MLTF_PSEAE
ID MLTF_PSEAE Reviewed; 490 AA.
AC Q9HXN1;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 118.
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=PA3764;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG07151.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE004091; AAG07151.1; ALT_INIT; Genomic_DNA.
DR PIR; C83175; C83175.
DR RefSeq; NP_252453.1; NC_002516.2.
DR RefSeq; WP_003104806.1; NZ_QZGE01000001.1.
DR PDB; 4OWD; X-ray; 2.21 A; A=33-459.
DR PDB; 4OYV; X-ray; 2.31 A; A=28-460.
DR PDB; 4OZ9; X-ray; 2.24 A; A=33-460.
DR PDB; 4P0G; X-ray; 1.65 A; A=28-460.
DR PDB; 4P11; X-ray; 1.89 A; A=28-460.
DR PDB; 5A5X; X-ray; 1.80 A; A=38-490, B=40-490.
DR PDB; 5AA1; X-ray; 2.89 A; A/B/C/D=8-490.
DR PDB; 5AA2; X-ray; 2.80 A; A/B/C/D=8-490.
DR PDB; 5AA3; X-ray; 3.20 A; A/B/C/D/E/F/G/H/I/J/K/L=8-490.
DR PDBsum; 4OWD; -.
DR PDBsum; 4OYV; -.
DR PDBsum; 4OZ9; -.
DR PDBsum; 4P0G; -.
DR PDBsum; 4P11; -.
DR PDBsum; 5A5X; -.
DR PDBsum; 5AA1; -.
DR PDBsum; 5AA2; -.
DR PDBsum; 5AA3; -.
DR AlphaFoldDB; Q9HXN1; -.
DR SMR; Q9HXN1; -.
DR STRING; 287.DR97_4111; -.
DR CAZy; GH23; Glycoside Hydrolase Family 23.
DR PaxDb; Q9HXN1; -.
DR PRIDE; Q9HXN1; -.
DR DNASU; 880530; -.
DR EnsemblBacteria; AAG07151; AAG07151; PA3764.
DR GeneID; 880530; -.
DR KEGG; pae:PA3764; -.
DR PATRIC; fig|208964.12.peg.3939; -.
DR PseudoCAP; PA3764; -.
DR HOGENOM; CLU_027494_0_1_6; -.
DR InParanoid; Q9HXN1; -.
DR OMA; YYDILTW; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IBA:GO_Central.
DR GO; GO:0016837; F:carbon-oxygen lyase activity, acting on polysaccharides; IEA:InterPro.
DR GO; GO:0008933; F:lytic transglycosylase activity; IBA:GO_Central.
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:0009253; P:peptidoglycan catabolic process; IBA:GO_Central.
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; PS00922; TRANSGLYCOSYLASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell outer membrane; Cell wall biogenesis/degradation; Lyase;
KW Membrane; Reference proteome; Signal.
