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Lantibiotic mutacin-2 (Lantibiotic mutacin H-29B) (Mutacin II)

 LANA_STRMG              Reviewed;          53 AA.
O54329; P84110;
27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
01-JUN-1998, sequence version 1.
22-NOV-2017, entry version 53.
RecName: Full=Lantibiotic mutacin-2;
AltName: Full=Lantibiotic mutacin H-29B;
AltName: Full=Mutacin II;
Flags: Precursor;
Name=mutA {ECO:0000312|EMBL:AAC38144.1};
Streptococcus mutans.
Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
Streptococcus.
NCBI_TaxID=1309;
[1] {ECO:0000312|EMBL:AAC38144.1}
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=T8 {ECO:0000312|EMBL:AAC38144.1};
PubMed=9461412; DOI=10.1016/S0378-1119(97)00578-7;
Woodruff W.A., Novak J., Caufield P.W.;
"Sequence analysis of mutA and mutM genes involved in the biosynthesis
of the lantibiotic mutacin II in Streptococcus mutans.";
Gene 206:37-43(1998).
[2] {ECO:0000305}
PROTEIN SEQUENCE OF 27-50, DEHYDRATION AT THR-51, LANTHIONINE
CROSS-LINKS, AND MUTAGENESIS OF CYS-41 AND CYS-52.
STRAIN=T8 {ECO:0000269|PubMed:10821848};
PubMed=10821848; DOI=10.1074/jbc.275.21.15845;
Krull R.E., Chen P., Novak J., Kirk M., Barnes S., Baker J.,
Krishna N.R., Caufield P.W.;
"Biochemical structural analysis of the lantibiotic mutacin II.";
J. Biol. Chem. 275:15845-15850(2000).
[3]
PROTEIN SEQUENCE OF 27-50, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES,
MASS SPECTROMETRY, AND POST-TRANSLATIONAL MODIFICATIONS.
STRAIN=29B;
PubMed=16626493; DOI=10.1186/1471-2180-6-36;
Nicolas G., Morency H., LaPointe G., Lavoie M.C.;
"Mutacin H-29B is identical to mutacin II (J-T8).";
BMC Microbiol. 6:36-36(2006).
[4] {ECO:0000305}
PROTEIN SEQUENCE OF 27-37, POST-TRANSLATIONAL MODIFICATIONS, AND
MUTAGENESIS OF ASN-27; VAL-33; PRO-35; THR-36; CYS-41; CYS-52 AND
CYS-53.
STRAIN=T8 {ECO:0000269|PubMed:9647795};
PubMed=9647795;
Chen P., Novak J., Kirk M., Barnes S., Qi F., Caufield P.W.;
"Structure-activity study of the lantibiotic mutacin II from
Streptococcus mutans T8 by a gene replacement strategy.";
Appl. Environ. Microbiol. 64:2335-2340(1998).
[5] {ECO:0000305}
PROTEIN SEQUENCE OF 27-34, FUNCTION, POST-TRANSLATIONAL MODIFICATIONS,
MASS SPECTROMETRY, AND BIOPHYSICOCHEMICAL PROPERTIES.
STRAIN=T8 {ECO:0000269|PubMed:8021218};
PubMed=8021218; DOI=10.1128/jb.176.14.4316-4320.1994;
Novak J., Caufield P.W., Miller E.J.;
"Isolation and biochemical characterization of a novel lantibiotic
mutacin from Streptococcus mutans.";
J. Bacteriol. 176:4316-4320(1994).
[6] {ECO:0000305}
FUNCTION.
STRAIN=T8 {ECO:0000269|PubMed:8592997};
PubMed=8592997; DOI=10.1128/AAC.39.12.2656;
Chikindas M.L., Novak J., Driessen A.J.M., Konings W.N.,
Schilling K.M., Caufield P.W.;
"Mutacin II, a bactericidal lantibiotic from Streptococcus mutans.";
Antimicrob. Agents Chemother. 39:2656-2660(1995).
