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Protein

Soluble lytic murein transglycosylase

Gene

slt

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

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 (By similarity).By similarity

Catalytic activityi

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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei505PROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Cell wall biogenesis/degradation

Protein family/group databases

CAZyiGH23. Glycoside Hydrolase Family 23.

Names & Taxonomyi

Protein namesi
Recommended name:
Soluble lytic murein transglycosylase (EC:4.2.2.n1)
Alternative name(s):
Peptidoglycan lytic exotransglycosylase
Slt70
Gene namesi
Name:slt
Ordered Locus Names:STM4582
OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Taxonomic identifieri99287 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeSalmonella
Proteomesi
  • UP000001014 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 27Sequence analysisAdd BLAST27
ChainiPRO_000003277928 – 645Soluble lytic murein transglycosylaseAdd BLAST618

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi133 ↔ 166By similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP39434.
PRIDEiP39434.

Interactioni

Protein-protein interaction databases

STRINGi99287.STM4582.

Structurei

3D structure databases

ProteinModelPortaliP39434.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni492 – 582Slt-type domainAdd BLAST91

Sequence similaritiesi

Belongs to the transglycosylase Slt family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4107SC1. Bacteria.
COG0741. LUCA.
HOGENOMiHOG000275388.
KOiK08309.
OMAiVDWHERY.
PhylomeDBiP39434.

Family and domain databases

Gene3Di1.10.1240.20. 1 hit.
1.25.20.10. 1 hit.
InterProiIPR023346. Lysozyme-like_dom.
IPR016026. Lytic_TGlyclase_suprhlx_U/L.
IPR012289. Lytic_TGlycosylase_superhlx_L.
IPR008939. Lytic_TGlycosylase_superhlx_U.
IPR000189. Transglyc_AS.
IPR008258. Transglycosylase_SLT_dom_1.
[Graphical view]
PfamiPF01464. SLT. 1 hit.
PF14718. SLT_L. 1 hit.
[Graphical view]
SUPFAMiSSF48435. SSF48435. 1 hit.
SSF53955. SSF53955. 1 hit.
PROSITEiPS00922. TRANSGLYCOSYLASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P39434-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDRAKPFVWR LVAASVCLLT FCHLARADSL EEQRNRYAQI KQAWDNRQMD
60 70 80 90 100
VVEQMMPGLK DYPLYPYLEY RKITDDLMNQ PAIAVTQFVR ANPTLPPART
110 120 130 140 150
LQSRFVNELA RREDWRGLLA FSPEKPGTTE AQCNYYYAKW STGQTEAAWQ
160 170 180 190 200
GAKDLWLTGK SQPNACDKLF SVWRASGKQD PLAYLERIRL AMKAGNTGLV
210 220 230 240 250
TVLAGQMPAE YQTIASAIIT LANDPNNVLI FARTTGATDF TRQMAEVAFA
260 270 280 290 300
SVARQDAENA RLMIPSLVQA QKLNEEQTQA LRDIVAWRLM GNDVTDAQAK
310 320 330 340 350
WRDDAIMRSQ STSLIERRVR MALGMGDRRG LNTWLARLPM EAKEKDEWRY
360 370 380 390 400
WQADLLLERG RDAEAKEILH ALMQKRGFYP MVAAQRLGEE YTLKIDKAPA
410 420 430 440 450
NVNSALTQGP EMARVRELMY WNLDNTARSE WANLVKSRSK SEQAQLARYA
460 470 480 490 500
FNQHWWDLSV QATIAGKLWD HLEERFPLAY NDLFTRYTRG KDISQSYAMA
510 520 530 540 550
IARQESAWNP KVKSPVGASG LMQIMPGTAT HTVKMFSIPD YRGPGQLLEP
560 570 580 590 600
ETNINIGTSY LQYVYQQFGN NRIFASAAYN AGPGRVRTWL GNSAGRIDAV
610 620 630 640
AFVESIPFSE TRGYVKNVLA YDAYYRHFMG QKEALMSDSE WQRRY
Length:645
Mass (Da):73,620
Last modified:December 19, 2001 - v2
Checksum:i4980ED7426958D7C
GO

Sequence cautioni

The sequence AAL23397 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE006468 Genomic DNA. Translation: AAL23397.1. Different initiation.
RefSeqiNP_463438.2. NC_003197.1.
WP_000373268.1. NC_003197.1.

Genome annotation databases

EnsemblBacteriaiAAL23397; AAL23397; STM4582.
GeneIDi1256108.
KEGGistm:STM4582.
PATRICi32388131. VBISalEnt20916_4825.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE006468 Genomic DNA. Translation: AAL23397.1. Different initiation.
RefSeqiNP_463438.2. NC_003197.1.
WP_000373268.1. NC_003197.1.

3D structure databases

ProteinModelPortaliP39434.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi99287.STM4582.

Protein family/group databases

CAZyiGH23. Glycoside Hydrolase Family 23.

Proteomic databases

PaxDbiP39434.
PRIDEiP39434.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAL23397; AAL23397; STM4582.
GeneIDi1256108.
KEGGistm:STM4582.
PATRICi32388131. VBISalEnt20916_4825.

Phylogenomic databases

eggNOGiENOG4107SC1. Bacteria.
COG0741. LUCA.
HOGENOMiHOG000275388.
KOiK08309.
OMAiVDWHERY.
PhylomeDBiP39434.

Family and domain databases

Gene3Di1.10.1240.20. 1 hit.
1.25.20.10. 1 hit.
InterProiIPR023346. Lysozyme-like_dom.
IPR016026. Lytic_TGlyclase_suprhlx_U/L.
IPR012289. Lytic_TGlycosylase_superhlx_L.
IPR008939. Lytic_TGlycosylase_superhlx_U.
IPR000189. Transglyc_AS.
IPR008258. Transglycosylase_SLT_dom_1.
[Graphical view]
PfamiPF01464. SLT. 1 hit.
PF14718. SLT_L. 1 hit.
[Graphical view]
SUPFAMiSSF48435. SSF48435. 1 hit.
SSF53955. SSF53955. 1 hit.
PROSITEiPS00922. TRANSGLYCOSYLASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSLT_SALTY
AccessioniPrimary (citable) accession number: P39434
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: December 19, 2001
Last modified: November 30, 2016
This is version 112 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.