ID A0A0A3Z4H3_9GAMM Unreviewed; 485 AA.
AC A0A0A3Z4H3;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 48.
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};
GN Name=mltF {ECO:0000256|HAMAP-Rule:MF_02016};
GN ORFNames=NG99_14110 {ECO:0000313|EMBL:KGT92521.1};
OS Erwinia typographi.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=371042 {ECO:0000313|EMBL:KGT92521.1, ECO:0000313|Proteomes:UP000030351};
RN [1] {ECO:0000313|EMBL:KGT92521.1, ECO:0000313|Proteomes:UP000030351}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M043b {ECO:0000313|EMBL:KGT92521.1,
RC ECO:0000313|Proteomes:UP000030351};
RA Chan K.-G., Tan W.-S.;
RT "Genome sequence of Erwinia typographi M043b.";
RL Submitted (OCT-2014) 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|ARBA:ARBA00001420, ECO:0000256|HAMAP-
CC 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:KGT92521.1}.
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; JRUQ01000040; KGT92521.1; -; Genomic_DNA.
DR RefSeq; WP_034893967.1; NZ_JRUQ01000040.1.
DR AlphaFoldDB; A0A0A3Z4H3; -.
DR STRING; 371042.NG99_14110; -.
DR eggNOG; COG4623; Bacteria.
DR OrthoDB; 9815002at2; -.
DR Proteomes; UP000030351; 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|ARBA:ARBA00023316,
KW 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 Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|HAMAP-Rule:MF_02016}.
FT DOMAIN 44..268
FT /note="Solute-binding protein family 3/N-terminal"
FT /evidence="ECO:0000259|SMART:SM00062"
FT REGION 269..485
FT /note="LT domain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02016"
FT ACT_SITE 313
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02016"
SQ SEQUENCE 485 AA; 55014 MW; 23A980677129A74E CRC64;
MKRLKINYLF IGLVTVLLAL ALWPAVPWYG GQQNQIEQIK SRGVLRVSTL NSPLAYYTIN
KAPAGMDYEL AKRFAGYLGV KLQITVRQNL SDLFDDLEDD KADVLAAGLI YNKDRESRFR
TGPAYYSVSQ QLVYRMGKPR PKNLGDLHGR LTVASDSAYL STLRGIKQNQ YPDLDWAIST
DQSPNALLEA VADGRLDYTV SDSVSVALLQ RIHPQLAVAF DITDEEPVTW YMQRDRDDSM
NAAMLDYFNQ MGEEGAMARL DEKYLGHVGT FDYVDTRTFL RAIDATLPVI RPLFEKYATE
MDWRLLAAIS YQESHWNPQA TSPTGVRGMM MLTRNTAESL NVSDRTDPEQ SIRGGSEYLI
SMMAKVPQTI PEDERIWFAL AAYNMGYAHM LDARKLTEKQ KGNPDSWADV KQRLPLLSQK
RYYSQTTYGY ARGQEAYNYV ENIRLYQISL VGYLLAQERK LAQQAAWEAE MGEGYPAVAP
QIALN
//
