ID R8ATM0_PLESH Unreviewed; 521 AA.
AC R8ATM0;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 03-MAY-2023, entry version 55.
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=PLESHI_03872 {ECO:0000313|EMBL:EON89668.1};
OS Plesiomonas shigelloides 302-73.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Plesiomonas.
OX NCBI_TaxID=1315976 {ECO:0000313|EMBL:EON89668.1, ECO:0000313|Proteomes:UP000014012};
RN [1] {ECO:0000313|EMBL:EON89668.1, ECO:0000313|Proteomes:UP000014012}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=302-73 {ECO:0000313|EMBL:EON89668.1,
RC ECO:0000313|Proteomes:UP000014012};
RX PubMed=23814109;
RA Pique N., Aquilini E., Alioto T., Minana-Galbis D., Tomas J.M.;
RT "Genome Sequence of Plesiomonas shigelloides Strain 302-73 (Serotype O1).";
RL Genome Announc. 1:e00404-13(2013).
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:EON89668.1}.
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DR EMBL; AQQO01000028; EON89668.1; -; Genomic_DNA.
DR RefSeq; WP_010862407.1; NZ_KB944507.1.
DR AlphaFoldDB; R8ATM0; -.
DR STRING; 703.SAMEA2665130_00589; -.
DR GeneID; 69705446; -.
DR PATRIC; fig|1315976.3.peg.756; -.
DR HOGENOM; CLU_027494_0_1_6; -.
DR OrthoDB; 9815002at2; -.
DR Proteomes; UP000014012; 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:UP000014012};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|HAMAP-Rule:MF_02016}.
FT DOMAIN 44..267
FT /note="Solute-binding protein family 3/N-terminal"
FT /evidence="ECO:0000259|SMART:SM00062"
FT REGION 268..521
FT /note="LT domain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02016"
FT REGION 497..521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 312
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02016"
SQ SEQUENCE 521 AA; 58430 MW; DB1F1F7FD7C30611 CRC64;
MKTLNFKWIS CLLLLAVGLA VLLPGRNWVF DRRSQLEQVK ERGELRVGTI NSALSYYIGP
NGPSGLEYEL TKRFADYLGV ELRIESAFSL TDLFPAVNEK RLDMAAAGLL FNQERLSQFR
VGPSYYSVSQ QLVYRKGKAR PKNLNDLKGT LMVASGSAHA ASLAKLTGKF TNLSWKATTD
LSSDELLRQV AEGSLDYTVA DSVSIAALQR IKPELAVAFD ISDEEPVVWY MRKSDDDSLY
AAMLDFMSEI VEDGTLARLE EKYFGHIDEF DYVDTRTFLA EIEKTLPQYQ KLFEQYAGEL
DWRLLAAVAY QESHWDPDAT SPTGVRGLMM LTRPTAASVG VSDRTDPEQS IRGGSDYLAR
LMDKIPESIP EDERAWFALA AYNIGFGHMM DARRLTKTQG ANPDSWADVK QRLPMLSQKR
YYAQTRYGFA RGGEAFRYVE NIRRYMQSLV GYDQAQQLAI AAKAKEVAPL NDNGEPAVIN
TAQEAREQNA LQRAEMKQSR QEAMTELKSP GAGLVTAKVK E
//
