MRDA_ECOLI
ID MRDA_ECOLI Reviewed; 633 AA.
AC P0AD65; P08150;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Peptidoglycan D,D-transpeptidase MrdA {ECO:0000255|HAMAP-Rule:MF_02081, ECO:0000305};
DE EC=3.4.16.4 {ECO:0000255|HAMAP-Rule:MF_02081, ECO:0000269|PubMed:3009484};
DE AltName: Full=Penicillin-binding protein 2 {ECO:0000255|HAMAP-Rule:MF_02081, ECO:0000303|PubMed:1103132, ECO:0000303|PubMed:3009484};
DE Short=PBP-2 {ECO:0000255|HAMAP-Rule:MF_02081, ECO:0000303|PubMed:3009484};
GN Name=mrdA {ECO:0000255|HAMAP-Rule:MF_02081, ECO:0000303|PubMed:3009484};
GN Synonyms=pbpA {ECO:0000303|PubMed:3533535, ECO:0000303|PubMed:3894330};
GN OrderedLocusNames=b0635, JW0630;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-18.
RC STRAIN=K12;
RX PubMed=3533535; DOI=10.1111/j.1432-1033.1986.tb09961.x;
RA Asoh S., Matsuzawa H., Ishino F., Strominger J.L., Matsuhashi M., Ohta T.;
RT "Nucleotide sequence of the pbpA gene and characteristics of the deduced
RT amino acid sequence of penicillin-binding protein 2 of Escherichia coli
RT K12.";
RL Eur. J. Biochem. 160:231-238(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
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 [6]
RP PROTEIN SEQUENCE OF 321-334 AND 633, ACTIVE SITE, PENICILLIN-BINDING, AND
RP MUTAGENESIS OF SER-330.
RX PubMed=3148617; DOI=10.1093/oxfordjournals.jbchem.a122556;
RA Takasuga A., Adachi H., Ishino F., Matsuhashi M., Ohta T., Matsuzawa H.;
RT "Identification of the penicillin-binding active site of penicillin-binding
RT protein 2 of Escherichia coli.";
RL J. Biochem. 104:822-826(1988).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 606-633.
RC STRAIN=K12;
RX PubMed=2644207; DOI=10.1128/jb.171.1.558-560.1989;
RA Matsuzawa H., Asoh S., Kunai K., Muraiso K., Takasuga A., Ohta T.;
RT "Nucleotide sequence of the rodA gene, responsible for the rod shape of
RT Escherichia coli: rodA and the pbpA gene, encoding penicillin-binding
RT protein 2, constitute the rodA operon.";
RL J. Bacteriol. 171:558-560(1989).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND ACTIVITY REGULATION.
RC STRAIN=K12;
RX PubMed=1103132; DOI=10.1073/pnas.72.8.2999;
RA Spratt B.G.;
RT "Distinct penicillin binding proteins involved in the division, elongation,
RT and shape of Escherichia coli K12.";
RL Proc. Natl. Acad. Sci. U.S.A. 72:2999-3003(1975).
RN [9]
RP DISRUPTION PHENOTYPE.
RX PubMed=3894330; DOI=10.1128/jb.163.2.615-622.1985;
RA Begg K.J., Donachie W.D.;
RT "Cell shape and division in Escherichia coli: experiments with shape and
RT division mutants.";
RL J. Bacteriol. 163:615-622(1985).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, PATHWAY, AND SUBCELLULAR
RP LOCATION.
RX PubMed=3009484; DOI=10.1016/s0021-9258(19)62717-1;
RA Ishino F., Park W., Tomioka S., Tamaki S., Takase I., Kunugita K.,
RA Matsuzawa H., Asoh S., Ohta T., Spratt B.G.;
RT "Peptidoglycan synthetic activities in membranes of Escherichia coli caused
RT by overproduction of penicillin-binding protein 2 and rodA protein.";
RL J. Biol. Chem. 261:7024-7031(1986).
RN [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12519203; DOI=10.1046/j.1365-2958.2003.03316.x;
RA Den Blaauwen T., Aarsman M.E., Vischer N.O., Nanninga N.;
RT "Penicillin-binding protein PBP2 of Escherichia coli localizes
RT preferentially in the lateral wall and at mid-cell in comparison with the
RT old cell pole.";
RL Mol. Microbiol. 47:539-547(2003).
CC -!- FUNCTION: Catalyzes cross-linking of the peptidoglycan cell wall
CC (PubMed:3009484). Responsible for the determination of the rod shape of
CC the cell (PubMed:1103132). Is probably required for lateral
CC peptidoglycan synthesis and maintenance of the correct diameter during
CC lateral and centripetal growth (PubMed:12519203).
CC {ECO:0000269|PubMed:1103132, ECO:0000269|PubMed:12519203,
CC ECO:0000269|PubMed:3009484}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also
CC transpeptidation of peptidyl-alanyl moieties that are N-acyl
CC substituents of D-alanine.; EC=3.4.16.4; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_02081, ECO:0000269|PubMed:3009484};
CC -!- ACTIVITY REGULATION: Inhibited by mecillinam and benzylpenicillin.
