MTGA_ECOLI
ID MTGA_ECOLI Reviewed; 242 AA.
AC P46022; Q2M904;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Biosynthetic peptidoglycan transglycosylase {ECO:0000255|HAMAP-Rule:MF_00766, ECO:0000305};
DE EC=2.4.1.129 {ECO:0000255|HAMAP-Rule:MF_00766, ECO:0000269|PubMed:8772200};
DE AltName: Full=Glycan polymerase {ECO:0000255|HAMAP-Rule:MF_00766, ECO:0000303|PubMed:6368264};
DE AltName: Full=Monofunctional biosynthetic peptidoglycan transglycosylase {ECO:0000305};
DE AltName: Full=Monofunctional glycosyltransferase {ECO:0000303|PubMed:8772200};
DE Short=Monofunctional GTase {ECO:0000303|PubMed:8772200};
DE AltName: Full=Peptidoglycan glycosyltransferase MtgA {ECO:0000255|HAMAP-Rule:MF_00766, ECO:0000305};
DE Short=PGT {ECO:0000255|HAMAP-Rule:MF_00766, ECO:0000305};
GN Name=mtgA {ECO:0000255|HAMAP-Rule:MF_00766, ECO:0000303|PubMed:18165305};
GN Synonyms=mgt {ECO:0000303|PubMed:8772200}, yrbM;
GN OrderedLocusNames=b3208, JW3175;
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 / 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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-39.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Smillie D.A., Fujita N., Townsley F.M., Ishihama A., Hayward R.S.;
RT "Sequence and characterisation of the gene encoding the sigma cross-
RT reacting protein 27A in Escherichia coli.";
RL Submitted (DEC-1993) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=6368264; DOI=10.1016/0014-5793(84)80226-4;
RA Hara H., Suzuki H.;
RT "A novel glycan polymerase that synthesizes uncross-linked peptidoglycan in
RT Escherichia coli.";
RL FEBS Lett. 168:155-160(1984).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND SUBCELLULAR LOCATION.
RX PubMed=8772200; DOI=10.1016/0014-5793(96)00809-5;
RA Di Berardino M., Dijkstra A., Stueber D., Keck W., Gubler M.;
RT "The monofunctional glycosyltransferase of Escherichia coli is a member of
RT a new class of peptidoglycan-synthesising enzymes.";
RL FEBS Lett. 392:184-188(1996).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, INTERACTION WITH FTSI; FTSW AND
RP FTSN, AND SUBCELLULAR LOCATION.
RX PubMed=18165305; DOI=10.1128/jb.01377-07;
RA Derouaux A., Wolf B., Fraipont C., Breukink E., Nguyen-Disteche M.,
RA Terrak M.;
RT "The monofunctional glycosyltransferase of Escherichia coli localizes to
RT the cell division site and interacts with penicillin-binding protein 3,
RT FtsW, and FtsN.";
RL J. Bacteriol. 190:1831-1834(2008).
CC -!- FUNCTION: Peptidoglycan polymerase that catalyzes glycan chain
CC elongation from lipid-linked precursors (PubMed:6368264,
CC PubMed:8772200, PubMed:18165305). May play a role in peptidoglycan
CC assembly during cell division in collaboration with other cell division
CC proteins (PubMed:18165305). {ECO:0000269|PubMed:18165305,
CC ECO:0000269|PubMed:6368264, ECO:0000269|PubMed:8772200}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-
CC Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-
CC (1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-
CC cis-undecaprenyl diphosphate = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-
CC D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans-octa-cis-undecaprenyl
CC diphosphate + di-trans,octa-cis-undecaprenyl diphosphate + H(+);
CC Xref=Rhea:RHEA:23708, Rhea:RHEA-COMP:9602, Rhea:RHEA-COMP:9603,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58405, ChEBI:CHEBI:60033,
CC ChEBI:CHEBI:78435; EC=2.4.1.129; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00766, ECO:0000269|PubMed:18165305,
CC ECO:0000269|PubMed:8772200};
CC -!- ACTIVITY REGULATION: Inhibited by EDTA (PubMed:6368264). Stimulated by
CC Ca(2+), Mn(2+) and Co(2+) (PubMed:6368264). Not inhibited by flavomycin
CC (PubMed:8772200). {ECO:0000269|PubMed:6368264,
CC ECO:0000269|PubMed:8772200}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.0-6.5. {ECO:0000269|PubMed:6368264,
CC ECO:0000269|PubMed:8772200};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00766, ECO:0000269|PubMed:18165305}.
