MLTF_ECOLI
ID MLTF_ECOLI Reviewed; 518 AA.
AC P0AGC5; P30135; Q2MAH2; Q83QJ0;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Membrane-bound lytic murein transglycosylase F {ECO:0000255|HAMAP-Rule:MF_02016};
DE EC=4.2.2.n1 {ECO:0000255|HAMAP-Rule:MF_02016};
DE AltName: Full=Murein lyase F {ECO:0000255|HAMAP-Rule:MF_02016};
DE Flags: Precursor;
GN Name=mltF {ECO:0000255|HAMAP-Rule:MF_02016}; Synonyms=yfhD;
GN OrderedLocusNames=b2558, JW2542;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RA Nashimoto H., Saito N.;
RL Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-345.
RX PubMed=2659070; DOI=10.1021/bi00432a017;
RA Schendel F.J., Mueller E., Stubbe J., Shiau A., Smith J.M.;
RT "Formylglycinamide ribonucleotide synthetase from Escherichia coli:
RT cloning, sequencing, overproduction, isolation, and characterization.";
RL Biochemistry 28:2459-2471(1989).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 77-518.
RC STRAIN=NWL37;
RX PubMed=1602968; DOI=10.1111/j.1365-2958.1992.tb01540.x;
RA Poulsen L.K., Larsen N.W., Molin S., Andersson P.;
RT "Analysis of an Escherichia coli mutant strain resistant to the cell-
RT killing function encoded by the gef gene family.";
RL Mol. Microbiol. 6:895-905(1992).
RN [6]
RP SIMILARITY TO SLT.
RX PubMed=8203016; DOI=10.1016/0968-0004(94)90201-1;
RA Koonin E.V., Rudd K.E.;
RT "A conserved domain in putative bacterial and bacteriophage
RT transglycosylases.";
RL Trends Biochem. Sci. 19:106-107(1994).
RN [7]
RP CHARACTERIZATION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR LOCATION.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=18234673; DOI=10.1074/jbc.m710135200;
RA Scheurwater E.M., Clarke A.J.;
RT "The C-terminal domain of Escherichia coli YfhD functions as a lytic
RT transglycosylase.";
RL J. Biol. Chem. 283:8363-8373(2008).
RN [8]
RP REVIEW.
RX PubMed=17468031; DOI=10.1016/j.biocel.2007.03.018;
RA Scheurwater E., Reid C.W., Clarke A.J.;
RT "Lytic transglycosylases: bacterial space-making autolysins.";
RL Int. J. Biochem. Cell Biol. 40:586-591(2008).
CC -!- FUNCTION: Murein-degrading enzyme that degrades murein glycan strands
CC and insoluble, high-molecular weight murein sacculi, with the
CC concomitant formation of a 1,6-anhydromuramoyl product. Lytic
CC transglycosylases (LTs) play an integral role in the metabolism of the
CC peptidoglycan (PG) sacculus. Their lytic action creates space within
CC the PG sacculus to allow for its expansion as well as for the insertion
CC of various structures such as secretion systems and flagella.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Exolytic cleavage of the (1->4)-beta-glycosidic linkage
CC between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine
CC (GlcNAc) residues in peptidoglycan, from either the reducing or the
CC non-reducing ends of the peptidoglycan chains, with concomitant
CC formation of a 1,6-anhydrobond in the MurNAc residue.; EC=4.2.2.n1;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02016};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.5-7.0. {ECO:0000269|PubMed:18234673};
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000255|HAMAP-
CC Rule:MF_02016, ECO:0000269|PubMed:18234673}; Peripheral membrane
CC protein {ECO:0000255|HAMAP-Rule:MF_02016, ECO:0000269|PubMed:18234673}.
CC Note=Attached to the inner leaflet of the outer membrane.
CC -!- DOMAIN: The N-terminal domain does not have lytic activity and probably
CC modulates enzymatic activity. The C-terminal domain is the catalytic
CC active domain.
CC -!- SIMILARITY: In the N-terminal section; belongs to the bacterial solute-
CC binding protein 3 family. {ECO:0000255|HAMAP-Rule:MF_02016}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the transglycosylase
CC Slt family. {ECO:0000255|HAMAP-Rule:MF_02016}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA79820.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA10908.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA10908.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAE76734.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA51065.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D64044; BAA10908.1; ALT_SEQ; Genomic_DNA.
