ID MLTB_ECOLI Reviewed; 361 AA.
AC P41052;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 27-MAR-2024, entry version 180.
DE RecName: Full=Membrane-bound lytic murein transglycosylase B;
DE EC=4.2.2.n1;
DE AltName: Full=35 kDa soluble lytic transglycosylase;
DE AltName: Full=Murein hydrolase B;
DE AltName: Full=Slt35;
DE Flags: Precursor;
GN Name=mltB; OrderedLocusNames=b2701, JW2671;
OS Escherichia coli (strain K12).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=7476170; DOI=10.1111/j.1365-2958.1995.tb02437.x;
RA Ehlert K., Hoeltje J.-V., Templin M.F.;
RT "Cloning and expression of a murein hydrolase lipoprotein from Escherichia
RT coli.";
RL Mol. Microbiol. 16:761-768(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7789526; DOI=10.1016/0014-5793(95)00505-4;
RA Dijkstra A.J., Hermann F., Keck W.;
RT "Cloning and controlled overexpression of the gene encoding the 35 kDa
RT soluble lytic transglycosylase from Escherichia coli.";
RL FEBS Lett. 366:115-118(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
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 PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-91.
RX PubMed=3553176; DOI=10.1016/s0021-9258(18)45594-9;
RA Yamada M., Saier M.H. Jr.;
RT "Glucitol-specific enzymes of the phosphotransferase system in Escherichia
RT coli. Nucleotide sequence of the gut operon.";
RL J. Biol. Chem. 262:5455-5463(1987).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 42-361.
RX PubMed=9761817; DOI=10.1107/s0907444997010330;
RA van Asselt E.J., Perrakis A., Kalk K.H., Lamzin V.S., Dijkstra B.W.;
RT "Accelerated X-ray structure elucidation of a 36 kDa
RT muramidase/transglycosylase using wARP.";
RL Acta Crystallogr. D 54:58-73(1998).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 40-361.
RX PubMed=10570954; DOI=10.1016/s0014-5793(99)01198-9;
RA van Asselt E.J., Dijkstra B.W.;
RT "Binding of calcium in the EF-hand of Escherichia coli lytic
RT transglycosylase Slt35 is important for stability.";
RL FEBS Lett. 458:429-435(1999).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 40-361.
RX PubMed=10545329; DOI=10.1016/s0969-2126(00)80051-9;
RA van Asselt E.J., Dijkstra A.J., Kalk K.H., Takacs B., Keck W.,
RA Dijkstra B.W.;
RT "Crystal structure of Escherichia coli lytic transglycosylase Slt35 reveals
RT a lysozyme-like catalytic domain with an EF-hand.";
RL Structure 7:1167-1180(1999).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.97 ANGSTROMS) OF 40-361.
RX PubMed=10684641; DOI=10.1021/bi992161p;
RA van Asselt E.J., Kalk K.H., Dijkstra B.W.;
RT "Crystallographic studies of the interactions of Escherichia coli lytic
RT transglycosylase Slt35 with peptidoglycan.";
RL Biochemistry 39:1924-1934(2000).
CC -!- FUNCTION: Murein-degrading enzyme. Catalyzes the cleavage of the
CC glycosidic bonds between N-acetylmuramic acid and N-acetylglucosamine
CC residues in peptidoglycan. May play a role in recycling of muropeptides
CC during cell elongation and/or cell division.
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 -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane; Lipid-anchor; Periplasmic
CC side.
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DR EMBL; U18785; AAB60060.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75743.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16563.1; -; Genomic_DNA.
DR EMBL; J02708; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A65050; A65050.
DR RefSeq; NP_417181.1; NC_000913.3.
DR RefSeq; WP_001295177.1; NZ_LN832404.1.
DR PDB; 1D0K; X-ray; 2.02 A; A=40-361.
DR PDB; 1D0L; X-ray; 1.97 A; A=40-361.
DR PDB; 1D0M; X-ray; 2.47 A; A=40-361.
DR PDB; 1LTM; X-ray; 1.70 A; A=42-361.
DR PDB; 1QDR; X-ray; 2.10 A; A=40-361.
DR PDB; 1QDT; X-ray; 2.10 A; A=40-361.
DR PDB; 1QUS; X-ray; 1.70 A; A=40-361.
DR PDB; 1QUT; X-ray; 2.44 A; A=40-361.
DR PDBsum; 1D0K; -.
DR PDBsum; 1D0L; -.
DR PDBsum; 1D0M; -.
DR PDBsum; 1LTM; -.
DR PDBsum; 1QDR; -.
DR PDBsum; 1QDT; -.
DR PDBsum; 1QUS; -.
DR PDBsum; 1QUT; -.
DR AlphaFoldDB; P41052; -.
DR SMR; P41052; -.
DR BioGRID; 4262079; 390.
DR BioGRID; 851516; 9.
DR DIP; DIP-10221N; -.
DR IntAct; P41052; 10.
DR STRING; 511145.b2701; -.
DR BindingDB; P41052; -.
DR ChEMBL; CHEMBL2046262; -.
DR DrugBank; DB02595; (2R,3S,5S)-2-(Hydroxymethyl)-5-[(2-sulfoethyl)carbamoyl]-3-pyrrolidiniumyl 2-acetamido-2-deoxy-4-O-sulfo-beta-D-glucopyranoside.
DR DrugBank; DB03709; Bicine.
DR CAZy; GH103; Glycoside Hydrolase Family 103.
DR jPOST; P41052; -.
DR PaxDb; 511145-b2701; -.
DR EnsemblBacteria; AAC75743; AAC75743; b2701.
DR GeneID; 75172783; -.
DR GeneID; 947184; -.
DR KEGG; ecj:JW2671; -.
