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Database: UniProt
Entry: A0A078LNG8_9PSED
LinkDB: A0A078LNG8_9PSED
Original site: A0A078LNG8_9PSED 
ID   A0A078LNG8_9PSED        Unreviewed;       487 AA.
AC   A0A078LNG8;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 37.
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=BN1079_01349 {ECO:0000313|EMBL:CDZ94038.1};
OS   Pseudomonas saudiphocaensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1499686 {ECO:0000313|EMBL:CDZ94038.1, ECO:0000313|Proteomes:UP000053902};
RN   [1] {ECO:0000313|EMBL:CDZ94038.1, ECO:0000313|Proteomes:UP000053902}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=20_BN {ECO:0000313|EMBL:CDZ94038.1,
RC   ECO:0000313|Proteomes:UP000053902};
RA   Urmite Genomes Urmite Genomes;
RL   Submitted (JUL-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|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}.
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DR   EMBL; CCSF01000001; CDZ94038.1; -; Genomic_DNA.
DR   RefSeq; WP_037023166.1; NZ_CCSF01000001.1.
DR   AlphaFoldDB; A0A078LNG8; -.
DR   STRING; 1499686.BN1079_01349; -.
DR   eggNOG; COG4623; Bacteria.
DR   HOGENOM; CLU_027494_0_1_6; -.
DR   OrthoDB; 9815002at2; -.
DR   Proteomes; UP000053902; 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:UP000053902};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|HAMAP-Rule:MF_02016}.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02016"
FT   CHAIN           29..487
FT                   /note="Membrane-bound lytic murein transglycosylase F"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02016"
FT                   /id="PRO_5008981731"
FT   DOMAIN          42..268
FT                   /note="Solute-binding protein family 3/N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00062"
FT   REGION          269..487
FT                   /note="LT domain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02016"
FT   ACT_SITE        315
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02016"
SQ   SEQUENCE   487 AA;  54663 MW;  B2739F096964D4FF CRC64;
     MFAQTQLRKR CTNWLLATGL LLMLTSCAEP PSAVERIKEE GVLRVITRNS PSTYFQDRNG
     EAGFEYELVK RFATHLGVEL QIETADNIEE IFARLNRPGG PALAAAGLVA SEGRQGIARF
     TDSYLDVTTQ VVYRRGERRP TQPQDMVGKR ILVLKGSSQA EKLKALQTEL PDLRYEESDA
     VEVVDLLRMV DEGLVDLTLV ESNELALNQV YFTNARVAFD LGEQNSLAWI LGKDEEDDTL
     LEAANAFLAE AKENGTLQRL RERYYGHVDV LGYVGAYAFA KHLQERLPRY EKIFRETAKV
     HGVDWRLLAA IGYQESHWQP DAVSKTGVRG LMMLTLNTAK AMGVTNRVDP VQSIQGGGKY
     IALVHSNLPD SIKEPDRTWF ALAAYNVGGG HLEDARKLAE AEGLDPNKWL DVKQMLPRLS
     QKQWYSKTRY GYARGGEPVH FVANIRRYYD ILTWVTQPQL EGQQLVQSEI HTPGINSTDL
     GESLPPL
//
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