MLTC_ECOLI
ID MLTC_ECOLI Reviewed; 359 AA.
AC P0C066; P52066; P71274; P76651; P76652; Q2M9N0;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Membrane-bound lytic murein transglycosylase C {ECO:0000255|HAMAP-Rule:MF_01616};
DE EC=4.2.2.n1 {ECO:0000255|HAMAP-Rule:MF_01616};
DE AltName: Full=Murein lyase C {ECO:0000255|HAMAP-Rule:MF_01616};
DE Flags: Precursor;
GN Name=mltC {ECO:0000255|HAMAP-Rule:MF_01616}; Synonyms=yggZ;
GN OrderedLocusNames=b2963, JW5481;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 162-200, AND IDENTIFICATION.
RC STRAIN=122-1;
RX PubMed=9158737; DOI=10.1089/mdr.1996.2.141;
RA Dijkstra A.J., Keck W.;
RT "Identification of new members of the lytic transglycosylase family in
RT Haemophilus influenzae and Escherichia coli.";
RL Microb. Drug Resist. 2:141-145(1996).
RN [4]
RP INDUCTION.
RC STRAIN=K12 / GC4468;
RX PubMed=14594836; DOI=10.1128/jb.185.22.6624-6632.2003;
RA Pomposiello P.J., Koutsolioutsou A., Carrasco D., Demple B.;
RT "SoxRS-regulated expression and genetic analysis of the yggX gene of
RT Escherichia coli.";
RL J. Bacteriol. 185:6624-6632(2003).
CC -!- FUNCTION: Murein-degrading enzyme. May play a role in recycling of
CC muropeptides during cell elongation and/or cell division.
CC {ECO:0000255|HAMAP-Rule:MF_01616}.
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_01616};
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}.
CC -!- INDUCTION: By SoxS. {ECO:0000269|PubMed:14594836}.
CC -!- SIMILARITY: Belongs to the transglycosylase Slt family.
CC {ECO:0000255|HAMAP-Rule:MF_01616}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA69130.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAA69130.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAA69131.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U28377; AAA69130.1; ALT_SEQ; Genomic_DNA.
DR EMBL; U28377; AAA69131.1; ALT_FRAME; Genomic_DNA.
DR EMBL; U00096; AAC76000.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE77026.1; -; Genomic_DNA.
DR EMBL; U59902; AAC44296.1; -; Genomic_DNA.
DR PIR; B65082; B65082.
DR RefSeq; NP_417438.2; NC_000913.3.
DR RefSeq; WP_000760323.1; NZ_STEB01000001.1.
DR PDB; 4C5F; X-ray; 2.34 A; A/B=20-359.
DR PDB; 4CFO; X-ray; 2.90 A; A/B=20-359.
DR PDB; 4CFP; X-ray; 2.15 A; A/B=20-359.
DR PDB; 4CHX; X-ray; 2.45 A; A/B=20-359.
DR PDBsum; 4C5F; -.
DR PDBsum; 4CFO; -.
DR PDBsum; 4CFP; -.
DR PDBsum; 4CHX; -.
DR AlphaFoldDB; P0C066; -.
DR SMR; P0C066; -.
DR BioGRID; 4262361; 452.
DR STRING; 511145.b2963; -.
DR CAZy; GH23; Glycoside Hydrolase Family 23.
DR jPOST; P0C066; -.
DR PaxDb; P0C066; -.
DR PRIDE; P0C066; -.
DR EnsemblBacteria; AAC76000; AAC76000; b2963.
DR EnsemblBacteria; BAE77026; BAE77026; BAE77026.
DR GeneID; 60901734; -.
DR GeneID; 945428; -.
DR KEGG; ecj:JW5481; -.
DR KEGG; eco:b2963; -.
DR PATRIC; fig|1411691.4.peg.3768; -.
DR EchoBASE; EB2810; -.
DR eggNOG; COG0741; Bacteria.
DR HOGENOM; CLU_044583_0_0_6; -.
DR OMA; AIMQIES; -.
DR PhylomeDB; P0C066; -.
DR BioCyc; EcoCyc:G7533-MON; -.
DR BioCyc; MetaCyc:G7533-MON; -.
DR PRO; PR:P0C066; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0031225; C:anchored component of membrane; ISM:EcoCyc.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; TAS:EcoCyc.
DR GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:InterPro.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0008932; F:lytic endotransglycosylase activity; IDA:EcoCyc.
DR GO; GO:0008933; F:lytic transglycosylase activity; IDA:EcoCyc.
