P0AGC3 (SLT_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Soluble lytic murein transglycosylase
EC=4.2.2.n1

Alternative name(s):
Exomuramidase
Peptidoglycan lytic exotransglycosylase
Slt70

Gene names

Name:	slt
Synonyms:	sltY
Ordered Locus Names:	b4392, JW4355

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	645 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Murein-degrading enzyme. Catalyzes the cleavage of the glycosidic bonds between N-acetylmuramic acid and N-acetylglucosamine residues in peptidoglycan. May play a role in recycling of muropeptides during cell elongation and/or cell division.
Catalytic activity	Exolytic cleavage of the (1->4)-beta-glycosidic linkage between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc) residues in peptidoglycan, from either the reducing or the non-reducing ends of the peptidoglycan chains, with concomitant formation of a 1,6-anhydrobond in the MurNAc residue.
Subcellular location	Periplasm. Note: Tightly associated with the murein sacculus.
Sequence similarities	Belongs to the transglycosylase Slt family.
Sequence caution	The sequence AAA97288.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	Cell wall biogenesis/degradation
Cellular component	Periplasm
Domain	Signal
Molecular function	Lyase
PTM	Disulfide bond
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	peptidoglycan metabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	membrane Inferred from electronic annotation. Source: InterPro outer membrane-bounded periplasmic space Inferred from direct assay Ref.1. Source: EcoliWiki
Molecular_function	carbon-oxygen lyase activity, acting on polysaccharides Inferred from electronic annotation. Source: EC hydrolase activity, hydrolyzing O-glycosyl compounds Inferred from electronic annotation. Source: InterPro lytic transglycosylase activity Inferred from direct assay Ref.1. Source: EcoliWiki
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 27

27

Ref.1

Chain

28 – 645

618

Soluble lytic murein transglycosylase

PRO_0000032778

Regions

Region

492 – 582

91

Slt-type domain

Sites

Active site

505

1

Amino acid modifications

Disulfide bond

133 ↔ 166

Experimental info

Mutagenesis

505

1

E → Q: Inactivates the enzyme.

Sequence conflict

583

1

P → L in AAA24634. Ref.1

Secondary structure

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645

Helix Strand Turn

Details...