[7] {ECO:0000305}
POST-TRANSLATIONAL MODIFICATIONS, AND MASS SPECTROMETRY.
STRAIN=T8 {ECO:0000269|PubMed:8660519};
PubMed=8660519; DOI=10.1006/abio.1996.0181;
Novak J., Kirk M., Caufield P.W., Barnes S., Morrison K., Baker J.;
"Detection of modified amino acids in lantibiotic peptide mutacin II
by chemical derivation and electrospray ionization-mass spectroscopic
analysis.";
Anal. Biochem. 236:358-360(1996).
[8] {ECO:0000305}
MUTAGENESIS OF GLU-14; VAL-15; SER-16; GLU-19; LEU-20; ILE-23; GLY-25
AND GLY-26.
STRAIN=T8 {ECO:0000269|PubMed:11179642};
PubMed=11179642; DOI=10.1111/j.1574-6968.2001.tb10511.x;
Chen P., Qi F., Novak J., Krull R.E., Caufield P.W.;
"Effect of amino acid substitutions in conserved residues in the
leader peptide on biosynthesis of the lantibiotic mutacin II.";
FEMS Microbiol. Lett. 195:139-144(2001).
-!- FUNCTION: Lanthionine-containing peptide antibiotic (lantibiotic)
active on Gram-positive bacteria including M.luteus, S.aureus,
Streptococcus, P.micros, P.acidilactici, C.sporogenes,
C.diphtheriae, A.viscosus, G.vaginalis, P.acnes, L.monocytogenes
and M.smegmatis, and Gram-negative bacteria including C.jejuni,
H.pylori and N.gonorrhoeae. Transiently and partially depolarizes
the transmembrane electrical potential and pH gradient of
susceptible cells, inhibits the uptake of amino acids and depletes
the intracellular ATP pool. {ECO:0000269|PubMed:16626493,
ECO:0000269|PubMed:8021218, ECO:0000269|PubMed:8592997}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Stable from pH 2.0 to 4.0. Activity decreases gradually with
increasing pH. {ECO:0000269|PubMed:16626493,
ECO:0000269|PubMed:8021218};
Temperature dependence:
Thermostable. {ECO:0000269|PubMed:16626493,
ECO:0000269|PubMed:8021218};
-!- PTM: Maturation of lantibiotics involves the enzymic conversion of
Thr, and Ser into dehydrated AA and the formation of thioether
bonds with cysteine. This is followed by membrane translocation
and cleavage of the modified precursor. {ECO:0000305}.
-!- PTM: It is not established whether the 2,3-didehydrobutyrine is
the E- or Z-isomer (PubMed:10821848, PubMed:16626493,
PubMed:9647795, PubMed:8021218 and PubMed:8660519).
-!- MASS SPECTROMETRY: Mass=3244.64; Mass_error=1.15;
Method=Electrospray; Range=27-53;
Evidence={ECO:0000269|PubMed:8021218};
-!- MASS SPECTROMETRY: Mass=3245.4; Mass_error=0.58;
Method=Electrospray; Range=27-53;
Evidence={ECO:0000269|PubMed:8660519};
-!- MASS SPECTROMETRY: Mass=3246.08; Mass_error=0.1; Method=MALDI;
Range=27-53; Evidence={ECO:0000269|PubMed:16626493};
-!- SIMILARITY: Belongs to the type A lantibiotic family.
{ECO:0000255}.
-----------------------------------------------------------------------
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EMBL; U40620; AAC38144.1; -; Genomic_DNA.
PIR; JC6526; JC6526.
PMAP-CutDB; O54329; -.
GO; GO:0005576; C:extracellular region; IC:UniProtKB.
GO; GO:0005102; F:receptor binding; IEA:UniProtKB-KW.
GO; GO:0006865; P:amino acid transport; IDA:UniProtKB.
GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:UniProtKB.
GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
GO; GO:0042391; P:regulation of membrane potential; IDA:UniProtKB.
InterPro; IPR007682; Lantibiotic_typ-A_Lactobact.
