MLTF_PSEU2
ID MLTF_PSEU2 Reviewed; 498 AA.
AC Q4ZX03;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=Membrane-bound lytic murein transglycosylase F {ECO:0000255|HAMAP-Rule:MF_02016};
DE EC=4.2.2.n1 {ECO:0000255|HAMAP-Rule:MF_02016};
DE AltName: Full=Murein lyase F {ECO:0000255|HAMAP-Rule:MF_02016};
DE Flags: Precursor;
GN Name=mltF {ECO:0000255|HAMAP-Rule:MF_02016}; OrderedLocusNames=Psyr_1268;
OS Pseudomonas syringae pv. syringae (strain B728a).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX NCBI_TaxID=205918;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B728a;
RX PubMed=16043691; DOI=10.1073/pnas.0504930102;
RA Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A.,
RA Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S.,
RA Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M.,
RA Kyrpides N.C., Ivanova N., Lindow S.E.;
RT "Comparison of the complete genome sequences of Pseudomonas syringae pv.
RT syringae B728a and pv. tomato DC3000.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(2005).
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:0000255|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:0000255|HAMAP-Rule:MF_02016};
CC -!- SUBCELLULAR LOCATION: Cell outer membrane; Peripheral membrane protein.
CC Note=Attached to the inner leaflet of the outer membrane.
CC {ECO:0000255|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:0000255|HAMAP-Rule:MF_02016}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the bacterial solute-
CC binding protein 3 family. {ECO:0000255|HAMAP-Rule:MF_02016}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the transglycosylase
CC Slt family. {ECO:0000255|HAMAP-Rule:MF_02016}.
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DR EMBL; CP000075; AAY36319.1; -; Genomic_DNA.
DR RefSeq; WP_011266923.1; NC_007005.1.
DR RefSeq; YP_234357.1; NC_007005.1.
DR AlphaFoldDB; Q4ZX03; -.
DR SMR; Q4ZX03; -.
DR STRING; 205918.Psyr_1268; -.
DR CAZy; GH23; Glycoside Hydrolase Family 23.
DR EnsemblBacteria; AAY36319; AAY36319; Psyr_1268.
DR KEGG; psb:Psyr_1268; -.
DR PATRIC; fig|205918.7.peg.1300; -.
DR eggNOG; COG4623; Bacteria.
DR HOGENOM; CLU_027494_0_1_6; -.
DR OMA; YYDILTW; -.
DR Proteomes; UP000000426; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016837; F:carbon-oxygen lyase activity, acting on polysaccharides; IEA:InterPro.
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 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 Pfam; PF00497; SBP_bac_3; 1.
DR Pfam; PF01464; SLT; 1.
DR SMART; SM00062; PBPb; 1.
DR SUPFAM; SSF53955; SSF53955; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS00922; TRANSGLYCOSYLASE; 1.
PE 3: Inferred from homology;
KW Cell outer membrane; Cell wall biogenesis/degradation; Lyase; Membrane;
KW Signal.
FT SIGNAL 1..29
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02016"
FT CHAIN 30..498
FT /note="Membrane-bound lytic murein transglycosylase F"
FT /id="PRO_0000353967"
FT REGION 30..267
FT /note="Non-LT domain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02016"
FT REGION 268..498
FT /note="LT domain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02016"
FT REGION 464..498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 314
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02016"
SQ SEQUENCE 498 AA; 55897 MW; 286C6ADA775CC218 CRC64;
MFFKPDFRPR CAKWLIATGL FLMLGACVEK PTTLERVKED GVLRVITRNS PATYFQDRNG
ETGFEYELVK RFADDLGVEL KIETADNLDD LFDQMNKPGG PVLGAAGLIE TPLRKQQARF
SHSYLEVTPQ VVYRNGQSRP TDPGDLVGKR IVVLKGSAHA EQLAALKAQN PGIQYEESDA
VEVVDLLRMV DEGQIDLTLV DSNELAMNQV YFPNVRVAFD LGEARAQRWA VAPGEDNSLL
NEINAYLDKV EKNGTLQRLK DRYYGHVDVL GYVGAYTFAQ HLQERLPKYE KHFQTSAKKE
QVDWRLLAAI GYQESMWQPT VTSKTGVRGL MMLTQNTAQA MGVSNRLDAR QSIQGGAKYF
AYIKDQLDDS IKEPDRTWLA LASYNIGSGH LEDARKLAQN EGLNPDKWLD VKKMLPRLAQ
KKWYSKTRYG YARGGEPVHF VANIRRYYDI LTWVTQPQLE GSQVADGNLH VPGVDKTQPP
VPPASPVPSS SSTDESPL
