MLTF_YERE8
ID MLTF_YERE8 Reviewed; 486 AA.
AC A1JKM2;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 25-MAY-2022, entry version 80.
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=YE1031;
OS Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 /
OS 8081).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=393305;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 13174 / 8081;
RX PubMed=17173484; DOI=10.1371/journal.pgen.0020206;
RA Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L.,
RA Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T.,
RA Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S.,
RA Sanders M., Whitehead S., Quail M.A., Dougan G., Parkhill J.,
RA Prentice M.B.;
RT "The complete genome sequence and comparative genome analysis of the high
RT pathogenicity Yersinia enterocolitica strain 8081.";
RL PLoS Genet. 2:2039-2051(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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AM286415; CAL11130.1; -; Genomic_DNA.
DR RefSeq; WP_005172712.1; NC_008800.1.
DR RefSeq; YP_001005365.1; NC_008800.1.
DR AlphaFoldDB; A1JKM2; -.
DR SMR; A1JKM2; -.
DR STRING; 393305.YE1031; -.
DR CAZy; GH23; Glycoside Hydrolase Family 23.
DR EnsemblBacteria; CAL11130; CAL11130; YE1031.
DR KEGG; yen:YE1031; -.
DR PATRIC; fig|393305.7.peg.1127; -.
DR eggNOG; COG4623; Bacteria.
DR HOGENOM; CLU_027494_0_1_6; -.
DR OMA; YYDILTW; -.
DR Proteomes; UP000000642; 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..21
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02016"
FT CHAIN 22..486
FT /note="Membrane-bound lytic murein transglycosylase F"
FT /id="PRO_5000200984"
FT REGION 22..268
FT /note="Non-LT domain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02016"
FT REGION 269..486
FT /note="LT domain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02016"
FT ACT_SITE 313
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02016"
SQ SEQUENCE 486 AA; 54685 MW; 01EE4E0DB695974B CRC64;
MTRIKLNYFV IGVVALLLAL ALWPNIPWRN GQEGQLDRIK ARGELRVSTI SSPLIYSTGK
DGPSGFDYEL AKRFADYLGV KLVMTPHHNI NDLFDTLDSD DADMIAAGLI YNSERLKRAR
TGPAYYSVSQ QLVYRLGSPR PKSFSDLKGQ LIVASGSAHM TTLKQLKQTK YPDLNWGSSV
DRSGKELLEQ VADGKLDYTL GDSVTIALLQ RIHPQLAVAF DVTDEEPVTW YFQQSHDDSL
YAAMLDFYSE MVEDGSLARL EEKYLGHVGS FDYVDTKTFL SAIDNVLPSF RPLFEKHAGE
IDWRLLAAIA YQESHWNPQA TSPTGVRGLM MLTRATASGL GVKDRVDPEE SIRGGSVYLQ
RLMQKVPDTI PEDERIWFAL AAYNLGYGHM LDARKLTKNQ NGNPDSWVDV KMRLPMLSQK
RYYPSTTYGY ARGHEAYNYV ENIRRYQVSL VGYLQEKEKK AAQHAAIEAE LGKAYPVVGP
GWSINN
