
DR InterPro; IPR043691; MpaA.
DR InterPro; IPR000834; Peptidase_M14.
DR Pfam; PF00246; Peptidase_M14; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000256|HAMAP-Rule:MF_02211};
KW Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_02211};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02211};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_02211};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_02211};
KW Metalloprotease {ECO:0000256|HAMAP-Rule:MF_02211};
KW Protease {ECO:0000256|HAMAP-Rule:MF_02211};
KW Reference proteome {ECO:0000313|Proteomes:UP000273595};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_02211}.
FT DOMAIN 43..157
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|Pfam:PF00246"
FT BINDING 49
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02211"
FT BINDING 52
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02211"
FT BINDING 157
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02211"
SQ SEQUENCE 235 AA; 25392 MW; 23698CC543FEF863 CRC64;
MPQNHPRPRR GKLEADRLRY GSSVLGAPLL WFPAPNADDA SGLILAGTHG DETAAVITLS
CAMRTLHERH RRHHVVLAVN PDGCQLGLRA NARGVDLNRN FPAANWQPGE TVYRWNSAAN
ERDVTLSTGE SAGSEPETQA LCALIHQLKP AWVVSFHEPL ACIEDPLDSE AGRWLAEKMG
LPLVTSVGYA TPGSFGSWCA DLGLPVITAE LPPVSADEAS EKYLTALVEL LSKTF
//
