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Peptidoglycan D,D-transpeptidase MrdA (EC 3.4.16.4) (Penicillin-binding protein 2) (PBP-2)

 MRDA_ECOLI              Reviewed;         633 AA.
P0AD65; P08150;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
01-AUG-1988, sequence version 1.
28-MAR-2018, entry version 103.
RecName: Full=Peptidoglycan D,D-transpeptidase MrdA {ECO:0000255|HAMAP-Rule:MF_02081, ECO:0000305};
EC=3.4.16.4 {ECO:0000255|HAMAP-Rule:MF_02081, ECO:0000269|PubMed:3009484};
AltName: Full=Penicillin-binding protein 2 {ECO:0000255|HAMAP-Rule:MF_02081, ECO:0000303|PubMed:1103132, ECO:0000303|PubMed:3009484};
Short=PBP-2 {ECO:0000255|HAMAP-Rule:MF_02081, ECO:0000303|PubMed:3009484};
Name=mrdA {ECO:0000255|HAMAP-Rule:MF_02081,
ECO:0000303|PubMed:3009484};
Synonyms=pbpA {ECO:0000303|PubMed:3533535,
ECO:0000303|PubMed:3894330}; OrderedLocusNames=b0635, JW0630;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-18.
STRAIN=K12;
PubMed=3533535; DOI=10.1111/j.1432-1033.1986.tb09961.x;
Asoh S., Matsuzawa H., Ishino F., Strominger J.L., Matsuhashi M.,
Ohta T.;
"Nucleotide sequence of the pbpA gene and characteristics of the
deduced amino acid sequence of penicillin-binding protein 2 of
Escherichia coli K12.";
Eur. J. Biochem. 160:231-238(1986).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=8905232; DOI=10.1093/dnares/3.3.137;
Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A.,
Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K.,
Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K.,
Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N.,
Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y.,
Yano M., Horiuchi T.;
"A 718-kb DNA sequence of the Escherichia coli K-12 genome
corresponding to the 12.7-28.0 min region on the linkage map.";
DNA Res. 3:137-155(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
"Sequence of minutes 4-25 of Escherichia coli.";
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[6]
PROTEIN SEQUENCE OF 321-334 AND 633, ACTIVE SITE, PENICILLIN-BINDING,
AND MUTAGENESIS OF SER-330.
PubMed=3148617;
Takasuga A., Adachi H., Ishino F., Matsuhashi M., Ohta T.,
Matsuzawa H.;
"Identification of the penicillin-binding active site of penicillin-
binding protein 2 of Escherichia coli.";
J. Biochem. 104:822-826(1988).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 606-633.
STRAIN=K12;
PubMed=2644207; DOI=10.1128/jb.171.1.558-560.1989;
Matsuzawa H., Asoh S., Kunai K., Muraiso K., Takasuga A., Ohta T.;
"Nucleotide sequence of the rodA gene, responsible for the rod shape
of Escherichia coli: rodA and the pbpA gene, encoding penicillin-
binding protein 2, constitute the rodA operon.";
J. Bacteriol. 171:558-560(1989).
[8]
FUNCTION, SUBCELLULAR LOCATION, AND ENZYME REGULATION.
STRAIN=K12;
PubMed=1103132; DOI=10.1073/pnas.72.8.2999;
Spratt B.G.;
"Distinct penicillin binding proteins involved in the division,
elongation, and shape of Escherichia coli K12.";
Proc. Natl. Acad. Sci. U.S.A. 72:2999-3003(1975).
[9]
DISRUPTION PHENOTYPE.
PubMed=3894330;
Begg K.J., Donachie W.D.;
"Cell shape and division in Escherichia coli: experiments with shape
and division mutants.";
J. Bacteriol. 163:615-622(1985).
[10]
FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, PATHWAY, AND
SUBCELLULAR LOCATION.
PubMed=3009484;
Ishino F., Park W., Tomioka S., Tamaki S., Takase I., Kunugita K.,
Matsuzawa H., Asoh S., Ohta T., Spratt B.G.;
"Peptidoglycan synthetic activities in membranes of Escherichia coli
caused by overproduction of penicillin-binding protein 2 and rodA
protein.";
J. Biol. Chem. 261:7024-7031(1986).
[11]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=12519203; DOI=10.1046/j.1365-2958.2003.03316.x;
Den Blaauwen T., Aarsman M.E., Vischer N.O., Nanninga N.;
"Penicillin-binding protein PBP2 of Escherichia coli localizes
preferentially in the lateral wall and at mid-cell in comparison with
the old cell pole.";
Mol. Microbiol. 47:539-547(2003).
-!- FUNCTION: Catalyzes cross-linking of the peptidoglycan cell wall
(PubMed:3009484). Responsible for the determination of the rod
shape of the cell (PubMed:1103132). Is probably required for
lateral peptidoglycan synthesis and maintenance of the correct
diameter during lateral and centripetal growth (PubMed:12519203).
{ECO:0000269|PubMed:1103132, ECO:0000269|PubMed:12519203,
ECO:0000269|PubMed:3009484}.
-!- CATALYTIC ACTIVITY: Preferential cleavage: (Ac)(2)-L-Lys-D-Ala-|-
D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are
N-acyl substituents of D-alanine. {ECO:0000255|HAMAP-
Rule:MF_02081, ECO:0000269|PubMed:3009484}.
-!- ENZYME REGULATION: Inhibited by mecillinam and benzylpenicillin.
{ECO:0000269|PubMed:1103132, ECO:0000269|PubMed:3009484}.
