MLTF_PHOPR
ID MLTF_PHOPR Reviewed; 514 AA.
AC Q6LU25;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 96.
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=PBPRA0787;
OS Photobacterium profundum (strain SS9).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=298386;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1253 / SS9;
RX PubMed=15746425; DOI=10.1126/science.1103341;
RA Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., Lauro F.M.,
RA Cestaro A., Malacrida G., Simionati B., Cannata N., Romualdi C.,
RA Bartlett D.H., Valle G.;
RT "Life at depth: Photobacterium profundum genome sequence and expression
RT analysis.";
RL Science 307:1459-1461(2005).
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; CR378665; CAG19200.1; -; Genomic_DNA.
DR RefSeq; WP_011217542.1; NC_006370.1.
DR AlphaFoldDB; Q6LU25; -.
DR SMR; Q6LU25; -.
DR STRING; 298386.PBPRA0787; -.
DR CAZy; GH23; Glycoside Hydrolase Family 23.
DR EnsemblBacteria; CAG19200; CAG19200; PBPRA0787.
DR KEGG; ppr:PBPRA0787; -.
DR eggNOG; COG4623; Bacteria.
DR HOGENOM; CLU_027494_0_1_6; -.
DR OMA; YYDILTW; -.
DR Proteomes; UP000000593; Chromosome 1.
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 Reference proteome; Signal.
FT SIGNAL 1..30
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02016"
FT CHAIN 31..514
FT /note="Membrane-bound lytic murein transglycosylase F"
FT /id="PRO_0000353953"
FT REGION 31..271
FT /note="Non-LT domain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02016"
FT REGION 272..514
FT /note="LT domain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02016"
FT REGION 482..514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 316
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02016"
SQ SEQUENCE 514 AA; 58181 MW; EA02F8052335C654 CRC64;
MLSNNPLITK FRELFTVALV LALLSGCQWQ DDNLTDLEKI RESGVIRVGT LNNQLSYYIG
NDGPTGLDYE LAQRFAQKLG VKLEMQPMFT LSGLFPTLER GGIDVVAAGL TISKDRIENY
HAAPAYYYAS QIVVYKNGQW RPRKPADLAL NKGTLSVVKG SSHEKHLIKL KEIHPDLTWE
SIEETDSDEL LRLVAKGELD FTIADSVDVA LSQRIHPDVA IAMELTEDEP IAWFVNKSTD
DSLYALLIEF FGEIKQSGEL AQLEEKYFGH VGSFDYVDTR AFLRAIESKL PRWESLFKKY
SNEFDWRLIA ALSYQESHWN PQAVSPTGVR GMMMLTLPTA KSVGVKNRLD PEQSIRGGAE
YLRKMISRVP DSIESHEKVW FALASYNVGF GHMMDARRLT HKQGGNQDTW TDVKQRLPLL
RQRKYYQQSR YGYARGDEAL NYVENIRRYY QSIIGYEQAH SHDYDSDDVQ VVDGLQTITL
PPVPPRQANV DGSLNNEAAI SSAEKTIEDP GPSQ
