MLTF_DESOH
ID MLTF_DESOH Reviewed; 454 AA.
AC A8ZWR8;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 2.
DT 25-MAY-2022, entry version 71.
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=Dole_2596;
OS Desulfococcus oleovorans (strain DSM 6200 / JCM 39069 / Hxd3).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales;
OC Desulfosudaceae; Desulfosudis.
OX NCBI_TaxID=96561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6200 / JCM 39069 / Hxd3;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Wawrik B.,
RA Richardson P.;
RT "Complete sequence of Desulfococcus oleovorans Hxd3.";
RL Submitted (OCT-2007) 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 -!- SEQUENCE CAUTION:
CC Sequence=ABW68399.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000859; ABW68399.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; A8ZWR8; -.
DR SMR; A8ZWR8; -.
DR STRING; 96561.Dole_2596; -.
DR CAZy; GH23; Glycoside Hydrolase Family 23.
DR EnsemblBacteria; ABW68399; ABW68399; Dole_2596.
DR KEGG; dol:Dole_2596; -.
DR eggNOG; COG4623; Bacteria.
DR HOGENOM; CLU_027494_0_1_7; -.
DR Proteomes; UP000008561; 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..24
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02016"
FT CHAIN 25..454
FT /note="Membrane-bound lytic murein transglycosylase F"
FT /id="PRO_0000353925"
FT REGION 25..265
FT /note="Non-LT domain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02016"
FT REGION 266..454
FT /note="LT domain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02016"
FT ACT_SITE 311
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02016"
SQ SEQUENCE 454 AA; 52993 MW; 0B29619506C3F511 CRC64;
MRRPLRRVTV VLLWVALAIG VAWFYDYRRS MQSLWKIRQH GKIVVLTENN ANSYYIYKET
PMGFEYDLAK AFAGHLGVDL EVKTPGWDAL FASLQRGDGD FIAASMTHTR KREQYADFSE
PYLSVRQHLI LHKSDHSIVT PAGLAGRTVH VREDTTYQQR LEALQADGID LQLVLHRNTP
TEELIEQVAK RQIDITVADS AIALLNRRYY PDIRIAFPIE KEQPLAWAVR KGDRGLRTEI
NRFFDEIKEN GTFTRIYNRY YTAVDTFDYV DVKKFHQRIY TRLPRFRPLI EKAADRHGFD
WQMIAAVIYQ ESHFDPFAQS HTGVKGLMQL TRVTAEEMGV TDRFDFEQNI TAGVAYLAKL
RHRFDDIEDP RTRLLFALAS YNIGYGHVRD AQQIAKNMGM DPNRWQSLKE VLPLLRNREY
YADTTYGYAR GNEAVRYIER ILTYYDILKQ KKAV