-!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
{ECO:0000255|HAMAP-Rule:MF_02081, ECO:0000269|PubMed:3009484}.
-!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
Rule:MF_02081, ECO:0000269|PubMed:1103132,
ECO:0000269|PubMed:3009484}; Single-pass membrane protein
{ECO:0000255|HAMAP-Rule:MF_02081}. Note=Localizes preferentially
in the lateral wall and at mid-cell in comparison with the old
cell pole. Localization at mid-cell is dependent on active FtsI.
{ECO:0000269|PubMed:12519203}.
-!- DISRUPTION PHENOTYPE: Temperature-sensitive mutants grow as normal
rods at 30 degrees Celsius but grow and divide as cocci during
prolonged culturing at 42 degrees Celsius.
{ECO:0000269|PubMed:3894330}.
-!- SIMILARITY: Belongs to the transpeptidase family. MrdA subfamily.
{ECO:0000255|HAMAP-Rule:MF_02081, ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X04516; CAA28201.1; -; Genomic_DNA.
EMBL; U82598; AAB40835.1; -; Genomic_DNA.
EMBL; U00096; AAC73736.1; -; Genomic_DNA.
EMBL; AP009048; BAA35282.1; -; Genomic_DNA.
EMBL; M22857; AAA24570.1; -; Genomic_DNA.
PIR; C24995; ZPECP2.
RefSeq; NP_415168.1; NC_000913.3.
RefSeq; WP_000776191.1; NZ_LN832404.1.
ProteinModelPortal; P0AD65; -.
SMR; P0AD65; -.
BioGrid; 4259912; 573.
DIP; DIP-48190N; -.
IntAct; P0AD65; 2.
STRING; 316385.ECDH10B_0704; -.
ChEMBL; CHEMBL1840; -.
DrugBank; DB01163; Amdinocillin.
DrugBank; DB01327; Cefazolin.
DrugBank; DB01413; Cefepime.
DrugBank; DB01328; Cefonicid.
DrugBank; DB01329; Cefoperazone.
DrugBank; DB00438; Ceftazidime.
DrugBank; DB01415; Ceftibuten.
DrugBank; DB06211; Doripenem.
DrugBank; DB00303; Ertapenem.
DrugBank; DB01598; Imipenem.
DrugBank; DB00948; Mezlocillin.
PaxDb; P0AD65; -.
PRIDE; P0AD65; -.
EnsemblBacteria; AAC73736; AAC73736; b0635.
EnsemblBacteria; BAA35282; BAA35282; BAA35282.
GeneID; 945240; -.
KEGG; ecj:JW0630; -.
KEGG; eco:b0635; -.
PATRIC; fig|1411691.4.peg.1633; -.
EchoBASE; EB0601; -.
EcoGene; EG10606; mrdA.
eggNOG; ENOG4105CJN; Bacteria.
eggNOG; COG0768; LUCA.
HOGENOM; HOG000266120; -.
InParanoid; P0AD65; -.
KO; K05515; -.
OMA; SCDTYYY; -.
PhylomeDB; P0AD65; -.
BioCyc; EcoCyc:EG10606-MONOMER; -.
BioCyc; MetaCyc:EG10606-MONOMER; -.
UniPathway; UPA00219; -.
PRO; PR:P0AD65; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoliWiki.
GO; GO:0008144; F:drug binding; IDA:EcoCyc.
GO; GO:0008658; F:penicillin binding; IMP:EcoliWiki.
GO; GO:0071972; F:peptidoglycan L,D-transpeptidase activity; IDA:EcoliWiki.
GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IDA:EcoCyc.
GO; GO:0071555; P:cell wall organization; IMP:EcoCyc.
GO; GO:0009252; P:peptidoglycan biosynthetic process; IMP:EcoCyc.
GO; GO:0008360; P:regulation of cell shape; IMP:EcoliWiki.
GO; GO:0046677; P:response to antibiotic; IMP:EcoliWiki.
GO; GO:0042493; P:response to drug; IDA:EcoCyc.
HAMAP; MF_02081; MrdA_transpept; 1.
InterPro; IPR012338; Beta-lactam/transpept-like.
InterPro; IPR005311; PBP_dimer.
InterPro; IPR036138; PBP_dimer_sf.
InterPro; IPR001460; PCN-bd_Tpept.
InterPro; IPR017790; Penicillin-binding_protein_2.
Pfam; PF03717; PBP_dimer; 1.
Pfam; PF00905; Transpeptidase; 1.
SUPFAM; SSF56519; SSF56519; 1.
SUPFAM; SSF56601; SSF56601; 1.
TIGRFAMs; TIGR03423; pbp2_mrdA; 1.
1: Evidence at protein level;
Carboxypeptidase; Cell inner membrane; Cell membrane; Cell shape;
Cell wall biogenesis/degradation; Complete proteome;
Direct protein sequencing; Hydrolase; Membrane;
Peptidoglycan synthesis; Protease; Reference proteome; Transmembrane;
Transmembrane helix.
CHAIN 1 633 Peptidoglycan D,D-transpeptidase MrdA.
/FTId=PRO_0000195444.
TRANSMEM 22 42 Helical. {ECO:0000255|HAMAP-
Rule:MF_02081}.
ACT_SITE 330 330 Acyl-ester intermediate.
{ECO:0000255|HAMAP-Rule:MF_02081,
ECO:0000269|PubMed:3148617}.
MUTAGEN 330 330 S->C: No longer binds penicillin.
{ECO:0000269|PubMed:3148617}.
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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