DR KEGG; eco:b2701; -.
DR PATRIC; fig|511145.12.peg.2792; -.
DR EchoBASE; EB2561; -.
DR eggNOG; COG2951; Bacteria.
DR HOGENOM; CLU_035402_1_0_6; -.
DR InParanoid; P41052; -.
DR OMA; IYGRYMG; -.
DR OrthoDB; 9772911at2; -.
DR PhylomeDB; P41052; -.
DR BioCyc; EcoCyc:G7410-MONOMER; -.
DR BioCyc; MetaCyc:G7410-MONOMER; -.
DR EvolutionaryTrace; P41052; -.
DR PRO; PR:P41052; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IDA:EcoCyc.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; TAS:EcoCyc.
DR GO; GO:0005509; F:calcium ion binding; IDA:EcoCyc.
DR GO; GO:0008932; F:lytic endotransglycosylase activity; IDA:EcoCyc.
DR GO; GO:0008933; F:lytic transglycosylase activity; IDA:EcoCyc.
DR GO; GO:0031402; F:sodium ion binding; IDA:EcoCyc.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009253; P:peptidoglycan catabolic process; IDA:EcoCyc.
DR CDD; cd13399; Slt35-like; 1.
DR Gene3D; 1.10.530.10; -; 1.
DR Gene3D; 1.10.8.350; Bacterial muramidase; 1.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR011757; Lytic_transglycosylase_MltB.
DR InterPro; IPR043426; MltB-like.
DR InterPro; IPR031304; SLT_2.
DR NCBIfam; TIGR02282; MltB; 1.
DR PANTHER; PTHR30163; MEMBRANE-BOUND LYTIC MUREIN TRANSGLYCOSYLASE B; 1.
DR PANTHER; PTHR30163:SF8; MEMBRANE-BOUND LYTIC MUREIN TRANSGLYCOSYLASE B; 1.
DR Pfam; PF13406; SLT_2; 1.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell outer membrane; Cell wall biogenesis/degradation;
KW Lipoprotein; Lyase; Membrane; Palmitate; Reference proteome; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000305"
FT CHAIN 19..361
FT /note="Membrane-bound lytic murein transglycosylase B"
FT /id="PRO_0000032784"
FT ACT_SITE 162
FT LIPID 19
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000305"
FT LIPID 19
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000305"
FT TURN 53..56
FT /evidence="ECO:0007829|PDB:1LTM"
FT HELIX 58..71
FT /evidence="ECO:0007829|PDB:1LTM"
FT HELIX 75..82
FT /evidence="ECO:0007829|PDB:1LTM"
FT HELIX 89..95
FT /evidence="ECO:0007829|PDB:1LTM"
FT HELIX 113..118
FT /evidence="ECO:0007829|PDB:1LTM"
FT TURN 119..121
FT /evidence="ECO:0007829|PDB:1LTM"
FT HELIX 124..136
FT /evidence="ECO:0007829|PDB:1LTM"
FT HELIX 138..148
FT /evidence="ECO:0007829|PDB:1LTM"
FT HELIX 152..163
FT /evidence="ECO:0007829|PDB:1LTM"
FT TURN 164..167
FT /evidence="ECO:0007829|PDB:1LTM"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:1D0M"
FT HELIX 174..183
FT /evidence="ECO:0007829|PDB:1LTM"
FT HELIX 186..188
FT /evidence="ECO:0007829|PDB:1LTM"
FT HELIX 189..205
FT /evidence="ECO:0007829|PDB:1LTM"
FT TURN 210..212
FT /evidence="ECO:0007829|PDB:1LTM"
FT TURN 222..225
FT /evidence="ECO:0007829|PDB:1LTM"
FT HELIX 228..234
FT /evidence="ECO:0007829|PDB:1LTM"
FT STRAND 239..242
FT /evidence="ECO:0007829|PDB:1LTM"
FT HELIX 249..262
FT /evidence="ECO:0007829|PDB:1LTM"
FT STRAND 271..277
FT /evidence="ECO:0007829|PDB:1LTM"
FT STRAND 280..282
FT /evidence="ECO:0007829|PDB:1D0L"
FT STRAND 285..291
FT /evidence="ECO:0007829|PDB:1LTM"
FT HELIX 292..297
FT /evidence="ECO:0007829|PDB:1LTM"
FT STRAND 301..304
FT /evidence="ECO:0007829|PDB:1LTM"
FT STRAND 311..318
FT /evidence="ECO:0007829|PDB:1LTM"
FT STRAND 320..328
FT /evidence="ECO:0007829|PDB:1LTM"
FT HELIX 330..336
FT /evidence="ECO:0007829|PDB:1LTM"
FT HELIX 342..360
FT /evidence="ECO:0007829|PDB:1LTM"
SQ SEQUENCE 361 AA; 40256 MW; 7E98F040504F75F9 CRC64;
MFKRRYVTLL PLFVLLAACS SKPKPTETDT TTGTPSGGFL LEPQHNVMQM GGDFANNPNA
QQFIDKMVNK HGFDRQQLQE ILSQAKRLDS VLRLMDNQAP TTSVKPPSGP NGAWLRYRKK
FITPDNVQNG VVFWNQYEDA LNRAWQVYGV PPEIIVGIIG VETRWGRVMG KTRILDALAT
LSFNYPRRAE YFSGELETFL LMARDEQDDP LNLKGSFAGA MGYGQFMPSS YKQYAVDFSG
DGHINLWDPV DAIGSVANYF KAHGWVKGDQ VAVMANGQAP GLPNGFKTKY SISQLAAAGL
TPQQPLGNHQ QASLLRLDVG TGYQYWYGLP NFYTITRYNH STHYAMAVWQ LGQAVALARV
Q
//
