MLTF_PSEAB
ID MLTF_PSEAB Reviewed; 489 AA.
AC Q02RN8;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 81.
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=PA14_15720;
OS Pseudomonas aeruginosa (strain UCBPP-PA14).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCBPP-PA14;
RX PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L., Grills G.,
RA Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT combinatorial.";
RL Genome Biol. 7:R90.1-R90.14(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=ABJ12999.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000438; ABJ12999.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_016254283.1; NZ_CP034244.1.
DR AlphaFoldDB; Q02RN8; -.
DR SMR; Q02RN8; -.
DR CAZy; GH23; Glycoside Hydrolase Family 23.
DR PRIDE; Q02RN8; -.
DR EnsemblBacteria; ABJ12999; ABJ12999; PA14_15720.
DR KEGG; pau:PA14_15720; -.
DR HOGENOM; CLU_027494_0_1_6; -.
DR BioCyc; PAER208963:G1G74-1294-MON; -.
DR Proteomes; UP000000653; 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..32
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02016"
FT CHAIN 33..489
FT /note="Membrane-bound lytic murein transglycosylase F"
FT /id="PRO_0000353956"
FT REGION 33..268
FT /note="Non-LT domain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02016"
FT REGION 269..489
FT /note="LT domain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02016"
FT REGION 466..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 315
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02016"
SQ SEQUENCE 489 AA; 55111 MW; 7DD1338270FD3C3B CRC64;
MFALTAYRLR CAAWLLATGI FLLLAGCSEA KAPTALERVQ KEGVLRVITR NSPATYFQDR
NGETGFEYEL AKRFAERLGV ELKIETADNL DDLYAQLSRE GGPALAAAGL TPGREDDASV
RYSHTYLDVT PQIIYRNGQQ RPTRPEDLVG KRIMVLKGSS HAEQLAELKK QYPELKYEES
DAVEVVDLLR MVDVGDIDLT LVDSNELAMN QVYFPNVRVA FDFGEARGLA WALPGGDDSL
MNEVNAFLDQ AKKEGLLQRL KDRYYGHVDV LGYVGAYTFA QHLQQRLPRY ESHFKQSGKQ
LDTDWRLLAA IGYQESLWQP GATSKTGVRG LMMLTNRTAQ AMGVSNRLDP KQSIQGGSKY
FVQIRSELPE SIKEPDRSWF ALAAYNIGGA HLEDARKMAE KEGLNPNKWL DVKKMLPRLA
QKQWYAKTRY GYARGGETVH FVQNVRRYYD ILTWVTQPQM EGSQIAESGL HLPGVNKTRP
EEDSGDEKL