DR EMBL; U36841; AAA79820.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC75611.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE76734.1; ALT_INIT; Genomic_DNA.
DR EMBL; M19501; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X72336; CAA51065.1; ALT_FRAME; Genomic_DNA.
DR PIR; E65033; E65033.
DR RefSeq; NP_417053.2; NC_000913.3.
DR RefSeq; WP_000734212.1; NZ_STEB01000011.1.
DR AlphaFoldDB; P0AGC5; -.
DR SMR; P0AGC5; -.
DR BioGRID; 4259207; 7.
DR STRING; 511145.b2558; -.
DR PaxDb; P0AGC5; -.
DR PRIDE; P0AGC5; -.
DR DNASU; 947028; -.
DR EnsemblBacteria; AAC75611; AAC75611; b2558.
DR EnsemblBacteria; BAE76734; BAE76734; BAE76734.
DR GeneID; 58390604; -.
DR GeneID; 947028; -.
DR KEGG; ecj:JW2542; -.
DR KEGG; eco:b2558; -.
DR PATRIC; fig|1411691.4.peg.4176; -.
DR EchoBASE; EB1347; -.
DR eggNOG; COG4623; Bacteria.
DR HOGENOM; CLU_027494_0_1_6; -.
DR InParanoid; P0AGC5; -.
DR OMA; YYDILTW; -.
DR PhylomeDB; P0AGC5; -.
DR BioCyc; EcoCyc:EG11373-MON; -.
DR BioCyc; MetaCyc:EG11373-MON; -.
DR PRO; PR:P0AGC5; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IDA:EcoCyc.
DR GO; GO:0016837; F:carbon-oxygen lyase activity, acting on polysaccharides; IEA:InterPro.
DR GO; GO:0008933; F:lytic transglycosylase activity; IDA:EcoCyc.
DR GO; GO:0016998; P:cell wall macromolecule catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009253; P:peptidoglycan catabolic process; IDA:EcoCyc.
DR HAMAP; MF_02016; MltF; 1.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR023703; MltF.
DR InterPro; IPR001638; Solute-binding_3/MltF_N.
DR InterPro; IPR000189; Transglyc_AS.
DR InterPro; IPR008258; Transglycosylase_SLT_dom_1.
DR Pfam; PF00497; SBP_bac_3; 1.
DR Pfam; PF01464; SLT; 1.
DR SMART; SM00062; PBPb; 1.
DR SUPFAM; SSF53955; SSF53955; 1.
DR PROSITE; PS00922; TRANSGLYCOSYLASE; 1.
PE 1: Evidence at protein level;
KW Cell outer membrane; Cell wall biogenesis/degradation; Lyase; Membrane;
KW Reference proteome; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02016"
FT CHAIN 22..518
FT /note="Membrane-bound lytic murein transglycosylase F"
FT /id="PRO_0000196562"
FT REGION 22..269
FT /note="Non-LT domain"
FT REGION 270..518
FT /note="LT domain"
FT ACT_SITE 314
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02016"
FT CONFLICT 150..151
FT /note="EQ -> DR (in Ref. 1; BAA10908 and 4; M19501)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 518 AA; 58302 MW; 70A5ABE842E47D4A CRC64;
MKKLKINYLF IGILALLLAV ALWPSIPWFG KADNRIAAIQ ARGELRVSTI HTPLTYNEIN
GKPFGLDYEL AKQFADYLGV KLKVTVRQNI SQLFDDLDNG NADLLAAGLV YNSERVKNYQ
PGPTYYSVSQ QLVYKVGQYR PRTLGNLTAE QLTVAPGHVV VNDLQTLKET KFPELSWKVD
DKKGSAELME DVIEGKLDYT IADSVAISLF QRVHPELAVA LDITDEQPVT WFSPLDGDNT
LSAALLDFFN EMNEDGTLAR IEEKYLGHGD DFDYVDTRTF LRAVDAVLPQ LKPLFEKYAE
EIDWRLLAAI AYQESHWDAQ ATSPTGVRGM MMLTKNTAQS LGITDRTDAE QSISGGVRYL
QDMMSKVPES VPENERIWFA LAAYNMGYAH MLDARALTAK TKGNPDSWAD VKQRLPLLSQ
KPYYSKLTYG YARGHEAYAY VENIRKYQIS LVGYLQEKEK QATEAAMQLA QDYPAVSPTE
LGKEKFPFLS FLSQSSSNYL THSPSLLFSR KGSEEKQN
