MLTF_YERPE
ID MLTF_YERPE Reviewed; 486 AA.
AC Q74SQ6; Q8D0Z9;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 107.
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};
GN OrderedLocusNames=YPO2922, y1308, YP_2535;
OS Yersinia pestis.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=632;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CO-92 / Biovar Orientalis;
RX PubMed=11586360; DOI=10.1038/35097083;
RA Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L.,
RA Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M.,
RA Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T.,
RA Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S.,
RA Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J.,
RA Stevens K., Whitehead S., Barrell B.G.;
RT "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL Nature 413:523-527(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIM10+ / Biovar Mediaevalis;
RX PubMed=12142430; DOI=10.1128/jb.184.16.4601-4611.2002;
RA Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P.,
RA Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D.,
RA Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A.,
RA Nilles M.L., Matson J.S., Blattner F.R., Perry R.D.;
RT "Genome sequence of Yersinia pestis KIM.";
RL J. Bacteriol. 184:4601-4611(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=91001 / Biovar Mediaevalis;
RX PubMed=15368893; DOI=10.1093/dnares/11.3.179;
RA Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D.,
RA Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L.,
RA Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H.,
RA Wang J., Huang P., Yang R.;
RT "Complete genome sequence of Yersinia pestis strain 91001, an isolate
RT avirulent to humans.";
RL DNA Res. 11:179-197(2004).
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=AAM84882.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AL590842; CAL21530.1; -; Genomic_DNA.
DR EMBL; AE009952; AAM84882.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE017042; AAS62732.1; -; Genomic_DNA.
DR PIR; AG0355; AG0355.
DR RefSeq; WP_002211562.1; NZ_WUCL01000098.1.
DR RefSeq; YP_002347852.1; NC_003143.1.
DR PDB; 5UH0; X-ray; 1.95 A; A/B=35-274.
DR PDBsum; 5UH0; -.
DR AlphaFoldDB; Q74SQ6; -.
DR SMR; Q74SQ6; -.
DR IntAct; Q74SQ6; 1.
DR STRING; 214092.YPO2922; -.
DR PaxDb; Q74SQ6; -.
DR DNASU; 1146255; -.
DR EnsemblBacteria; AAM84882; AAM84882; y1308.
DR EnsemblBacteria; AAS62732; AAS62732; YP_2535.
DR GeneID; 57975876; -.
DR KEGG; ype:YPO2922; -.
DR KEGG; ypk:y1308; -.
DR KEGG; ypm:YP_2535; -.
DR PATRIC; fig|214092.21.peg.3373; -.
DR eggNOG; COG4623; Bacteria.
DR HOGENOM; CLU_027494_0_1_6; -.
DR OMA; YYDILTW; -.
DR Proteomes; UP000000815; Chromosome.
DR Proteomes; UP000001019; Chromosome.
DR Proteomes; UP000002490; 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..21
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02016"
FT CHAIN 22..486
FT /note="Membrane-bound lytic murein transglycosylase F"
FT /id="PRO_0000353999"
FT REGION 22..268
FT /note="Non-LT domain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02016"
FT REGION 269..486
FT /note="LT domain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02016"
FT ACT_SITE 313
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02016"
FT HELIX 35..42
FT /evidence="ECO:0007829|PDB:5UH0"
FT STRAND 44..50
FT /evidence="ECO:0007829|PDB:5UH0"
FT TURN 53..55
FT /evidence="ECO:0007829|PDB:5UH0"
FT STRAND 59..62
FT /evidence="ECO:0007829|PDB:5UH0"
FT HELIX 66..78
FT /evidence="ECO:0007829|PDB:5UH0"
FT STRAND 80..88
FT /evidence="ECO:0007829|PDB:5UH0"
FT HELIX 90..98
FT /evidence="ECO:0007829|PDB:5UH0"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:5UH0"
FT HELIX 113..117
FT /evidence="ECO:0007829|PDB:5UH0"
FT STRAND 119..128
FT /evidence="ECO:0007829|PDB:5UH0"
FT STRAND 130..135
FT /evidence="ECO:0007829|PDB:5UH0"
FT STRAND 151..154
FT /evidence="ECO:0007829|PDB:5UH0"
FT HELIX 158..168
FT /evidence="ECO:0007829|PDB:5UH0"
FT STRAND 176..181
FT /evidence="ECO:0007829|PDB:5UH0"
FT HELIX 184..192
FT /evidence="ECO:0007829|PDB:5UH0"
FT STRAND 195..202
FT /evidence="ECO:0007829|PDB:5UH0"
FT HELIX 203..210
FT /evidence="ECO:0007829|PDB:5UH0"
FT STRAND 216..221
FT /evidence="ECO:0007829|PDB:5UH0"
FT STRAND 226..233
FT /evidence="ECO:0007829|PDB:5UH0"
FT HELIX 239..253
FT /evidence="ECO:0007829|PDB:5UH0"
FT HELIX 256..263
FT /evidence="ECO:0007829|PDB:5UH0"
SQ SEQUENCE 486 AA; 54808 MW; 521B5821A8074D1A CRC64;
MTRIKLSYFT IGLVALLLAL ALWPNIPWRN GQEGQLDQIK ARGELRVSTI SSPLIYSTEK
DTPSGFDYEL AKRFADYLGV KLVIIPHHNI DDLFDALDND DTDLLAAGLI YNRERLNRAR
TGPAYYSVSQ QLVYRLGSPR PKSFSDLKGQ VVVASGSAHM TTLKRLKQTK YPELNWSSSV
DKSGKELLEQ VAEGKLDYTL GDSATIALLQ RIHPQLAVAF DVTDEEPVTW YFKQSDDDSL
YAAMLDFYSE MVEDGSLARL EEKYLGHVGS FDYVDTKTFL SAIDNVLPSY QHLFEKHAGD
IDWKLLAVIA YQESHWNPQA TSPTGVRGLM MLTRATADGL GVKDRVDPEE SIRGGAIYLQ
RLMKKLPETI PEDERIWFAL AAYNLGYGHM LDARRLTKNQ NGNPDSWVDV KMRLPMLSQK
RYYPSTTYGY ARGHEAYNYV ENIRRYQVSL VGYLQEKEKK AAQHAAIEAE LGKSNPVVGP
GWSIGD