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:0034599; P:cellular response to oxidative stress; IEP:EcoCyc.
DR GO; GO:0009253; P:peptidoglycan catabolic process; IDA:EcoCyc.
DR HAMAP; MF_01616; MltC; 1.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR023664; Murein_transglycosylaseC.
DR InterPro; IPR024570; Murein_transglycosylaseC_N.
DR InterPro; IPR000189; Transglyc_AS.
DR InterPro; IPR008258; Transglycosylase_SLT_dom_1.
DR Pfam; PF11873; Mltc_N; 1.
DR Pfam; PF01464; SLT; 1.
DR SUPFAM; SSF53955; SSF53955; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS00922; TRANSGLYCOSYLASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell outer membrane; Cell wall biogenesis/degradation;
KW Lipoprotein; Lyase; Membrane; Palmitate; Reference proteome; Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01616"
FT CHAIN 17..359
FT /note="Membrane-bound lytic murein transglycosylase C"
FT /id="PRO_0000032785"
FT LIPID 17
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01616"
FT LIPID 17
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01616"
FT HELIX 36..52
FT /evidence="ECO:0007829|PDB:4CFP"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:4CFP"
FT STRAND 62..69
FT /evidence="ECO:0007829|PDB:4CFP"
FT TURN 70..73
FT /evidence="ECO:0007829|PDB:4CFP"
FT STRAND 74..79
FT /evidence="ECO:0007829|PDB:4CFP"
FT TURN 80..83
FT /evidence="ECO:0007829|PDB:4CFP"
FT STRAND 84..89
FT /evidence="ECO:0007829|PDB:4CFP"
FT HELIX 95..108
FT /evidence="ECO:0007829|PDB:4CFP"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:4CFP"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:4CFO"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:4CFO"
FT STRAND 140..142
FT /evidence="ECO:0007829|PDB:4CFO"
FT HELIX 148..161
FT /evidence="ECO:0007829|PDB:4CFP"
FT STRAND 164..167
FT /evidence="ECO:0007829|PDB:4CFP"
FT STRAND 169..179
FT /evidence="ECO:0007829|PDB:4CFP"
FT HELIX 184..190
FT /evidence="ECO:0007829|PDB:4CFP"
FT HELIX 193..203
FT /evidence="ECO:0007829|PDB:4CFP"
FT HELIX 207..218
FT /evidence="ECO:0007829|PDB:4CFP"
FT TURN 232..235
FT /evidence="ECO:0007829|PDB:4CFP"
FT TURN 238..240
FT /evidence="ECO:0007829|PDB:4CFP"
FT HELIX 241..247
FT /evidence="ECO:0007829|PDB:4CFP"
FT TURN 248..250
FT /evidence="ECO:0007829|PDB:4CFP"
FT HELIX 257..260
FT /evidence="ECO:0007829|PDB:4CFP"
FT HELIX 263..279
FT /evidence="ECO:0007829|PDB:4CFP"
FT TURN 280..284
FT /evidence="ECO:0007829|PDB:4CFP"
FT HELIX 288..301
FT /evidence="ECO:0007829|PDB:4CFP"
FT HELIX 303..307
FT /evidence="ECO:0007829|PDB:4CFP"
FT TURN 308..310
FT /evidence="ECO:0007829|PDB:4CFP"
FT HELIX 314..321
FT /evidence="ECO:0007829|PDB:4CFP"
FT HELIX 326..335
FT /evidence="ECO:0007829|PDB:4CFP"
FT HELIX 340..357
FT /evidence="ECO:0007829|PDB:4CFP"
SQ SEQUENCE 359 AA; 40113 MW; 618F0FCC9C41969C CRC64;
MKKYLALALI APLLISCSTT KKGDTYNEAW VKDTNGFDIL MGQFAHNIEN IWGFKEVVIA
GPKDYVKYTD QYQTRSHINF DDGTITIETI AGTEPAAHLR RAIIKTLLMG DDPSSVDLYS
DVDDITISKE PFLYGQVVDN TGQPIRWEGR ASNFADYLLK NRLKSRSNGL RIIYSVTINM
VPNHLDKRAH KYLGMVRQAS RKYGVDESLI LAIMQTESSF NPYAVSRSDA LGLMQVVQHT
AGKDVFRSQG KSGTPSRSFL FDPASNIDTG TAYLAMLNNV YLGGIDNPTS RRYAVITAYN
GGAGSVLRVF SNDKIQAANI INTMTPGDVY QTLTTRHPSA ESRRYLYKVN TAQKSYRRR
