ID B1HUJ8_LYSSC Unreviewed; 381 AA.
AC B1HUJ8;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 79.
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=Bsph_3867 {ECO:0000313|EMBL:ACA41343.1};
OS Lysinibacillus sphaericus (strain C3-41).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX NCBI_TaxID=444177 {ECO:0000313|EMBL:ACA41343.1, ECO:0000313|Proteomes:UP000002164};
RN [1] {ECO:0000313|EMBL:ACA41343.1, ECO:0000313|Proteomes:UP000002164}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C3-41 {ECO:0000313|EMBL:ACA41343.1,
RC ECO:0000313|Proteomes:UP000002164};
RX PubMed=18296527; DOI=10.1128/JB.01652-07;
RA Hu X., Fan W., Han B., Liu H., Zheng D., Li Q., Dong W., Yan J., Gao M.,
RA Berry C., Yuan Z.;
RT "Complete genome sequence of the mosquitocidal bacterium Bacillus
RT sphaericus C3-41 and comparison with those of closely related Bacillus
RT species.";
RL J. Bacteriol. 190:2892-2902(2008).
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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_02065};
CC Single-pass membrane protein {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; CP000817; ACA41343.1; -; Genomic_DNA.
DR AlphaFoldDB; B1HUJ8; -.
DR EnsemblBacteria; ACA41343; ACA41343; Bsph_3867.
DR KEGG; lsp:Bsph_3867; -.
DR HOGENOM; CLU_025574_2_3_9; -.
DR Proteomes; UP000002164; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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 TRANSMEM 33..56
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
FT SITE 265
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 381 AA; 42975 MW; 5BC0F6C047C51591 CRC64;
MIGGKPVNNG TKKQEMFSKM QEKKSEVKIV RKIVAIVAIV FVLVIGIVGL FGYNYVKGAL
KPLDPDATKT IAVEVPIGSS LSSISTLLEK KGVIKDARVF KYYAKFKNES QFQAGNYDLT
QAMTFDELIE SLKTGKVYRK PVFTMTIPEG LTIEQIGKVI EKKTPYSQKE FMDLVTSDTF
VQQMMANYPE LVTDAVLAEN IRYDLEGYLY PATYSYYEEK PSLEAIVEEM IAAMNKVVKN
YSDVLVEKQM SVHQLLTFAS LLEEEATAQT DRETIASVFY NRIDEGMPLQ TDPTVLYALG
DHKDRVLYED LEVDNAYNTY KNKGLPPGPI AGAGKTSIEA TLNPSQTDYF YFLADKEGVN
HFSKTYDEHL QKIAKYLQKE E
//