CC {ECO:0000269|PubMed:1103132, ECO:0000269|PubMed:3009484}.
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_02081, ECO:0000269|PubMed:3009484}.
CC -!- INTERACTION:
CC P0AD65; P02918: mrcA; NbExp=5; IntAct=EBI-1124032, EBI-1126191;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_02081, ECO:0000269|PubMed:1103132, ECO:0000269|PubMed:3009484};
CC Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_02081}.
CC Note=Localizes preferentially in the lateral wall and at mid-cell in
CC comparison with the old cell pole. Localization at mid-cell is
CC dependent on active FtsI. {ECO:0000269|PubMed:12519203}.
CC -!- DISRUPTION PHENOTYPE: Temperature-sensitive mutants grow as normal rods
CC at 30 degrees Celsius but grow and divide as cocci during prolonged
CC culturing at 42 degrees Celsius. {ECO:0000269|PubMed:3894330}.
CC -!- SIMILARITY: Belongs to the transpeptidase family. MrdA subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_02081, ECO:0000305}.
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DR EMBL; X04516; CAA28201.1; -; Genomic_DNA.
DR EMBL; U82598; AAB40835.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73736.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35282.1; -; Genomic_DNA.
DR EMBL; M22857; AAA24570.1; -; Genomic_DNA.
DR PIR; C24995; ZPECP2.
DR RefSeq; NP_415168.1; NC_000913.3.
DR RefSeq; WP_000776191.1; NZ_STEB01000031.1.
DR PDB; 6G9F; X-ray; 2.35 A; A=57-615.
DR PDB; 6G9P; X-ray; 2.10 A; A=52-633.
DR PDB; 6G9S; X-ray; 2.00 A; A=52-633.
DR PDBsum; 6G9F; -.
DR PDBsum; 6G9P; -.
DR PDBsum; 6G9S; -.
DR AlphaFoldDB; P0AD65; -.
DR SMR; P0AD65; -.
DR BioGRID; 4259912; 573.
DR ComplexPortal; CPX-5718; Elongasome complex.
DR DIP; DIP-48190N; -.
DR IntAct; P0AD65; 6.
DR STRING; 511145.b0635; -.
DR ChEMBL; CHEMBL1840; -.
DR ChEMBL; CHEMBL2354313; -.
DR DrugBank; DB01163; Amdinocillin.
DR DrugBank; DB01602; Bacampicillin.
DR DrugBank; DB00578; Carbenicillin.
DR DrugBank; DB09319; Carindacillin.
DR DrugBank; DB01327; Cefazolin.
DR DrugBank; DB01413; Cefepime.
DR DrugBank; DB01328; Cefonicid.
DR DrugBank; DB01329; Cefoperazone.
DR DrugBank; DB00438; Ceftazidime.
DR DrugBank; DB01415; Ceftibuten.
DR DrugBank; DB09050; Ceftolozane.
DR DrugBank; DB01000; Cyclacillin.
DR DrugBank; DB06211; Doripenem.
DR DrugBank; DB00303; Ertapenem.
DR DrugBank; DB01598; Imipenem.
DR DrugBank; DB00948; Mezlocillin.
DR DrugCentral; P0AD65; -.
DR MEROPS; X52.001; -.
DR jPOST; P0AD65; -.
DR PaxDb; P0AD65; -.
DR PRIDE; P0AD65; -.
DR EnsemblBacteria; AAC73736; AAC73736; b0635.
DR EnsemblBacteria; BAA35282; BAA35282; BAA35282.
DR GeneID; 66671091; -.
DR GeneID; 945240; -.
DR KEGG; ecj:JW0630; -.
DR KEGG; eco:b0635; -.
DR PATRIC; fig|1411691.4.peg.1633; -.
DR EchoBASE; EB0601; -.
DR eggNOG; COG0768; Bacteria.
DR HOGENOM; CLU_009289_1_2_6; -.
DR InParanoid; P0AD65; -.
DR OMA; SCDTYYY; -.
DR PhylomeDB; P0AD65; -.
DR BioCyc; EcoCyc:EG10606-MON; -.
DR BioCyc; MetaCyc:EG10606-MON; -.
DR UniPathway; UPA00219; -.
DR PRO; PR:P0AD65; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoliWiki.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; ISM:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0008658; F:penicillin binding; IDA:EcoCyc.
DR GO; GO:0071972; F:peptidoglycan L,D-transpeptidase activity; IDA:EcoliWiki.
DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IDA:EcoCyc.
DR GO; GO:0071555; P:cell wall organization; IMP:EcoCyc.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IDA:EcoCyc.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0008360; P:regulation of cell shape; IMP:EcoliWiki.
DR GO; GO:0046677; P:response to antibiotic; IMP:EcoliWiki.
DR Gene3D; 3.40.710.10; -; 1.
DR HAMAP; MF_02081; MrdA_transpept; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR005311; PBP_dimer.
DR InterPro; IPR036138; PBP_dimer_sf.
