ID   MLTF_NITMU              Reviewed;         478 AA.
AC   Q2Y6L9;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   25-MAY-2022, entry version 87.
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=Nmul_A2311;
OS   Nitrosospira multiformis (strain ATCC 25196 / NCIMB 11849 / C 71).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC   Nitrosomonadaceae; Nitrosospira.
OX   NCBI_TaxID=323848;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25196 / NCIMB 11849 / C 71;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA   Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Lykidis A., Richardson P.;
RT   "Complete sequence of chromosome 1 of Nitrosospira multiformis ATCC
RT   25196.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000103; ABB75602.1; -; Genomic_DNA.
DR   RefSeq; WP_011381608.1; NZ_FNVK01000006.1.
DR   AlphaFoldDB; Q2Y6L9; -.
DR   SMR; Q2Y6L9; -.
DR   STRING; 323848.Nmul_A2311; -.
DR   CAZy; GH23; Glycoside Hydrolase Family 23.
DR   EnsemblBacteria; ABB75602; ABB75602; Nmul_A2311.
DR   KEGG; nmu:Nmul_A2311; -.
DR   eggNOG; COG4623; Bacteria.
DR   HOGENOM; CLU_027494_0_1_4; -.
DR   OMA; YYDILTW; -.
DR   OrthoDB; 1444566at2; -.
DR   Proteomes; UP000002718; 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..29
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02016"
FT   CHAIN           30..478
FT                   /note="Membrane-bound lytic murein transglycosylase F"
FT                   /id="PRO_0000353951"
FT   REGION          30..269
FT                   /note="Non-LT domain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02016"
FT   REGION          271..478
FT                   /note="LT domain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02016"
FT   ACT_SITE        316
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02016"
SQ   SEQUENCE   478 AA;  54437 MW;  B0E5C4FE5A617009 CRC64;
     MFPDSSYLFS MRSLSRFLIA IFGCGALLAS CDSFERSVLP FDKTDELVVI TVNSPDTYYE
     NAEGSYAGLD YDLATEFAKE LGMKVRFKTV PRLDKAWSLL EKHKGHFAAG MNISAKHSRH
     VAFGPIYQLV QPQLAYNTDY NKPKNLHQLG GRTIRIAKGV THAEQLNKAK HEVPELKWKE
     MDLTPDELLA RLAEGKVDYV VADSTQINLA KNFYPNLNAA FNLGDSVGRA WAFSPFAEQA
     LLEATQKFFT RIQQDGTLTR LLDRYYGHIE RLHHTDVNGI LAKRRTILPE LREHFYEAEE
     LSGIDWRLIA ALAYQESHWD ALATSPSNVR GIMMLTEITA DRMKVTDRLD ARQSILAGAR
     YFALLKDKLP TRIKEPDRTW MALAAYNQGP SHLEDARILA QKMGLSPDAW VDLKKTLPLL
     SQSEHFRTLR HGFARGGQAV VLAESVRIYY EILQKYEPPY SWGFPIVARK EDDSWQEF