ID   MLTF_MANSM              Reviewed;         484 AA.
AC   Q65RJ5;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 2.
DT   25-MAY-2022, entry version 88.
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=MS1808;
OS   Mannheimia succiniciproducens (strain MBEL55E).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Basfia.
OX   NCBI_TaxID=221988;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MBEL55E;
RX   PubMed=15378067; DOI=10.1038/nbt1010;
RA   Hong S.H., Kim J.S., Lee S.Y., In Y.H., Choi S.S., Rih J.-K., Kim C.H.,
RA   Jeong H., Hur C.G., Kim J.J.;
RT   "The genome sequence of the capnophilic rumen bacterium Mannheimia
RT   succiniciproducens.";
RL   Nat. Biotechnol. 22:1275-1281(2004).
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=AAU38415.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE016827; AAU38415.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_041639973.1; NC_006300.1.
DR   AlphaFoldDB; Q65RJ5; -.
DR   SMR; Q65RJ5; -.
DR   STRING; 221988.MS1808; -.
DR   CAZy; GH23; Glycoside Hydrolase Family 23.
DR   EnsemblBacteria; AAU38415; AAU38415; MS1808.
DR   KEGG; msu:MS1808; -.
DR   eggNOG; COG4623; Bacteria.
DR   HOGENOM; CLU_027494_0_1_6; -.
DR   OrthoDB; 1444566at2; -.
DR   Proteomes; UP000000607; 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.
PE   3: Inferred from homology;
KW   Cell outer membrane; Cell wall biogenesis/degradation; Lyase; Membrane;
KW   Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02016"
FT   CHAIN           19..484
FT                   /note="Membrane-bound lytic murein transglycosylase F"
FT                   /id="PRO_0000353949"
FT   REGION          19..267
FT                   /note="Non-LT domain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02016"
FT   REGION          268..484
FT                   /note="LT domain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02016"
FT   REGION          459..484
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        312
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02016"
SQ   SEQUENCE   484 AA;  55745 MW;  CDFB5F477F27773C CRC64;
     MKGLLLRIIA AFALVLWAID MVFPWQQMMR SEENRYNAIQ QRGKLVVGTV NNPVSYFIGN
     EGQAGLEYEL SRAFADYLGV ELEMKAMDNG EQLFDALEDN EIDIAAANLL YQAKKAETFQ
     LGPAYYSASW QLVYRKGESR PQSLSQIKDK LIIARGSELP LILQGYQTKY PNLKWQLENN
     QTQEELLLQV AQGKIKYTVA NSIDVSAVQQ VRPEIAVAFD VTDEASVHWY LPNNSYNELQ
     AALLDFMNTA LEGGLIARIE EKYFNHFSQF DYVDMRQYVQ AINDILPKYA PLFDRYKGDL
     DWRLLAAIAY QESHWNENAT SPTGVRGMMM LTKDTAERMK IADRTDAEQS IKAGSEYLHW
     LISQVPDSIP KEDRIWFALT GYNMGLGHML DARRLTKNLG GDPDNWLDVK KNLPLLAEKR
     YYPNLKYGYA RGYEAFQYVE NIRRYMNSII NYYRVQENAD NKDKPSETDE NLPLPLTDNQ
     EKQE