MLTF_PSEE4
ID MLTF_PSEE4 Reviewed; 485 AA.
AC Q1I5L3;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 2.
DT 25-MAY-2022, entry version 85.
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}; OrderedLocusNames=PSEEN4388;
OS Pseudomonas entomophila (strain L48).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=384676;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L48;
RX PubMed=16699499; DOI=10.1038/nbt1212;
RA Vodovar N., Vallenet D., Cruveiller S., Rouy Z., Barbe V., Acosta C.,
RA Cattolico L., Jubin C., Lajus A., Segurens B., Vacherie B., Wincker P.,
RA Weissenbach J., Lemaitre B., Medigue C., Boccard F.;
RT "Complete genome sequence of the entomopathogenic and metabolically
RT versatile soil bacterium Pseudomonas entomophila.";
RL Nat. Biotechnol. 24:673-679(2006).
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 {ECO:0000255|HAMAP-Rule:MF_02016}.
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 -!- SUBCELLULAR LOCATION: Cell outer membrane; Peripheral membrane protein.
CC Note=Attached to the inner leaflet of the outer membrane.
CC {ECO:0000255|HAMAP-Rule:MF_02016}.
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. {ECO:0000255|HAMAP-Rule:MF_02016}.
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=CAK17072.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CT573326; CAK17072.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_044488430.1; NC_008027.1.
DR AlphaFoldDB; Q1I5L3; -.
DR SMR; Q1I5L3; -.
DR STRING; 384676.PSEEN4388; -.
DR CAZy; GH23; Glycoside Hydrolase Family 23.
DR EnsemblBacteria; CAK17072; CAK17072; PSEEN4388.
DR KEGG; pen:PSEEN4388; -.
DR eggNOG; COG4623; Bacteria.
DR HOGENOM; CLU_027494_0_1_6; -.
DR OrthoDB; 1444566at2; -.
DR Proteomes; UP000000658; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016837; F:carbon-oxygen lyase activity, acting on polysaccharides; IEA:InterPro.
DR GO; GO:0008933; F:lytic transglycosylase activity; IEA:UniProtKB-UniRule.
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:0000270; P:peptidoglycan metabolic process; IEA:InterPro.
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 3: Inferred from homology;
KW Cell outer membrane; Cell wall biogenesis/degradation; Lyase; Membrane;
KW Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02016"
FT CHAIN 28..485
FT /note="Membrane-bound lytic murein transglycosylase F"
FT /id="PRO_0000353958"
FT REGION 28..267
FT /note="Non-LT domain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02016"
FT REGION 268..485
FT /note="LT domain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02016"
FT REGION 465..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 314
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02016"
SQ SEQUENCE 485 AA; 54842 MW; F3D964B79AC7D236 CRC64;
MFAHTAFRQR CARWLFATGL FLMLGACVEK PSTLERVKED GVLRVITRNS PATYFQDRNG
ETGFEYELVK RFADDLGVKL QIETADNLDE LFDQLGKPSG PVLAAAGLVS SERRGAQARF
SHPYLEVTPQ VIYRNGRSRP TNAKGLVGKK IMVLKGSSHA DQLAELKKQN PGLEYEESDA
VEVVDLLRMV DEGQIDLTLV DSNELAMNQV YFPNVRVAFD LGDTRDQRWA VAAGDDNSLL
NEINEFLDKS QKNGTLQRLK DRYYGHVDVL GYVGAYTFAQ HLQQRLPKYE KHFKATSKVE
QVDWRLLAAI GYQESMWQPE VTSKTGVRGL MMLTQRTAQA MGVSNRLDPK QSIQGGAKYF
MVVKDQLDDS IKEPDRTWFA LAAYNVGSGH LEDARTLAKR EGLNPNKWLD VKKMLPRLSQ
KQWYSKTKYG YARGGEPVHF VANIRRYYDI LTWVTQPQLE GQVAEGNLHV PGVNKDKPAE
QSPQM
