ID A0A2U2N4Z4_9GAMM Unreviewed; 480 AA.
AC A0A2U2N4Z4;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Membrane-bound lytic murein transglycosylase F {ECO:0000256|HAMAP-Rule:MF_02016};
DE EC=4.2.2.n1 {ECO:0000256|HAMAP-Rule:MF_02016};
DE AltName: Full=Murein lyase F {ECO:0000256|HAMAP-Rule:MF_02016};
DE Flags: Precursor;
GN Name=mltF {ECO:0000256|HAMAP-Rule:MF_02016};
GN ORFNames=DEM34_05155 {ECO:0000313|EMBL:PWG64275.1};
OS Spiribacter halobius.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Spiribacter.
OX NCBI_TaxID=2182432 {ECO:0000313|EMBL:PWG64275.1, ECO:0000313|Proteomes:UP000245474};
RN [1] {ECO:0000313|EMBL:PWG64275.1, ECO:0000313|Proteomes:UP000245474}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E85 {ECO:0000313|EMBL:PWG64275.1,
RC ECO:0000313|Proteomes:UP000245474};
RA Zheng W.-S., Lu D.-C., Du Z.-J.;
RT "Spiribacter halobius sp. nov., a moderately halophilic bacterium isolated
RT from marine solar saltern.";
RL Submitted (MAY-2018) 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:0000256|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:0000256|HAMAP-Rule:MF_02016};
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000256|HAMAP-
CC Rule:MF_02016}; Peripheral membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_02016}. Membrane {ECO:0000256|ARBA:ARBA00004170}; Peripheral
CC membrane protein {ECO:0000256|ARBA:ARBA00004170}. Note=Attached to the
CC inner leaflet of the outer membrane. {ECO:0000256|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:0000256|HAMAP-Rule:MF_02016}.
CC -!- SIMILARITY: Belongs to the transglycosylase Slt family.
CC {ECO:0000256|ARBA:ARBA00007734}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the transglycosylase
CC Slt family. {ECO:0000256|HAMAP-Rule:MF_02016}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the bacterial solute-
CC binding protein 3 family. {ECO:0000256|HAMAP-Rule:MF_02016}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_02016}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PWG64275.1}.
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DR EMBL; QFFI01000006; PWG64275.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U2N4Z4; -.
DR OrthoDB; 9815002at2; -.
DR Proteomes; UP000245474; Unassembled WGS sequence.
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 GO; GO:0000270; P:peptidoglycan metabolic process; IEA:InterPro.
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; IPR000189; Transglyc_AS.
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.
DR PROSITE; PS00922; TRANSGLYCOSYLASE; 1.
PE 3: Inferred from homology;
KW Cell outer membrane {ECO:0000256|ARBA:ARBA00023237, ECO:0000256|HAMAP-
KW Rule:MF_02016};
KW Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_02016};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_02016};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_02016};
KW Reference proteome {ECO:0000313|Proteomes:UP000245474};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|HAMAP-Rule:MF_02016}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02016"
FT CHAIN 22..480
FT /note="Membrane-bound lytic murein transglycosylase F"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02016"
FT /id="PRO_5015791432"
FT DOMAIN 40..263
FT /note="Solute-binding protein family 3/N-terminal"
FT /evidence="ECO:0000259|SMART:SM00062"
FT REGION 264..480
FT /note="LT domain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02016"
FT ACT_SITE 310
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02016"
SQ SEQUENCE 480 AA; 53860 MW; 26A05B4CF7BB0A3A CRC64;
MRRLQAHAVI ALLLAALLAV AWLQAQPERE PFDELTARGT LVVGTRYGPT TYYETRQGAH
GLEQALVRRF AEALGLAVEF RPVAEIATLL AMLERGEIDM AAGGLGKRPG DAERFAYSRP
YMTVEPRVVY ANGGDRPTGI GELAGRRLLV VSDSLHEARL RAAAEPYPGV RWESLPRASS
DDLLYRLTSG QADAVVTDSN ELTVNQHFYP EVRSAFTLGE PYGLRWAFRP GQDSLRARAD
AFLDRFEASG KLASLFERYH GHLRRFDYVG TRRFIRDVTR VLPRYRSAFQ EAAAEHDLDW
RLLAAIGYQE SHWDPEAVSP TGVRGVMMLT LSTAAQVGIE DRLEPAQSII GGARYLSSLL
ERLPESIAEP HRTWFALAAY NVGLGHLEDA RVLTERQGGD PDSWFDVRER LPLLAQERYY
STLRYGYARG AEPVAYVARI RRYYELLRRI TEPRITEGPG VEAPLPLDRL LFDDGLQSAF
//
