(data stored in ACNUC7421 zone)

SWISSPROT: MRDA_ECO57

ID   MRDA_ECO57              Reviewed;         633 AA.
AC   P0AD67; P08150;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1988, sequence version 1.
DT   05-JUL-2017, entry version 84.
DE   RecName: Full=Peptidoglycan D,D-transpeptidase MrdA {ECO:0000255|HAMAP-Rule:MF_02081};
DE            EC=3.4.16.4 {ECO:0000255|HAMAP-Rule:MF_02081};
DE   AltName: Full=Penicillin-binding protein 2 {ECO:0000255|HAMAP-Rule:MF_02081};
DE            Short=PBP-2 {ECO:0000255|HAMAP-Rule:MF_02081};
GN   Name=mrdA {ECO:0000255|HAMAP-Rule:MF_02081}; Synonyms=pbpA;
GN   OrderedLocusNames=Z0781, ECs0673;
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.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., 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.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Catalyzes cross-linking of the peptidoglycan cell wall.
CC       {ECO:0000255|HAMAP-Rule:MF_02081}.
CC   -!- CATALYTIC ACTIVITY: Preferential cleavage: (Ac)(2)-L-Lys-D-Ala-|-
CC       D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are
CC       N-acyl substituents of D-alanine. {ECO:0000255|HAMAP-
CC       Rule:MF_02081}.
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_02081}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_02081}; Single-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_02081}.
CC   -!- SIMILARITY: Belongs to the transpeptidase family. MrdA subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_02081}.
DR   EMBL; AE005174; AAG54969.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB34096.1; -; Genomic_DNA.
DR   PIR; A90713; A90713.
DR   PIR; E85563; E85563.
DR   RefSeq; NP_308700.1; NC_002695.1.
DR   RefSeq; WP_000776191.1; NZ_MWVM01000011.1.
DR   ProteinModelPortal; P0AD67; -.
DR   STRING; 155864.Z0781; -.
DR   EnsemblBacteria; AAG54969; AAG54969; Z0781.
DR   EnsemblBacteria; BAB34096; BAB34096; BAB34096.
DR   GeneID; 917034; -.
DR   KEGG; ece:Z0781; -.
DR   KEGG; ecs:ECs0673; -.
DR   PATRIC; fig|386585.9.peg.785; -.
DR   eggNOG; ENOG4105CJN; Bacteria.
DR   eggNOG; COG0768; LUCA.
DR   HOGENOM; HOG000266120; -.
DR   KO; K05515; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR   GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   HAMAP; MF_02081; MrdA_transpept; 1.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR005311; PBP_dimer.
DR   InterPro; IPR001460; PCN-bd_Tpept.
DR   InterPro; IPR017790; Penicillin-binding_protein_2.
DR   Pfam; PF03717; PBP_dimer; 1.
DR   Pfam; PF00905; Transpeptidase; 1.
DR   SUPFAM; SSF56519; SSF56519; 1.
DR   SUPFAM; SSF56601; SSF56601; 1.
DR   TIGRFAMs; TIGR03423; pbp2_mrdA; 1.
PE   3: Inferred from homology;
DR   PRODOM; P0AD67.
DR   SWISS-2DPAGE; P0AD67.
KW   Carboxypeptidase; Cell inner membrane; Cell membrane; Cell shape;
KW   Cell wall biogenesis/degradation; Complete proteome; Hydrolase;
KW   Membrane; Peptidoglycan synthesis; Protease; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    633       Peptidoglycan D,D-transpeptidase MrdA.
FT                                /FTId=PRO_0000195445.
FT   TRANSMEM     22     42       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_02081}.
FT   ACT_SITE    330    330       Acyl-ester intermediate.
FT                                {ECO:0000255|HAMAP-Rule:MF_02081}.
SQ   SEQUENCE   633 AA;  70857 MW;  FE2305C002743AF6 CRC64;
     MKLQNSFRDY TAESALFVRR ALVAFLGILL LTGVLIANLY NLQIVRFTDY QTRSNENRIK
     LVPIAPSRGI IYDRNGIPLA LNRTIYQIEM MPEKVDNVQQ TLDALRSVVD LTDDDIAAFR
     KERARSHRFT SIPVKTNLTE VQVARFAVNQ YRFPGVEVKG YKRRYYPYGS ALTHVIGYVS
     KINDKDVERL NNDGKLANYA ATHDIGKLGI ERYYEDVLHG QTGYEEVEVN NRGRVIRQLK
     EVPPQAGHDI YLTLDLKLQQ YIETLLAGSR AAVVVTDPRT GGVLALVSTP SYDPNLFVDG
     ISSKDYSALL NDPNTPLVNR ATQGVYPPAS TVKPYVAVSA LSAGVITRNT TLFDPGWWQL
     PGSEKRYRDW KKWGHGRLNV TRSLEESADT FFYQVAYDMG IDRLSEWMGK FGYGHYTGID
     LAEERSGNMP TREWKQKRFK KPWYQGDTIP VGIGQGYWTA TPIQMSKALM ILINDGIVKV
     PHLLMSTAED GKQVPWVQPH EPPVGDIHSG YWELAKDGMY GVANRPNGTA HKYFASAPYK
     IAAKSGTAQV FGLKANETYN AHKIAERLRD HKLMTAFAPY NNPQVAVAMI LENGGAGPAV
     GTLMRQILDH IMLGDNNTDL PAENPAVAAA EDH
//

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