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 1: Evidence at protein level;
KW 3D-structure; Carboxypeptidase; Cell inner membrane; Cell membrane;
KW Cell shape; Cell wall biogenesis/degradation; Direct protein sequencing;
KW Hydrolase; Membrane; Peptidoglycan synthesis; Protease; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..633
FT /note="Peptidoglycan D,D-transpeptidase MrdA"
FT /id="PRO_0000195444"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02081"
FT ACT_SITE 330
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02081,
FT ECO:0000269|PubMed:3148617"
FT MUTAGEN 330
FT /note="S->C: No longer binds penicillin."
FT /evidence="ECO:0000269|PubMed:3148617"
FT STRAND 59..64
FT /evidence="ECO:0007829|PDB:6G9S"
FT STRAND 78..90
FT /evidence="ECO:0007829|PDB:6G9S"
FT HELIX 92..94
FT /evidence="ECO:0007829|PDB:6G9S"
FT HELIX 98..109
FT /evidence="ECO:0007829|PDB:6G9S"
FT HELIX 113..124
FT /evidence="ECO:0007829|PDB:6G9S"
FT STRAND 132..138
FT /evidence="ECO:0007829|PDB:6G9S"
FT HELIX 140..149
FT /evidence="ECO:0007829|PDB:6G9S"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:6G9S"
FT STRAND 156..165
FT /evidence="ECO:0007829|PDB:6G9S"
FT HELIX 169..172
FT /evidence="ECO:0007829|PDB:6G9S"
FT HELIX 173..176
FT /evidence="ECO:0007829|PDB:6G9S"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:6G9S"
FT HELIX 184..192
FT /evidence="ECO:0007829|PDB:6G9S"
FT HELIX 196..199
FT /evidence="ECO:0007829|PDB:6G9S"
FT STRAND 204..206
FT /evidence="ECO:0007829|PDB:6G9S"
FT HELIX 209..213
FT /evidence="ECO:0007829|PDB:6G9S"
FT HELIX 215..219
FT /evidence="ECO:0007829|PDB:6G9S"
FT STRAND 223..229
FT /evidence="ECO:0007829|PDB:6G9S"
FT HELIX 231..233
FT /evidence="ECO:0007829|PDB:6G9S"
FT STRAND 235..242
FT /evidence="ECO:0007829|PDB:6G9S"
FT STRAND 250..253
FT /evidence="ECO:0007829|PDB:6G9S"
FT HELIX 256..266
FT /evidence="ECO:0007829|PDB:6G9S"
FT STRAND 271..276
FT /evidence="ECO:0007829|PDB:6G9S"
FT TURN 278..280
FT /evidence="ECO:0007829|PDB:6G9S"
FT STRAND 282..290
FT /evidence="ECO:0007829|PDB:6G9S"
FT HELIX 295..298
FT /evidence="ECO:0007829|PDB:6G9S"
FT HELIX 303..310
FT /evidence="ECO:0007829|PDB:6G9S"
FT HELIX 320..323
FT /evidence="ECO:0007829|PDB:6G9S"
FT HELIX 329..332
FT /evidence="ECO:0007829|PDB:6G9S"
FT HELIX 333..342
FT /evidence="ECO:0007829|PDB:6G9S"
FT STRAND 352..359
FT /evidence="ECO:0007829|PDB:6G9S"
FT STRAND 366..368
FT /evidence="ECO:0007829|PDB:6G9S"
FT STRAND 376..378
FT /evidence="ECO:0007829|PDB:6G9S"
FT HELIX 380..385
FT /evidence="ECO:0007829|PDB:6G9S"
FT HELIX 390..410
FT /evidence="ECO:0007829|PDB:6G9S"
FT TURN 411..414
FT /evidence="ECO:0007829|PDB:6G9S"
FT HELIX 432..439
FT /evidence="ECO:0007829|PDB:6G9S"
FT HELIX 445..451
FT /evidence="ECO:0007829|PDB:6G9S"
FT TURN 452..454
FT /evidence="ECO:0007829|PDB:6G9S"
FT HELIX 462..473
FT /evidence="ECO:0007829|PDB:6G9S"
FT TURN 474..476
FT /evidence="ECO:0007829|PDB:6G9S"
FT STRAND 484..487
FT /evidence="ECO:0007829|PDB:6G9S"
FT STRAND 489..491
FT /evidence="ECO:0007829|PDB:6G9S"
FT STRAND 507..510
FT /evidence="ECO:0007829|PDB:6G9F"
FT HELIX 511..524
FT /evidence="ECO:0007829|PDB:6G9S"
FT HELIX 531..534
FT /evidence="ECO:0007829|PDB:6G9S"
FT STRAND 542..548
FT /evidence="ECO:0007829|PDB:6G9S"
FT STRAND 571..578
FT /evidence="ECO:0007829|PDB:6G9S"
FT STRAND 580..582
FT /evidence="ECO:0007829|PDB:6G9S"
FT STRAND 585..591
FT /evidence="ECO:0007829|PDB:6G9S"
FT HELIX 592..594
FT /evidence="ECO:0007829|PDB:6G9S"
FT STRAND 596..598
FT /evidence="ECO:0007829|PDB:6G9S"
FT HELIX 600..612
FT /evidence="ECO:0007829|PDB:6G9S"
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
