MLTF_SHEWM
ID MLTF_SHEWM Reviewed; 480 AA.
AC B1KLC4;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 79.
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=Swoo_1563;
OS Shewanella woodyi (strain ATCC 51908 / MS32).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=392500;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51908 / MS32;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Lykidis A., Zhao J.-S., Richardson P.;
RT "Complete sequence of Shewanella woodyi ATCC 51908.";
RL Submitted (FEB-2008) 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}.
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DR EMBL; CP000961; ACA85849.1; -; Genomic_DNA.
DR RefSeq; WP_012324195.1; NC_010506.1.
DR AlphaFoldDB; B1KLC4; -.
DR SMR; B1KLC4; -.
DR STRING; 392500.Swoo_1563; -.
DR CAZy; GH23; Glycoside Hydrolase Family 23.
DR EnsemblBacteria; ACA85849; ACA85849; Swoo_1563.
DR KEGG; swd:Swoo_1563; -.
DR eggNOG; COG4623; Bacteria.
DR HOGENOM; CLU_027494_0_1_6; -.
DR OMA; YYDILTW; -.
DR OrthoDB; 1444566at2; -.
DR Proteomes; UP000002168; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Cell outer membrane; Cell wall biogenesis/degradation; Lyase; Membrane;
KW Reference proteome; Signal.
FT SIGNAL 1..15
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02016"
FT CHAIN 16..480
FT /note="Membrane-bound lytic murein transglycosylase F"
FT /id="PRO_5000317081"
FT REGION 16..259
FT /note="Non-LT domain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02016"
FT REGION 260..480
FT /note="LT domain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02016"
FT ACT_SITE 304
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02016"
SQ SEQUENCE 480 AA; 54833 MW; D2CBD24F7F47E227 CRC64;
MNRILLTLLT LTLLAGCQRV AVEETKLVPP AVEKTVLNVG TIYGSQIYVT TGQGEAGFDY
EMASRFADHL ELELAMKPYS NIKELYQALN SGEVDLIAAG LADTPTRREN FRLGPPLYRV
NQVLVYKQGT PQPKDISQLK DEITVITDSS FVDTLSQLQK IYPELVWDQE QDKDNEELLA
MIARGEISYT IADSTTFEIS RRYMPELRAG LTLKEKQAIV WLLPAQNSDK LMSELLTFWH
GEKLDGTLAH LDEKYFAHVK RFDYVDTRAF LRAIDNKLPK YKERFQYYAG DLDWRKLAAT
AYQESHWNPN ARSPTGVRGL MMLTLPTAKQ MGIENRLDAE QSIKGGAKYL RGILNRLPDS
IPDNQRMWFA LASYNIGYGH VEDARKLAES MGLNPSAWRD LKEVLPLLQK RKYYKQTRYG
YARGNEAVHY VDNIRRYYDT LVWIDNQNKL LEENQALIEE SQLADQIGIG EKAITGAQPE