Pfam; PF04604; L_biotic_typeA; 1.
1: Evidence at protein level;
Antibiotic; Antimicrobial; Bacteriocin; Direct protein sequencing;
Lantibiotic; Thioether bond.
PROPEP 1 26 {ECO:0000269|PubMed:10821848,
ECO:0000269|PubMed:16626493,
ECO:0000269|PubMed:8021218,
ECO:0000269|PubMed:9647795}.
/FTId=PRO_0000017128.
PEPTIDE 27 53 Lantibiotic mutacin-2.
/FTId=PRO_0000017129.
MOD_RES 51 51 2,3-didehydrobutyrine.
{ECO:0000269|PubMed:10821848}.
CROSSLNK 36 41 Beta-methyllanthionine (Thr-Cys).
{ECO:0000269|PubMed:10821848}.
CROSSLNK 38 52 Lanthionine (Ser-Cys).
{ECO:0000269|PubMed:10821848}.
CROSSLNK 45 53 Lanthionine (Ser-Cys).
{ECO:0000269|PubMed:10821848}.
MUTAGEN 14 14 E->D: No loss of activity or protein
production.
{ECO:0000269|PubMed:11179642}.
MUTAGEN 14 14 E->K: Reduced protein production to about
10% of wild-type level.
{ECO:0000269|PubMed:11179642}.
MUTAGEN 15 15 V->I,A: No loss of activity or protein
production.
{ECO:0000269|PubMed:11179642}.
MUTAGEN 15 15 V->L: Reduced protein production to about
50% of wild-type level.
{ECO:0000269|PubMed:11179642}.
MUTAGEN 16 16 S->T,A: No loss of activity or protein
production.
{ECO:0000269|PubMed:11179642}.
MUTAGEN 19 19 E->D: No loss of activity or protein
production.
{ECO:0000269|PubMed:11179642}.
MUTAGEN 19 19 E->K: Reduced protein production to about
75% of wild-type level.
{ECO:0000269|PubMed:11179642}.
MUTAGEN 20 20 L->K: No mature protein is produced.
{ECO:0000269|PubMed:11179642}.
MUTAGEN 20 20 L->M: No loss of activity or protein
production.
{ECO:0000269|PubMed:11179642}.
MUTAGEN 23 23 I->D: No mature protein is produced.
{ECO:0000269|PubMed:11179642}.
MUTAGEN 23 23 I->V: No loss of activity or protein
production.
{ECO:0000269|PubMed:11179642}.
MUTAGEN 25 25 G->A: No mature protein is produced.
{ECO:0000269|PubMed:11179642}.
MUTAGEN 26 26 G->A: No mature protein is produced.
{ECO:0000269|PubMed:11179642}.
MUTAGEN 27 27 Missing: No protein is secreted.
{ECO:0000269|PubMed:9647795}.
MUTAGEN 33 33 V->A: No loss of activity.
{ECO:0000269|PubMed:9647795}.
MUTAGEN 35 35 P->A: Low activity, less than 10% of
wild-type. {ECO:0000269|PubMed:9647795}.
MUTAGEN 36 36 T->A: Loss of secretion.
{ECO:0000269|PubMed:9647795}.
MUTAGEN 36 36 T->S: No loss of activity.
{ECO:0000269|PubMed:9647795}.
MUTAGEN 41 41 C->A: Loss of activity.
{ECO:0000269|PubMed:10821848,
ECO:0000269|PubMed:9647795}.
MUTAGEN 52 52 C->A: Loss of activity.
{ECO:0000269|PubMed:10821848,
ECO:0000269|PubMed:9647795}.
MUTAGEN 53 53 C->A: Low activity, less than 10% of
wild-type level.
{ECO:0000269|PubMed:9647795}.
SEQUENCE 53 AA; 6020 MW; 6C3788E2C9EC6525 CRC64;
MNKLNSNAVV SLNEVSDSEL DTILGGNRWW QGVVPTVSYE CRMNSWQHVF TCC


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