ID A0A1V4EXR6_9BACL Unreviewed; 348 AA.
AC A0A1V4EXR6;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
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=B2M26_01520 {ECO:0000313|EMBL:OPG17438.1};
OS Ferroacidibacillus organovorans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Alicyclobacillaceae;
OC Ferroacidibacillus.
OX NCBI_TaxID=1765683 {ECO:0000313|EMBL:OPG17438.1, ECO:0000313|Proteomes:UP000190229};
RN [1] {ECO:0000313|EMBL:OPG17438.1, ECO:0000313|Proteomes:UP000190229}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Huett2 {ECO:0000313|EMBL:OPG17438.1,
RC ECO:0000313|Proteomes:UP000190229};
RA Schopf S.;
RT "Draft genome of Acidibacillus ferrooxidans Huett2.";
RL Submitted (FEB-2017) 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:OPG17438.1}.
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DR EMBL; MWPS01000003; OPG17438.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V4EXR6; -.
DR Proteomes; UP000190229; 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 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:UP000190229};
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 227
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 348 AA; 38966 MW; C676650E4A6E4EB3 CRC64;
MKPRMRRRGG LSLLVAFALF WGGISSYQAI YLPGNVAKTT WINIPAGATS TQIADILYRS
RVIRSPFWFR VYLSLSGQAD RLQAGRYPFS PKQNVPSVVN ELTRGSVAYN TVTVTFPEGY
TVTQMAATLQ RSGVCSSRSF MHAVKADHFS YAFLATSYRR SSVRDPLEGF LFPNTYDFVR
GESPRTVIQT MLQMTQQVLD PYRLREIARE GLTVQEVMTV ASMIEREAKL KVERPLVASV
IYNRLHLHPP MKLQIDATVL YALNGHGSLN NDLYINNPYN TYVYGGLPPG PIANPGLASI
QAALHPAKTD YYFYVARNDG SGGHYFSTTY AQQLRNEVKS QQNAARHG
//
