MLTG_ECOLI
ID MLTG_ECOLI Reviewed; 340 AA.
AC P28306; P71200; P75944; Q2MBI2;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Endolytic murein transglycosylase {ECO:0000255|HAMAP-Rule:MF_02065, ECO:0000305};
DE EC=4.2.2.- {ECO:0000255|HAMAP-Rule:MF_02065, ECO:0000269|PubMed:26507882};
DE AltName: Full=Peptidoglycan polymerization terminase {ECO:0000255|HAMAP-Rule:MF_02065, ECO:0000303|PubMed:26507882};
GN Name=mltG {ECO:0000255|HAMAP-Rule:MF_02065, ECO:0000303|PubMed:26507882};
GN Synonyms=yceG; OrderedLocusNames=b1097, JW1083;
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 1-243.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=1644759; DOI=10.1128/jb.174.16.5317-5323.1992;
RA Green J.M., Merkel W.K., Nichols B.P.;
RT "Characterization and sequence of Escherichia coli pabC, the gene encoding
RT aminodeoxychorismate lyase, a pyridoxal phosphate-containing enzyme.";
RL J. Bacteriol. 174:5317-5323(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 239-340.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8631667; DOI=10.1128/jb.178.10.2804-2812.1996;
RA Reynes J.-P., Tiraby M., Baron M., Drocourt D., Tiraby G.;
RT "Escherichia coli thymidylate kinase: molecular cloning, nucleotide
RT sequence, and genetic organization of the corresponding tmk locus.";
RL J. Bacteriol. 178:2804-2812(1996).
RN [5]
RP FUNCTION, INTERACTION WITH PBP1B, SUBCELLULAR LOCATION, DISRUPTION
RP PHENOTYPE, AND MUTAGENESIS OF GLU-218.
RX PubMed=26507882; DOI=10.1111/mmi.13258;
RA Yunck R., Cho H., Bernhardt T.G.;
RT "Identification of MltG as a potential terminase for peptidoglycan
RT polymerization in bacteria.";
RL Mol. Microbiol. 99:700-718(2016).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) OF 72-340, AND SUBUNIT.
RG New York structural genomix research consortium (NYSGXRC);
RT "Crystal structure of predicted aminodeoxychorismate lyase from Escherichia
RT coli.";
RL Submitted (SEP-2007) to the PDB data bank.
CC -!- FUNCTION: Functions as a peptidoglycan terminase that cleaves nascent
CC peptidoglycan strands endolytically to terminate their elongation.
CC {ECO:0000255|HAMAP-Rule:MF_02065, ECO:0000269|PubMed:26507882}.
CC -!- SUBUNIT: Homodimer (Ref.6). Interacts with PBP1b (PubMed:26507882).
CC {ECO:0000269|PubMed:26507882, ECO:0000269|Ref.6}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_02065, ECO:0000269|PubMed:26507882}; Single-pass membrane
CC protein {ECO:0000255|HAMAP-Rule:MF_02065, ECO:0000269|PubMed:26507882}.
CC -!- DISRUPTION PHENOTYPE: Inactivation leads to a significant increase in
CC glycan strand length in the mature peptidoglycan matrix.
CC {ECO:0000269|PubMed:26507882}.
CC -!- SIMILARITY: Belongs to the transglycosylase MltG family.
CC {ECO:0000255|HAMAP-Rule:MF_02065, ECO:0000305}.
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DR EMBL; U00096; AAC74181.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76374.1; -; Genomic_DNA.
DR EMBL; M93135; AAA24268.1; -; Genomic_DNA.
DR EMBL; U41456; AAB06877.1; -; Genomic_DNA.
DR PIR; F64853; F64853.
DR RefSeq; NP_415615.1; NC_000913.3.
DR RefSeq; WP_000756827.1; NZ_SSZK01000019.1.
DR PDB; 2R1F; X-ray; 2.21 A; A/B=72-340.
DR PDBsum; 2R1F; -.
DR AlphaFoldDB; P28306; -.
DR SMR; P28306; -.
DR BioGRID; 4260071; 973.
DR IntAct; P28306; 4.
DR STRING; 511145.b1097; -.
DR jPOST; P28306; -.
DR PaxDb; P28306; -.
DR PRIDE; P28306; -.
DR EnsemblBacteria; AAC74181; AAC74181; b1097.
DR EnsemblBacteria; BAE76374; BAE76374; BAE76374.
