A7MGZ5 (MLTF_CROS8) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Membrane-bound lytic murein transglycosylase F
EC=4.2.2.n1

Alternative name(s):
Murein lyase F

Gene names

Name:	mltF
Ordered Locus Names:	ESA_00703

Organism

Cronobacter sakazakii (strain ATCC BAA-894) (Enterobacter sakazakii) [Complete proteome] [HAMAP]

Taxonomic identifier

290339 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Cronobacter › Cronobacter sakazakii

Protein attributes

Sequence length	519 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella By similarity. HAMAP-Rule MF_02016
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. HAMAP-Rule MF_02016
Subcellular location	Cell outer membrane; Peripheral membrane protein. Note: Attached to the inner leaflet of the outer membrane By similarity. HAMAP-Rule MF_02016
Domain	The N-terminal domain does not have lytic activity and probably modulates enzymatic activity. The C-terminal domain is the catalytic active domain By similarity. HAMAP-Rule MF_02016
Sequence similarities	In the N-terminal section; belongs to the bacterial solute-binding protein 3 family. In the C-terminal section; belongs to the transglycosylase Slt family.

Ontologies

Keywords
Biological process	Cell wall biogenesis/degradation
Cellular component	Cell membrane Cell outer membrane Membrane
Domain	Signal
Molecular function	Lyase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	cell wall macromolecule catabolic process Inferred from electronic annotation. Source: HAMAP
Cellular_component	cell outer membrane Inferred from electronic annotation. Source: UniProtKB-SubCell outer membrane-bounded periplasmic space Inferred from electronic annotation. Source: InterPro plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	carbon-oxygen lyase activity, acting on polysaccharides Inferred from electronic annotation. Source: EC lytic transglycosylase activity Inferred from electronic annotation. Source: HAMAP transporter activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 32	32	Potential
	Chain	33 – 519	487	Membrane-bound lytic murein transglycosylase F HAMAP-Rule MF_02016		PRO_0000353936
Regions
	Region	33 – 269	237	Non-LT domain By similarity
	Region	270 – 519	250	LT domain By similarity
Sites
	Active site	314	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	A7MGZ5 [UniParc]. Last modified October 2, 2007. Version 1. Checksum: 818FB065D8B03B13	FASTA	519	57,617
	10 20 30 40 50 60 MKKLKLNYLL IGVVTLLLAV ALWPAIPWSG KADNRIAAIQ ARGVLRVSTI ATPLTMYRAG 70 80 90 100 110 120 DTMSGLDYEL SQAFADYLGV KLKITVRQNI SQLFDDLDNN DADLLAAGLV YNEARSQHYQ 130 140 150 160 170 180 AGPIYYSVSQ QMVYRVGSLR PRSLASIKEG QLTIAPGHVA QSELEQLKAS KYPDLTWRVD 190 200 210 220 230 240 PKLSSNELML QVAQGTLDYT IADSVAISLF QRVHPQLAVA LDLSDEQPVT WFSRRSSDNS 250 260 270 280 290 300 LSAALLDFFN QINEDGTLAR LEEKYLGHGN DFDYVDTRSF LRAVDSVLPE LQPLFEKYAT 310 320 330 340 350 360 DIDWRLLAAI SYQESHWDSQ ATSPTGVRGL MMLTRNTAQS LGLTDRLDAE QSISGGARYL 370 380 390 400 410 420 KDMMSKVPES VPEEERIWFA LAAYNMGYAH MLDARALTAK QKGNPDSWSD VKQRLPLLSQ 430 440 450 460 470 480 RPYYSKLTYG YARGHEAYAY VENIRKYQIS LVGYLLEKEK QAAAAAQPKL VQSYPTNITP 490 500 510 QGLFPSPFSS LPLGPFSQAG AGGKTHSALP NTLSPVSPR

References

[1]

"Genome sequence of Cronobacter sakazakii BAA-894 and comparative genomic hybridization analysis with other Cronobacter species." Kucerova E., Clifton S.W., Xia X.Q., Long F., Porwollik S., Fulton L., Fronick C., Minx P., Kyung K., Warren W., Fulton R., Feng D., Wollam A., Shah N., Bhonagiri V., Nash W.E., Hallsworth-Pepin K., Wilson R.K., McClelland M., Forsythe S.J. PLoS ONE 5:E9556-E9556(2010) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-894.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000783 Genomic DNA. Translation: ABU75981.1.
RefSeq	YP_001436817.1. NC_009778.1.
3D structure databases
ProteinModelPortal	A7MGZ5.
ModBase	Search...
Protein-protein interaction databases
STRING	290339.ESA_00703.
Protein family/group databases
CAZy	GH23. Glycoside Hydrolase Family 23.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABU75981; ABU75981; ESA_00703.
GeneID	5548883.
KEGG	esa:ESA_00703.
PATRIC	20393627. VBICroSak107175_0621.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG4623.
HOGENOM	HOG000218316.
OMA	MMLTRNT.
ProtClustDB	PRK10859.
Enzyme and pathway databases
BioCyc	CSAK290339:GJ80-697-MONOMER.
Family and domain databases
HAMAP	MF_02016. MltF.
InterPro	IPR023346. Lysozyme-like_dom. IPR008258. Lytic_TGlycosylase-like_cat. IPR023703. MltF. IPR001638. SBP_bac_3. [Graphical view]
Pfam	PF00497. SBP_bac_3. 1 hit. PF01464. SLT. 1 hit. [Graphical view]
SMART	SM00062. PBPb. 1 hit. [Graphical view]
SUPFAM	SSF53955. SSF53955. 1 hit.
PROSITE	PS00922. TRANSGLYCOSYLASE. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MLTF_CROS8

Accession

Primary (citable) accession number: A7MGZ5

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 25, 2008
Last sequence update:	October 2, 2007
Last modified:	May 1, 2013
This is version 36 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program