ID D1NSB0_9BIFI Unreviewed; 355 AA.
AC D1NSB0;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 24-JAN-2024, entry version 43.
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=BIFGAL_02666 {ECO:0000313|EMBL:EFA23562.1};
OS Bifidobacterium gallicum DSM 20093 = LMG 11596.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=561180 {ECO:0000313|EMBL:EFA23562.1, ECO:0000313|Proteomes:UP000003656};
RN [1] {ECO:0000313|EMBL:EFA23562.1, ECO:0000313|Proteomes:UP000003656}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20093 {ECO:0000313|EMBL:EFA23562.1,
RC ECO:0000313|Proteomes:UP000003656};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EFA23562.1}.
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DR EMBL; ABXB03000001; EFA23562.1; -; Genomic_DNA.
DR AlphaFoldDB; D1NSB0; -.
DR STRING; 561180.BIFGAL_02666; -.
DR eggNOG; COG1559; Bacteria.
DR Proteomes; UP000003656; Unassembled WGS sequence.
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 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 233
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 355 AA; 38355 MW; CE62BDC93EF677BD CRC64;
MRARRKARQR HRIVAIVVSI AVLALLVVGG IVAVKALKNW QSGQTNQAVV DDYPGPGTSD
VQFSVETGQG ADQIAQNLVD AGIIKSAAAF TSVVAANHLT LYPGTFPMKL QMKASDAATI
LSNQGNAAGF LEVRPGERDT DVIANAAKVS GIPQEEFQKI LDNKGSGILP AEANGSFEGW
LEPGSYDVAK ENDATQILRT MVEARIAKLD ELGVPQGQER ERLLIIASIA EAEVNLPEYY
GKVTRVIDNR LAKDMTLGMD STVAYGLHTT GNMLTNEQLA DASNPYNTRV NKGLPPTPIS
NPGDNAIQAA LHPEDGDWLY FVTVNLKTGE TKFTDNDEQF QQYVQEYKTN NPDAS
//
