ID MLTF_MARMM Reviewed; 456 AA.
AC Q0AQY9;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 2.
DT 24-JAN-2024, entry version 93.
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=Mmar10_1005;
OS Maricaulis maris (strain MCS10).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Maricaulales; Maricaulaceae;
OC Maricaulis.
OX NCBI_TaxID=394221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCS10;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Saunders E., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Viollier P.,
RA Stephens C., Richardson P.;
RT "Complete sequence of Maricaulis maris MCS10.";
RL Submitted (AUG-2006) 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=ABI65298.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000449; ABI65298.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_011642945.1; NC_008347.1.
DR AlphaFoldDB; Q0AQY9; -.
DR SMR; Q0AQY9; -.
DR STRING; 394221.Mmar10_1005; -.
DR CAZy; GH23; Glycoside Hydrolase Family 23.
DR KEGG; mmr:Mmar10_1005; -.
DR eggNOG; COG4623; Bacteria.
DR HOGENOM; CLU_027494_0_1_5; -.
DR Proteomes; UP000001964; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
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 CDD; cd13403; MLTF-like; 1.
DR CDD; cd01009; PBP2_YfhD_N; 1.
DR Gene3D; 1.10.530.10; -; 1.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
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 PANTHER; PTHR35936; MEMBRANE-BOUND LYTIC MUREIN TRANSGLYCOSYLASE F; 1.
DR PANTHER; PTHR35936:SF32; MEMBRANE-BOUND LYTIC MUREIN TRANSGLYCOSYLASE F; 1.
DR Pfam; PF00497; SBP_bac_3; 1.
DR Pfam; PF01464; SLT; 1.
DR SMART; SM00062; PBPb; 1.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
PE 3: Inferred from homology;
KW Cell outer membrane; Cell wall biogenesis/degradation; Lyase; Membrane;
KW Reference proteome; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02016"
FT CHAIN 23..456
FT /note="Membrane-bound lytic murein transglycosylase F"
FT /id="PRO_5000131754"
FT REGION 23..267
FT /note="Non-LT domain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02016"
FT REGION 268..456
FT /note="LT domain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02016"
FT ACT_SITE 314
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02016"
SQ SEQUENCE 456 AA; 50172 MW; 845E67D0A90395C7 CRC64;
MKTWPSRAVS LLLLALALPV GCSEPPPPVR DPDTLATIRE RGELVVLTLA GPTSLIENED
GPPSGYEVDL ANAFAASLGV TARFEVAASL PDLFDALAAG DGHVAAAGLT LTPERSERLA
FSPVYKSVTE QLVCRRGGVN PTRLERLPDA DIVVLEGSSY EETLRAIGVT HTALRWRTRP
GGSAMPLLEA VDDGQADCTI ADSHLADFAR RRHPELIVAR NLTGEQPLAW AYDARIDGLG
EALSAWFATA HADGLLEALD ETWFGRFGDY DYVDVARFVR RVENRLPRYR RLFEAAADEL
PFEWELLAAQ AYQESHWDPD AVSATGVRGL MMLTLSTAER VGIDDRTDPE QSIVGGAAYL
DDLYERVPDS VTGPDRLWFA LAAYNVGMGH MYDARRLAER LGRDKDSWDD LAEILPLLSD
PAHYSTLRYG YARGHEPVRY VAKIREYRAL LAAQDL
//