CC -!- SUBUNIT: Interacts with FtsI, FtsW and FtsN.
CC {ECO:0000269|PubMed:18165305}.
CC -!- INTERACTION:
CC P46022; P0AD68: ftsI; NbExp=3; IntAct=EBI-558469, EBI-548564;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00766, ECO:0000269|PubMed:8772200}; Single-pass membrane
CC protein {ECO:0000255|HAMAP-Rule:MF_00766}. Note=Localizes to the cell
CC division site. {ECO:0000269|PubMed:18165305}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 51 family.
CC {ECO:0000255|HAMAP-Rule:MF_00766, ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=D13188; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U18997; AAA58010.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76240.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77252.1; -; Genomic_DNA.
DR EMBL; D13188; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; B65112; B65112.
DR RefSeq; NP_417675.1; NC_000913.3.
DR RefSeq; WP_000047091.1; NZ_STEB01000012.1.
DR AlphaFoldDB; P46022; -.
DR SMR; P46022; -.
DR BioGRID; 4259286; 274.
DR BioGRID; 852041; 1.
DR DIP; DIP-10266N; -.
DR IntAct; P46022; 6.
DR STRING; 511145.b3208; -.
DR CAZy; GT51; Glycosyltransferase Family 51.
DR PaxDb; P46022; -.
DR PRIDE; P46022; -.
DR EnsemblBacteria; AAC76240; AAC76240; b3208.
DR EnsemblBacteria; BAE77252; BAE77252; BAE77252.
DR GeneID; 66672890; -.
DR GeneID; 947728; -.
DR KEGG; ecj:JW3175; -.
DR KEGG; eco:b3208; -.
DR PATRIC; fig|1411691.4.peg.3523; -.
DR EchoBASE; EB2659; -.
DR eggNOG; COG0744; Bacteria.
DR HOGENOM; CLU_006354_1_1_6; -.
DR InParanoid; P46022; -.
DR OMA; PAPKCFD; -.
DR PhylomeDB; P46022; -.
DR BioCyc; EcoCyc:G7668-MON; -.
DR BioCyc; MetaCyc:G7668-MON; -.
DR UniPathway; UPA00219; -.
DR PRO; PR:P46022; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0016763; F:pentosyltransferase activity; IEA:InterPro.
DR GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IDA:EcoCyc.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0043164; P:Gram-negative-bacterium-type cell wall biogenesis; IDA:EcoCyc.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IDA:EcoCyc.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR Gene3D; 1.10.3810.10; -; 1.
DR HAMAP; MF_00766; PGT_MtgA; 1.
DR InterPro; IPR001264; Glyco_trans_51.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR036950; PBP_transglycosylase.
DR InterPro; IPR011812; Pep_trsgly.
DR PANTHER; PTHR30400; PTHR30400; 1.
DR Pfam; PF00912; Transgly; 1.
DR SUPFAM; SSF53955; SSF53955; 1.
DR TIGRFAMs; TIGR02070; mono_pep_trsgly; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Cell shape;
KW Cell wall biogenesis/degradation; Glycosyltransferase; Membrane;
KW Peptidoglycan synthesis; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..242
FT /note="Biosynthetic peptidoglycan transglycosylase"
FT /id="PRO_0000083125"
FT TRANSMEM 19..39
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00766"
SQ SEQUENCE 242 AA; 27342 MW; AB3B21B91BE4BA8C CRC64;
MSKSRLTVFS FVRRFLLRLM VVLAVFWGGG IALFSVAPVP FSAVMVERQV SAWLHGNFRY
VAHSDWVSMD QISPWMGLAV IAAEDQKFPE HWGFDVASIE KALAHNERNE NRIRGASTIS
QQTAKNLFLW DGRSWVRKGL EAGLTLGIET VWSKKRILTV YLNIAEFGDG VFGVEAAAQR
YFHKPASKLT RSEAALLAAV LPNPLRFKVS SPSGYVRSRQ AWILRQMYQL GGEPFMQQHQ
LD
