ID   MLTF_PASMU              Reviewed;         492 AA.
AC   Q9CPJ2;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 2.
DT   25-MAY-2022, entry version 109.
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=PM0045;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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=AAK02129.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE004439; AAK02129.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_041422488.1; NC_002663.1.
DR   AlphaFoldDB; Q9CPJ2; -.
DR   SMR; Q9CPJ2; -.
DR   STRING; 747.DR93_2034; -.
DR   CAZy; GH23; Glycoside Hydrolase Family 23.
DR   EnsemblBacteria; AAK02129; AAK02129; PM0045.
DR   KEGG; pmu:PM0045; -.
DR   PATRIC; fig|272843.6.peg.45; -.
DR   HOGENOM; CLU_027494_0_1_6; -.
DR   OMA; YYDILTW; -.
DR   Proteomes; UP000000809; 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   Reference proteome; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02016"
FT   CHAIN           19..492
FT                   /note="Membrane-bound lytic murein transglycosylase F"
FT                   /id="PRO_0000353952"
FT   REGION          19..268
FT                   /note="Non-LT domain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02016"
FT   REGION          270..492
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   492 AA;  56176 MW;  59AC499A9434D43D CRC64;
     MKGLFLRIIA IVALLLWAID MVFPWQQIMR SEENRYTAIQ SRGKLVVGTI NNPISYFIDH
     AGQAAGLEYE LSKAFADYLN VDLEILAMSN GDELFSALKN NKIDIAAANL LYQPNKLDMF
     QVGPTYNSAS WQLVYRKGTE RPRSLGELKG SLSIASGSEL TELLKVEKEK YPDLIWRVNE
     KLTPEELLIQ MADGKIDYVI ANSIDVSAVQ QIKPNVAVAF DVTDESTVHW YLPSNSYSEL
     QASLLDFMNS AIETGLIARI EEKYFNHLAQ FDYVDTRSYL RAIETVLPKF APLFEKYKGD
     LDWCLLAAIA YQESHWNPDA TSPTGVRGMM MLTKATAERM RIQDRTDPEQ SIKAGSEYLH
     WLITQMPDTI KEDERIWFAL AAYNMGLGHL LDARRLTKSL GGDPDNWLDV KKNLPLLAEK
     RYYTGLKYGY ARGYEAYHYV ENIRRYMNSI VHYYRVQQAQ IEETLDTQAA EIENINEIKK
     ETDTLATTVT TQ