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MPAA_ECOLI
ID   MPAA_ECOLI              Reviewed;         242 AA.
AC   P0ACV6; P51983; P77675;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   24-NOV-2009, sequence version 2.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Murein peptide amidase A {ECO:0000255|HAMAP-Rule:MF_02211, ECO:0000303|PubMed:12511517};
DE            EC=3.4.17.- {ECO:0000255|HAMAP-Rule:MF_02211, ECO:0000269|PubMed:12511517, ECO:0000269|PubMed:22970852};
DE   AltName: Full=Gamma-D-Glu-Dap amidase {ECO:0000255|HAMAP-Rule:MF_02211, ECO:0000303|PubMed:12511517};
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:12511517};
GN   Synonyms=ycjI; OrderedLocusNames=b1326, JW1319;
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 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA   Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA   Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA   Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA   Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA   Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA   Wada C., Yamamoto Y., Horiuchi T.;
RT   "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT   the 28.0-40.1 min region on the linkage map.";
RL   DNA Res. 3:363-377(1996).
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 201-242.
RC   STRAIN=K12;
RX   PubMed=7499381; DOI=10.1074/jbc.270.48.28635;
RA   Cha M.-K., Kim H.-K., Kim I.-H.;
RT   "Thioredoxin-linked 'thiol peroxidase' from periplasmic space of
RT   Escherichia coli.";
RL   J. Biol. Chem. 270:28635-28641(1995).
RN   [5]
RP   IDENTIFICATION.
RA   Rudd K.E.;
RL   Unpublished observations (MAR-1996).
RN   [6]
RP   FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX   PubMed=12511517; DOI=10.1128/jb.185.2.679-682.2003;
RA   Uehara T., Park J.T.;
RT   "Identification of MpaA, an amidase in Escherichia coli that hydrolyzes the
RT   gamma-D-glutamyl-meso-diaminopimelate bond in murein peptides.";
RL   J. Bacteriol. 185:679-682(2003).
RN   [7]
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION,
RP   BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND SUBUNIT.
RC   STRAIN=K12 / MG1655 / ATCC 47076;
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 (PubMed:12511517, PubMed:22970852). Has weak activity with L-Ala-
CC       gamma-D-Glu-L-Lys, MurNAc-tripeptide and gamma-D-Glu-meso-Dap
CC       (PubMed:22970852). Cannot hydrolyze murein tetrapeptide
CC       (PubMed:22970852). {ECO:0000269|PubMed:12511517,
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:12511517,
CC         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   -!- ACTIVITY REGULATION: Inhibited by EDTA. {ECO:0000269|PubMed:22970852}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.41 mM for L-alanyl-gamma-D-glutamyl-meso-diaminopimelic acid
CC         {ECO:0000269|PubMed:22970852};
CC         Note=kcat is 38.3 sec(-1). {ECO:0000269|PubMed:22970852};
CC       pH dependence:
CC         Optimum pH is 8.0. {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       ECO:0000305|PubMed:12511517}.
CC   -!- SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000255|HAMAP-
CC       Rule:MF_02211, ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA14908.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; U00096; AAC74408.2; -; Genomic_DNA.
DR   EMBL; AP009048; BAA14908.1; ALT_INIT; Genomic_DNA.
DR   EMBL; U33213; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; A64882; A64882.
DR   RefSeq; NP_415842.2; NC_000913.3.
DR   RefSeq; WP_000219122.1; NZ_LN832404.1.
DR   AlphaFoldDB; P0ACV6; -.
DR   SMR; P0ACV6; -.
DR   BioGRID; 4260153; 289.
DR   IntAct; P0ACV6; 4.
DR   STRING; 511145.b1326; -.
DR   MEROPS; M14.034; -.
DR   jPOST; P0ACV6; -.
DR   PaxDb; P0ACV6; -.
DR   PRIDE; P0ACV6; -.
DR   EnsemblBacteria; AAC74408; AAC74408; b1326.
DR   EnsemblBacteria; BAA14908; BAA14908; BAA14908.
DR   GeneID; 945969; -.
DR   KEGG; ecj:JW1319; -.
DR   KEGG; eco:b1326; -.
DR   PATRIC; fig|1411691.4.peg.952; -.
DR   EchoBASE; EB3665; -.
DR   eggNOG; COG2866; Bacteria.
DR   HOGENOM; CLU_102905_0_0_6; -.
DR   PhylomeDB; P0ACV6; -.
DR   BioCyc; EcoCyc:G6662-MON; -.
DR   BioCyc; MetaCyc:G6662-MON; -.
DR   UniPathway; UPA00549; -.
DR   PRO; PR:P0ACV6; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004040; F:amidase activity; IGI:EcoliWiki.
DR   GO; GO:0061473; F:murein tripeptide carboxypeptidase activity; IDA:EcoCyc.
DR   GO; GO:0008270; F:zinc ion binding; IDA:EcoCyc.
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:0009050; P:glycopeptide catabolic process; IMP:EcoCyc.
DR   GO; GO:0009253; P:peptidoglycan catabolic process; IMP:EcoCyc.
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   Carboxypeptidase; Cell wall biogenesis/degradation; Cytoplasm; Hydrolase;
KW   Metal-binding; Metalloprotease; Protease; Reference proteome; Zinc.
FT   CHAIN           1..242
FT                   /note="Murein peptide amidase A"
FT                   /id="PRO_0000168894"
FT   BINDING         49
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:A7N805, ECO:0000255|HAMAP-
FT                   Rule:MF_02211"
FT   BINDING         52
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:A7N805, ECO:0000255|HAMAP-
FT                   Rule:MF_02211"
FT   BINDING         157
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:A7N805, ECO:0000255|HAMAP-
FT                   Rule:MF_02211"
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
 
 
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