Helix

30 – 45

16

Helix

49 – 55

7

Helix

57 – 59

3

Helix

65 – 75

11

Helix

76 – 79

4

Helix

82 – 91

10

Helix

96 – 111

16

Helix

115 – 121

7

Helix

129 – 141

13

Helix

145 – 156

12

Helix

166 – 175

10

Helix

181 – 193

13

Helix

197 – 205

9

Helix

209 – 211

3

Helix

212 – 223

12

Helix

225 – 227

3

Helix

228 – 234

7

Helix

239 – 255

17

Helix

257 – 270

14

Helix

275 – 287

13

Beta strand

291 – 293

3

Helix

296 – 307

12

Helix

312 – 324

13

Helix

328 – 337

10

Helix

342 – 344

3

Helix

346 – 358

13

Helix

362 – 373

12

Helix

378 – 386

9

Helix

405 – 408

4

Helix

410 – 420

11

Helix

424 – 435

12

Helix

440 – 452

13

Helix

456 – 465

10

Helix

472 – 475

4

Helix

481 – 488

8

Beta strand

491 – 493

3

Helix

495 – 506

12

Turn

520 – 523

4

Helix

526 – 536

11

Helix

544 – 548

5

Helix

550 – 567

18

Turn

568 – 570

3

Helix

572 – 581

10

Helix

583 – 593

11

Helix

599 – 605

7

Helix

609 – 628

20

Helix

638 – 642

5

Sequences

	Sequence		Length	Mass (Da)
	P0AGC3 [UniParc]. Last modified December 20, 2005. Version 1. Checksum: F8B0115376E8A947	FASTA	645	73,353
	10 20 30 40 50 60 MEKAKQVTWR LLAAGVCLLT VSSVARADSL DEQRSRYAQI KQAWDNRQMD VVEQMMPGLK 70 80 90 100 110 120 DYPLYPYLEY RQITDDLMNQ PAVTVTNFVR ANPTLPPART LQSRFVNELA RREDWRGLLA 130 140 150 160 170 180 FSPEKPGTTE AQCNYYYAKW NTGQSEEAWQ GAKELWLTGK SQPNACDKLF SVWRASGKQD 190 200 210 220 230 240 PLAYLERIRL AMKAGNTGLV TVLAGQMPAD YQTIASAIIS LANNPNTVLT FARTTGATDF 250 260 270 280 290 300 TRQMAAVAFA SVARQDAENA RLMIPSLAQA QQLNEDQIQE LRDIVAWRLM GNDVTDEQAK 310 320 330 340 350 360 WRDDAIMRSQ STSLIERRVR MALGTGDRRG LNTWLARLPM EAKEKDEWRY WQADLLLERG 370 380 390 400 410 420 REAEAKEILH QLMQQRGFYP MVAAQRIGEE YELKIDKAPQ NVDSALTQGP EMARVRELMY 430 440 450 460 470 480 WNLDNTARSE WANLVKSKSK TEQAQLARYA FNNQWWDLSV QATIAGKLWD HLEERFPLAY 490 500 510 520 530 540 NDLFKRYTSG KEIPQSYAMA IARQESAWNP KVKSPVGASG LMQIMPGTAT HTVKMFSIPG 550 560 570 580 590 600 YSSPGQLLDP ETNINIGTSY LQYVYQQFGN NRIFSSAAYN AGPGRVRTWL GNSAGRIDAV 610 620 630 640 AFVESIPFSE TRGYVKNVLA YDAYYRYFMG DKPTLMSATE WGRRY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Murein-metabolizing enzymes from Escherichia coli: sequence analysis and controlled overexpression of the slt gene, which encodes the soluble lytic transglycosylase." Engel H., Kazemier B., Keck W. J. Bacteriol. 173:6773-6782(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 28-41.
[2]	"Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes." Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R. Nucleic Acids Res. 23:2105-2119(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"DNA sequence of the E. coli trpR gene and prediction of the amino acid sequence of Trp repressor." Singleton C.K., Roeder W.D., Bogosian G., Somerville R.L., Weith H.L. Nucleic Acids Res. 8:1551-1560(1980) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 549-639.
[6]	"Nucleotide sequence and expression of Escherichia coli trpR, the structural gene for the trp aporepressor." Gunsalus R.P., Yanofsky C. Proc. Natl. Acad. Sci. U.S.A. 77:7117-7121(1980) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 640-645.
[7]	"Molecular cloning, overexpression and mapping of the slt gene encoding the soluble lytic transglycosylase of Escherichia coli." Betzner A.S., Keck W. Mol. Gen. Genet. 219:489-491(1989) [PubMed] [Europe PMC] [Abstract] Cited for: GENE MAPPING.
[8]	"Escherichia coli proteome analysis using the gene-protein database." VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C. Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY 2D-GEL.
[9]	"Crystallization of the soluble lytic transglycosylase from Escherichia coli K12." Rozeboom H.J., Dijkstra B.W., Engel H., Keck W. J. Mol. Biol. 212:557-559(1990) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS). Strain: K12.
[10]	"Doughnut-shaped structure of a bacterial muramidase revealed by X-ray crystallography." Thunnissen A.-M.W.H., Dijkstra A.J., Kalk K.H., Rozeboom H.J., Engel H., Keck W., Dijkstra B.W. Nature 367:750-753(1994) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
[11]	"Structure of the 70-kDa soluble lytic transglycosylase complexed with bulgecin A. Implications for the enzymatic mechanism." Thunnissen A.-M.W.H., Rozeboom H.J., Kalk K.H., Dijkstra B.W. Biochemistry 34:12729-12737(1995) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
[12]	"High resolution crystal structures of the Escherichia coli lytic transglycosylase Slt70 and its complex with a peptidoglycan fragment." van Asselt E.J., Thunnissen A.-M.W.H., Dijkstra B.W. J. Mol. Biol. 291:877-898(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M69185 Genomic DNA. Translation: AAA24634.1.
U14003 Genomic DNA. Translation: AAA97288.1. Different initiation.
U00096 Genomic DNA. Translation: AAC77345.2.
AP009048 Genomic DNA. Translation: BAE78381.1.
J01715 Genomic DNA. No translation available.

PIR

QQECW1. S56616.

RefSeq

NP_418809.4. NC_000913.2.
YP_492522.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1QSA	X-ray	1.65	A	28-645	[»]
1QTE	X-ray	1.90	A	28-645	[»]
1SLY	X-ray	2.80	A	28-645	[»]

ProteinModelPortal

P0AGC3.

SMR

P0AGC3. Positions 28-645.

ModBase

Search...

Protein-protein interaction databases

IntAct

P0AGC3. 5 interactions.

STRING

511145.b4392.

Protein family/group databases

CAZy

GH23. Glycoside Hydrolase Family 23.

Proteomic databases

PaxDb

P0AGC3.

PRIDE

P0AGC3.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC77345; AAC77345; b4392.
BAE78381; BAE78381; BAE78381.

GeneID

12931805.
948908.

KEGG

ecj:Y75_p4276.
eco:b4392.

PATRIC

32124402. VBIEscCol129921_4541.

Organism-specific databases

EchoBASE

EB0943.

EcoGene

EG10950. slt.

Phylogenomic databases

eggNOG

COG0741.

HOGENOM

HOG000275388.

KO

K08309.

OMA

RQESAFM.

ProtClustDB

PRK11619.

Enzyme and pathway databases

BioCyc

EcoCyc:EG10950-MONOMER.
ECOL316407:JW4355-MONOMER.
MetaCyc:EG10950-MONOMER.

Gene expression databases

Genevestigator

P0AGC3.

Family and domain databases

Gene3D

1.10.1240.20. 1 hit.
1.25.20.10. 1 hit.

InterPro

IPR023346. Lysozyme-like_dom.
IPR016026. Lytic_TGlyclase_suprhlx_U/L.
IPR008258. Lytic_TGlycosylase-like_cat.
IPR012289. Lytic_TGlycosylase_superhlx_L.
IPR008939. Lytic_TGlycosylase_superhlx_U.
IPR000189. Transglyc_AS.
[Graphical view]

Pfam

PF01464. SLT. 1 hit.
[Graphical view]

SUPFAM

SSF48435. Lytic_TGlycosylase_suprhlx_U/L. 1 hit.
SSF53955. SSF53955. 1 hit.

PROSITE

PS00922. TRANSGLYCOSYLASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P0AGC3.

Entry information

Entry name

SLT_ECOLI

Accession

Primary (citable) accession number: P0AGC3
Secondary accession number(s): P03810 , P76820, Q2M5S5, Q8XB18

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	December 20, 2005
Last modified:	May 1, 2013
This is version 77 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program