MLTF_SHEDO
ID MLTF_SHEDO Reviewed; 494 AA.
AC Q12PR8;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 25-MAY-2022, entry version 87.
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=Sden_1272;
OS Shewanella denitrificans (strain OS217 / ATCC BAA-1090 / DSM 15013).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=318161;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OS217 / ATCC BAA-1090 / DSM 15013;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of Shewanella denitrificans OS217.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP000302; ABE54558.1; -; Genomic_DNA.
DR RefSeq; WP_011495717.1; NC_007954.1.
DR AlphaFoldDB; Q12PR8; -.
DR SMR; Q12PR8; -.
DR STRING; 318161.Sden_1272; -.
DR CAZy; GH23; Glycoside Hydrolase Family 23.
DR EnsemblBacteria; ABE54558; ABE54558; Sden_1272.
DR KEGG; sdn:Sden_1272; -.
DR eggNOG; COG4623; Bacteria.
DR HOGENOM; CLU_027494_0_1_6; -.
DR OMA; YYDILTW; -.
DR OrthoDB; 1444566at2; -.
DR Proteomes; UP000001982; 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 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; 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; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Cell outer membrane; Cell wall biogenesis/degradation; Lyase; Membrane;
KW Reference proteome; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02016"
FT CHAIN 21..494
FT /note="Membrane-bound lytic murein transglycosylase F"
FT /id="PRO_5000114486"
FT REGION 21..259
FT /note="Non-LT domain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02016"
FT REGION 260..494
FT /note="LT domain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02016"
FT REGION 473..494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 304
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02016"
SQ SEQUENCE 494 AA; 56073 MW; 8D52CD1C87900C48 CRC64;
MIKYLYVILL GLLLSGCQPA EVVEIEASPK AQKRTVLKVG TLYGPQIYVN NSQGETGFDY
EMANRFADYL GVSLEMIPFT DRKQLFKALK DNDIDIIAAG IAKTPGRGEQ FKMGPTLYKV
NQVLVYREGT PEPKDIGTLS GEITVMSNSS SVNTLTQLQK DYPELLWNQV NDKDNEELFA
LIAKGELNYT ISDSNSLLIN QRFLPELRAG MILEEKIEVV WLLPPKNSDK LMSQLLAFWH
NEQRAGTLEH LNEKYFGHVK RFDYVDTRAF IRAIDNVLPA YRSLFETYSG ELDWRKLAAA
SYQESHWNPN ARSKTGVRGM MMLTQPTASY VGVSDRTDAE QSIRGGAIYL KDMIERLPES
ISDSQRIWFA LAAYNIGMGH VEDARRLAVS MDMDPDAWRD VKKVLPLLQQ RKYYKQTRYG
YARGSQAVHY VDSIRRYYDT LVWVDNQTKK MEVIEAPVEI LADKVDANDN IKQSLASDSK
TNNTLKPKLG AGQP
