ID   MLTF_MAGMM              Reviewed;         507 AA.
AC   A0L862;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 2.
DT   25-MAY-2022, entry version 77.
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=Mmc1_1646;
OS   Magnetococcus marinus (strain ATCC BAA-1437 / JCM 17883 / MC-1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Magnetococcales;
OC   Magnetococcaceae; Magnetococcus.
OX   NCBI_TaxID=156889;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1437 / JCM 17883 / MC-1;
RX   PubMed=19465526; DOI=10.1128/aem.02874-08;
RA   Schubbe S., Williams T.J., Xie G., Kiss H.E., Brettin T.S., Martinez D.,
RA   Ross C.A., Schuler D., Cox B.L., Nealson K.H., Bazylinski D.A.;
RT   "Complete genome sequence of the chemolithoautotrophic marine magnetotactic
RT   coccus strain MC-1.";
RL   Appl. Environ. Microbiol. 75:4835-4852(2009).
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=ABK44155.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000471; ABK44155.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; A0L862; -.
DR   SMR; A0L862; -.
DR   STRING; 156889.Mmc1_1646; -.
DR   CAZy; GH23; Glycoside Hydrolase Family 23.
DR   EnsemblBacteria; ABK44155; ABK44155; Mmc1_1646.
DR   KEGG; mgm:Mmc1_1646; -.
DR   eggNOG; COG4623; Bacteria.
DR   HOGENOM; CLU_027494_0_1_5; -.
DR   Proteomes; UP000002586; 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   Reference proteome; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02016"
FT   CHAIN           21..507
FT                   /note="Membrane-bound lytic murein transglycosylase F"
FT                   /id="PRO_0000353948"
FT   REGION          21..261
FT                   /note="Non-LT domain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02016"
FT   REGION          264..507
FT                   /note="LT domain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02016"
FT   ACT_SITE        310
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02016"
SQ   SEQUENCE   507 AA;  58263 MW;  2BB0E26EC804728B CRC64;
     MRRYPTLVVL LLLVLLPVLG CDLSMKRPIM DEIRKTGVLV VVTRNAPTTY YQGRDRVEGF
     EHDLATLFAA HLGVKVAFIK KQSRGEVLQT LHEGKAHLAA AGLVRQEEDG DRYLYGPDYQ
     SVFQQVVCRR GGVRPTNLLK LTQAKLTVVK ESAYEDRLRE LQQLVPQLTW HSDDNLSVEQ
     VLEQVWLGKV DCTLADSNVV ALNRRYYPEL TVKFPINAEQ RLAWTLPKRA VFLHKEVVTW
     FNEIRSNGQL DELFEKYYGF VEGQSFDFVD NRQFIKRMSE RLPSYKHLFM EAARKYHIPW
     QLLAAQAYQE SHWDPKARSS TGVRGIMMLT QVTAKALGID DRLDPKSSIH GGAWYLSNMR
     RRLPSTITEP DRTWIALAAY NVGLGHISDA RRLAKKQNLN PNRWSDLRQV LPLLSQSKYF
     KDTKFGYARG DEPVRYVAKV RHYNDILTRM ERKNYTGETT PFVEPNTALP MVPLKEQAVI
     GEINPMDGRM VETSGKEAAV PSPKRRY