ID A0A167TM09_9BACI Unreviewed; 364 AA.
AC A0A167TM09;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
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 ORFNames=GFC30_2801 {ECO:0000313|EMBL:ANB61410.1};
OS Anoxybacillus amylolyticus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Anoxybacillus.
OX NCBI_TaxID=294699 {ECO:0000313|EMBL:ANB61410.1, ECO:0000313|Proteomes:UP000076865};
RN [1] {ECO:0000313|EMBL:ANB61410.1, ECO:0000313|Proteomes:UP000076865}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15939 {ECO:0000313|EMBL:ANB61410.1,
RC ECO:0000313|Proteomes:UP000076865};
RX PubMed=16682297; DOI=10.1016/j.syapm.2005.10.003;
RA Poli A., Esposito E., Lama L., Orlando P., Nicolaus G., de Appolonia F.,
RA Gambacorta A., Nicolaus B.;
RT "Anoxybacillus amylolyticus sp. nov., a thermophilic amylase producing
RT bacterium isolated from Mount Rittmann (Antarctica).";
RL Syst. Appl. Microbiol. 29:300-307(2006).
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; CP015438; ANB61410.1; -; Genomic_DNA.
DR RefSeq; WP_066326384.1; NZ_CP015438.1.
DR AlphaFoldDB; A0A167TM09; -.
DR KEGG; aamy:GFC30_2801; -.
DR PATRIC; fig|294699.3.peg.2886; -.
DR OrthoDB; 9814591at2; -.
DR Proteomes; UP000076865; 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 Reference proteome {ECO:0000313|Proteomes:UP000076865};
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 18..40
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
FT SITE 249
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 364 AA; 41089 MW; 1C29027B9338E10F CRC64;
MEQNGLFPKD IQLVRKTVFI VSAVIIFLVV ATAIGSYVYI ESALKPVDPT DKRPVAISIP
IGSTVSDIAT TLEKKGIIKS AAVFRYYVKF KNHANFQAGN YKLTKAMTLP QIIDSLKKGK
VMEEIKVKIT IPEGKNLEDI ATIISQKTGY TKEEVMHQLN DRAYIQTLIK KYPMVLSNDV
LNKNIRYPLE GYLFPATYSF AEEKPPLSSI IEAMVEKTVE VVGKYEQEME EKNFTPHRLL
TIASLIEAEA TEKADRKKIA SVFYNRLHIG MPLQTDPTIL YALGTHKERV YYEDLKVNSP
YNTYIHKGLP PGPIASPGEM SIQAALEPDQ TKYLYFLATP EGDVIFTNTL EEHNREKAKY
IGKQ
//
