ID A0A432X7Z4_9GAMM Unreviewed; 488 AA.
AC A0A432X7Z4;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 13.
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=CWE15_06255 {ECO:0000313|EMBL:RUO43001.1};
OS Aliidiomarina taiwanensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Idiomarinaceae; Aliidiomarina.
OX NCBI_TaxID=946228 {ECO:0000313|EMBL:RUO43001.1, ECO:0000313|Proteomes:UP000286976};
RN [1] {ECO:0000313|EMBL:RUO43001.1, ECO:0000313|Proteomes:UP000286976}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AIT1 {ECO:0000313|EMBL:RUO43001.1,
RC ECO:0000313|Proteomes:UP000286976};
RX PubMed=30364313; DOI=.3389/fmicb.2018.02453;
RA Liu Y., Lai Q., Shao Z.;
RT "Genome-Based Analysis Reveals the Taxonomy and Diversity of the Family
RT Idiomarinaceae.";
RL Front. Microbiol. 9:2453-2453(2018).
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: 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:RUO43001.1}.
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DR EMBL; PIPQ01000002; RUO43001.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A432X7Z4; -.
DR OrthoDB; 9815002at2; -.
DR Proteomes; UP000286976; 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 Reference proteome {ECO:0000313|Proteomes:UP000286976};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|HAMAP-Rule:MF_02016};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..44
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 61..285
FT /note="Solute-binding protein family 3/N-terminal"
FT /evidence="ECO:0000259|SMART:SM00062"
FT REGION 38..285
FT /note="Non-LT domain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02016"
FT REGION 286..488
FT /note="LT domain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02016"
FT ACT_SITE 330
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02016"
SQ SEQUENCE 488 AA; 56319 MW; 4403EDBBEA5F046A CRC64;
MASDSSPTKQ GLQPAHRVVL FRILRAATVL GLVMIIPLWL NIFAPEPIEH SRLRHVLERG
ELRIGTLMTP TNFQERNGLR GGFEYDLANG LAKQLGVQLE VTQVLDIRQL WTLLEHKQVD
FLAAGLDVTA MRRDNLRFSP PYNFIEQKLV YKQGTRDRPR DWSQVQGRIR VVSDSSHEEL
LRRISTLHPH LNWSSTHLYD ADELLDQVMA EEIDFAIVDS HHLNIRRRYY PDLSIAFTVR
DKVPLAWVFP NESDDSLYAS AIEYIGSQHN TGHIAKLTDR YFGHVQEFNY VDTQLFIAAV
EHTLPKYLDM FQRYAGGLDW RLLAAVSYQE SLWDPWARSP TGVRGLMMLT LPTAHAMGVR
SRLDPEESIR GGARYLALLH QRIPARITEP DRTWFALAAY NVGMGHLNDA RIITERQGGN
PDYWIDVRER LPLLRQKQFY RTTQYGYARG DEPVRYVGNI RRYYDTLKWL DEQGRIPYPE
AASGVLAD
//