FT SIGNAL 1..32
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02016"
FT CHAIN 33..490
FT /note="Membrane-bound lytic murein transglycosylase F"
FT /id="PRO_0000353957"
FT REGION 33..269
FT /note="Non-LT domain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02016"
FT REGION 270..490
FT /note="LT domain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02016"
FT REGION 467..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 316
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02016"
FT HELIX 35..42
FT /evidence="ECO:0007829|PDB:4P0G"
FT STRAND 44..52
FT /evidence="ECO:0007829|PDB:4P0G"
FT TURN 53..55
FT /evidence="ECO:0007829|PDB:4P0G"
FT STRAND 56..59
FT /evidence="ECO:0007829|PDB:4P0G"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:4P0G"
FT HELIX 66..78
FT /evidence="ECO:0007829|PDB:4P0G"
FT STRAND 81..89
FT /evidence="ECO:0007829|PDB:4P0G"
FT HELIX 90..97
FT /evidence="ECO:0007829|PDB:4P0G"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:4P0G"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:5AA1"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:4P0G"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:4P0G"
FT STRAND 131..136
FT /evidence="ECO:0007829|PDB:4P0G"
FT HELIX 145..148
FT /evidence="ECO:0007829|PDB:4P0G"
FT STRAND 153..156
FT /evidence="ECO:0007829|PDB:4P0G"
FT HELIX 160..171
FT /evidence="ECO:0007829|PDB:4P0G"
FT STRAND 178..182
FT /evidence="ECO:0007829|PDB:4P0G"
FT HELIX 185..193
FT /evidence="ECO:0007829|PDB:4P0G"
FT STRAND 196..203
FT /evidence="ECO:0007829|PDB:4P0G"
FT HELIX 204..210
FT /evidence="ECO:0007829|PDB:4P0G"
FT TURN 211..213
FT /evidence="ECO:0007829|PDB:4P0G"
FT STRAND 217..222
FT /evidence="ECO:0007829|PDB:4P0G"
FT STRAND 227..229
FT /evidence="ECO:0007829|PDB:4P0G"
FT STRAND 232..237
FT /evidence="ECO:0007829|PDB:4P0G"
FT HELIX 240..254
FT /evidence="ECO:0007829|PDB:4P0G"
FT HELIX 257..266
FT /evidence="ECO:0007829|PDB:4P0G"
FT HELIX 268..272
FT /evidence="ECO:0007829|PDB:4P0G"
FT HELIX 274..286
FT /evidence="ECO:0007829|PDB:4P0G"
FT HELIX 288..302
FT /evidence="ECO:0007829|PDB:4P0G"
FT HELIX 306..317
FT /evidence="ECO:0007829|PDB:4P0G"
FT STRAND 326..328
FT /evidence="ECO:0007829|PDB:4P11"
FT TURN 331..334
FT /evidence="ECO:0007829|PDB:4P0G"
FT HELIX 337..343
FT /evidence="ECO:0007829|PDB:4P0G"
FT HELIX 351..368
FT /evidence="ECO:0007829|PDB:4P0G"
FT HELIX 377..388
FT /evidence="ECO:0007829|PDB:4P0G"
FT HELIX 390..402
FT /evidence="ECO:0007829|PDB:4P0G"
FT HELIX 410..416
FT /evidence="ECO:0007829|PDB:4P0G"
FT HELIX 417..421
FT /evidence="ECO:0007829|PDB:4P0G"
FT HELIX 423..426
FT /evidence="ECO:0007829|PDB:4P0G"
FT STRAND 429..431
FT /evidence="ECO:0007829|PDB:4P0G"
FT HELIX 436..454
FT /evidence="ECO:0007829|PDB:4P0G"
SQ SEQUENCE 490 AA; 55227 MW; 191CB459DBB67121 CRC64;
MFALTAYRLR CAAWLLATGI FLLLAGCSEA KAPTALERVQ KEGVLRVITR NSPATYFQDR
NGETGFEYEL AKRFAERLGV ELKIETADNL DDLYAQLSRE GGPALAAAGL TPGREDDASV
RYSHTYLDVT PQIIYRNGQQ RPTRPEDLVG KRIMVLKGSS HAEQLAELKK QYPELKYEES
DAVEVVDLLR MVDVGDIDLT LVDSNELAMN QVYFPNVRVA FDFGEARGLA WALPGGDDDS
LMNEVNAFLD QAKKEGLLQR LKDRYYGHVD VLGYVGAYTF AQHLQQRLPR YESHFKQSGK
QLDTDWRLLA AIGYQESLWQ PGATSKTGVR GLMMLTNRTA QAMGVSNRLD PKQSIQGGSK
YFVQIRSELP ESIKEPDRSW FALAAYNIGG AHLEDARKMA EKEGLNPNKW LDVKKMLPRL
AQKQWYAKTR YGYARGGETV HFVQNVRRYY DILTWVTQPQ MEGSQIAESG LHLPGVNKTR
PEEDSGDEKL
