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Database: UniProt
Entry: D5WXF7_KYRT2
LinkDB: D5WXF7_KYRT2
Original site: D5WXF7_KYRT2 
ID   D5WXF7_KYRT2            Unreviewed;       344 AA.
AC   D5WXF7;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   RecName: Full=Endolytic murein transglycosylase {ECO:0000256|HAMAP-Rule:MF_02065};
DE            EC=4.2.2.- {ECO:0000256|HAMAP-Rule:MF_02065};
DE   AltName: Full=Peptidoglycan polymerization terminase {ECO:0000256|HAMAP-Rule:MF_02065};
GN   Name=mltG {ECO:0000256|HAMAP-Rule:MF_02065};
GN   OrderedLocusNames=Btus_1142 {ECO:0000313|EMBL:ADG05878.1};
OS   Kyrpidia tusciae (strain DSM 2912 / NBRC 15312 / T2) (Bacillus tusciae).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Alicyclobacillaceae; Kyrpidia.
OX   NCBI_TaxID=562970 {ECO:0000313|EMBL:ADG05878.1, ECO:0000313|Proteomes:UP000002368};
RN   [1] {ECO:0000313|Proteomes:UP000002368}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2912 / NBRC 15312 / T2 {ECO:0000313|Proteomes:UP000002368};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA   Ovchinnikova G., Chertkov O., Brettin T., Detter J.C., Han C., Larimer F.,
RA   Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T.,
RA   Wu D., Pukall R., Schneider S., Wahrenburg C., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Bacillus tusciae DSM 2912.";
RL   Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADG05878.1, ECO:0000313|Proteomes:UP000002368}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2912 / NBRC 15312 / T2 {ECO:0000313|Proteomes:UP000002368};
RX   PubMed=22180816; DOI=10.4056/sigs.2144922;
RA   Klenk H.P., Lapidus A., Chertkov O., Copeland A., Del Rio T.G., Nolan M.,
RA   Lucas S., Chen F., Tice H., Cheng J.F., Han C., Bruce D., Goodwin L.,
RA   Pitluck S., Pati A., Ivanova N., Mavromatis K., Daum C., Chen A.,
RA   Palaniappan K., Chang Y.J., Land M., Hauser L., Jeffries C.D., Detter J.C.,
RA   Rohde M., Abt B., Pukall R., Goker M., Bristow J., Markowitz V.,
RA   Hugenholtz P., Eisen J.A.;
RT   "Complete genome sequence of the thermophilic, hydrogen-oxidizing Bacillus
RT   tusciae type strain (T2) and reclassification in the new genus, Kyrpidia
RT   gen. nov. as Kyrpidia tusciae comb. nov. and emendation of the family
RT   Alicyclobacillaceae da Costa and Rainey, 2010.";
RL   Stand. Genomic Sci. 5:121-134(2011).
CC   -!- FUNCTION: Functions as a peptidoglycan terminase that cleaves nascent
CC       peptidoglycan strands endolytically to terminate their elongation.
CC       {ECO:0000256|HAMAP-Rule:MF_02065}.
CC   -!- SIMILARITY: Belongs to the transglycosylase MltG family.
CC       {ECO:0000256|HAMAP-Rule:MF_02065}.
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DR   EMBL; CP002017; ADG05878.1; -; Genomic_DNA.
DR   AlphaFoldDB; D5WXF7; -.
DR   STRING; 562970.Btus_1142; -.
DR   KEGG; bts:Btus_1142; -.
DR   eggNOG; COG1559; Bacteria.
DR   HOGENOM; CLU_025574_2_1_9; -.
DR   Proteomes; UP000002368; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0008932; F:lytic endotransglycosylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd08010; MltG_like; 1.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR   Gene3D; 3.30.1490.480; Endolytic murein transglycosylase; 1.
DR   HAMAP; MF_02065; MltG; 1.
DR   InterPro; IPR003770; MLTG-like.
DR   NCBIfam; TIGR00247; endolytic transglycosylase MltG; 1.
DR   PANTHER; PTHR30518:SF2; ENDOLYTIC MUREIN TRANSGLYCOSYLASE; 1.
DR   PANTHER; PTHR30518; UNCHARACTERIZED; 1.
DR   Pfam; PF02618; YceG; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW   Rule:MF_02065};
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316,
KW   ECO:0000256|HAMAP-Rule:MF_02065};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_02065};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_02065};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW   Rule:MF_02065};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW   Rule:MF_02065}.
FT   SITE            225
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ   SEQUENCE   344 AA;  37507 MW;  AC842689E67413CA CRC64;
     MIRPAVKKAL AAAVAGLIIA AGVGGWAWFR PTAAGAPVVV VIRPGSSVSD IADELQRAGL
     VRHASAFQVY VWGRRLAPQL KAGRYQFVPG TSIPTLAWAI AEGKVSPDTV RVTIPEGFTV
     EKIADLLQAQ GVCSKAEFLR EVDHGQFNGA ILASIPKGAP MQHRLEGYLF PDTYFWEKHS
     PAHQVIQDMI DNLAAHIPQD WIRTAEARGE SWHAVMTVAS MVEREAKVPA ERPQIAGVIY
     NRLRSRPPMP LQVDATVEYA VGYKPVLTYQ DLEVDSPFNT YIHIGLPPGP IANPGLDSIR
     AAVFPATNDY YYYVAKGDGS GAHYFARTYA EHLQNEEKAQ GSSP
//
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