DR GeneID; 945660; -.
DR KEGG; ecj:JW1083; -.
DR KEGG; eco:b1097; -.
DR PATRIC; fig|1411691.4.peg.1171; -.
DR EchoBASE; EB1457; -.
DR eggNOG; COG1559; Bacteria.
DR HOGENOM; CLU_025574_0_2_6; -.
DR InParanoid; P28306; -.
DR OMA; IAMPGKA; -.
DR PhylomeDB; P28306; -.
DR BioCyc; EcoCyc:EG11494-MON; -.
DR BioCyc; MetaCyc:EG11494-MON; -.
DR EvolutionaryTrace; P28306; -.
DR PRO; PR:P28306; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; ISM:EcoCyc.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; ISM:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0008932; F:lytic endotransglycosylase activity; IDA:EcoCyc.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0000270; P:peptidoglycan metabolic process; IMP:EcoCyc.
DR CDD; cd08010; MltG_like; 1.
DR HAMAP; MF_02065; MltG; 1.
DR InterPro; IPR003770; MLTG-like.
DR PANTHER; PTHR30518; PTHR30518; 1.
DR Pfam; PF02618; YceG; 1.
DR TIGRFAMs; TIGR00247; TIGR00247; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane;
KW Cell wall biogenesis/degradation; Lyase; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..340
FT /note="Endolytic murein transglycosylase"
FT /id="PRO_0000168817"
FT TOPO_DOM 1..3
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:26507882"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02065"
FT TOPO_DOM 25..340
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:26507882"
FT SITE 218
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02065,
FT ECO:0000269|PubMed:26507882"
FT MUTAGEN 218
FT /note="E->Q: Lack of activity."
FT /evidence="ECO:0000269|PubMed:26507882"
FT STRAND 85..89
FT /evidence="ECO:0007829|PDB:2R1F"
FT HELIX 95..104
FT /evidence="ECO:0007829|PDB:2R1F"
FT STRAND 110..113
FT /evidence="ECO:0007829|PDB:2R1F"
FT HELIX 120..128
FT /evidence="ECO:0007829|PDB:2R1F"
FT HELIX 142..149
FT /evidence="ECO:0007829|PDB:2R1F"
FT STRAND 164..168
FT /evidence="ECO:0007829|PDB:2R1F"
FT HELIX 174..194
FT /evidence="ECO:0007829|PDB:2R1F"
FT HELIX 205..218
FT /evidence="ECO:0007829|PDB:2R1F"
FT HELIX 222..224
FT /evidence="ECO:0007829|PDB:2R1F"
FT HELIX 225..238
FT /evidence="ECO:0007829|PDB:2R1F"
FT HELIX 245..252
FT /evidence="ECO:0007829|PDB:2R1F"
FT HELIX 253..255
FT /evidence="ECO:0007829|PDB:2R1F"
FT HELIX 262..266
FT /evidence="ECO:0007829|PDB:2R1F"
FT TURN 273..275
FT /evidence="ECO:0007829|PDB:2R1F"
FT STRAND 276..278
FT /evidence="ECO:0007829|PDB:2R1F"
FT HELIX 289..296
FT /evidence="ECO:0007829|PDB:2R1F"
FT STRAND 305..308
FT /evidence="ECO:0007829|PDB:2R1F"
FT STRAND 310..319
FT /evidence="ECO:0007829|PDB:2R1F"
FT HELIX 320..338
FT /evidence="ECO:0007829|PDB:2R1F"
SQ SEQUENCE 340 AA; 38247 MW; 4C9217B0BFCA4E6E CRC64;
MKKVLLIILL LLVVLGIAAG VGVWKVRHLA DSKLLIKEET IFTLKPGTGR LALGEQLYAD
KIINRPRVFQ WLLRIEPDLS HFKAGTYRFT PQMTVREMLK LLESGKEAQF PLRLVEGMRL
SDYLKQLREA PYIKHTLSDD KYATVAQALE LENPEWIEGW FWPDTWMYTA NTTDVALLKR
AHKKMVKAVD SAWEGRADGL PYKDKNQLVT MASIIEKETA VASERDKVAS VFINRLRIGM
RLQTDPTVIY GMGERYNGKL SRADLETPTA YNTYTITGLP PGAIATPGAD SLKAAAHPAK
TPYLYFVADG KGGHTFNTNL ASHNKSVQDY LKVLKEKNAQ
